|
Name |
Accession |
Description |
Interval |
E-value |
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-489 |
1.01e-73 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 241.89 E-value: 1.01e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 6 VSNLTFGYEGSPelIFDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQGEY-PYSGTISAS--VEFEYFPYEV-ANLSRTG 81
Cdd:COG0488 1 LENLSKSFGGRP--LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELePDSGEVSIPkgLRIGYLPQEPpLDDDLTV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 82 LEVVREIAPE----------------------------------AEDWEIQRE----LGLLDLAERSLELPFSSLSNGER 123
Cdd:COG0488 79 LDTVLDGDAElraleaeleeleaklaepdedlerlaelqeefeaLGGWEAEARaeeiLSGLGFPEEDLDRPVSELSGGWR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 124 TKVLLAAMFLKENAFLLIDEPTNHLDLEGRRKLGSYLARKRG-FLLVSHDRAFLDQCVDHILAINRTNIEIQRGNFSSWW 202
Cdd:COG0488 159 RRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGtVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAYL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 203 ENRRRQDAFELARQEKLQKDIGRLTESARRASgwsdrtekskfgvdktgAKAAdrgfvghKAAKLMQRSKSIQR-RREEA 281
Cdd:COG0488 239 EQRAERLEQEAAAYAKQQKKIAKEEEFIRRFR-----------------AKAR-------KAKQAQSRIKALEKlEREEP 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 282 VEEKKQLlqNLERQEALavtplpcRAGARLAEFRDVAVCYDGRTVCREITFEVLAGERIALQGANGC-----------GK 350
Cdd:COG0488 295 PRRDKTV--EIRFPPPE-------RLGKKVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAgkstllkllagEL 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 351 SsllklllgeeiPHSGTVETMSGLVVSYVSQNTDHLRGSLT---EFART-QGLDGSRFRTILRKLDVPREQFEKDLADYS 426
Cdd:COG0488 366 E-----------PDSGTVKLGETVKIGYFDQHQEELDPDKTvldELRDGaPGGTEQEVRGYLGRFLFSGDDAFKPVGVLS 434
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2468763893 427 SGQKKKVLLAASLCTQAHLYVWDEPLNFIDVISRMQVEDLLLACRPTLLFVEHDARFCDEIAT 489
Cdd:COG0488 435 GGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRVAT 497
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-188 |
4.09e-44 |
|
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: 152.22 E-value: 4.09e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 4 IDVSNLTFGYEGSPelIFDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQGEY-PYSGTI--SASVEFEYFPyevanlsrt 80
Cdd:cd03221 1 IELENLSKTYGGKL--LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELePDEGIVtwGSTVKIGYFE--------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 81 glevvreiapeaedweiQrelglldlaerslelpfssLSNGERTKVLLAAMFLKENAFLLIDEPTNHLDLEGRRKLGSYL 160
Cdd:cd03221 70 -----------------Q-------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEAL 113
|
170 180
....*....|....*....|....*....
gi 2468763893 161 ARKRG-FLLVSHDRAFLDQCVDHILAINR 188
Cdd:cd03221 114 KEYPGtVILVSHDRYFLDQVATKIIELED 142
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-201 |
1.26e-41 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 155.61 E-value: 1.26e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 3 MIDVSNLTFGYEGspELIFDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQGEY-PYSGTI--SASVEFEYFPYEVANL-- 77
Cdd:COG0488 315 VLELEGLSKSYGD--KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELePDSGTVklGETVKIGYFDQHQEELdp 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 78 SRTGLEVVREIAPEAEDWEIQRELGLLDLAERSLELPFSSLSNGERTKVLLAAMFLKENAFLLIDEPTNHLDLEGRRKLG 157
Cdd:COG0488 393 DKTVLDELRDGAPGGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALE 472
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2468763893 158 SYLARKRG-FLLVSHDRAFLDQCVDHILAINRTNIEIQRGNFSSW 201
Cdd:COG0488 473 EALDDFPGtVLLVSHDRYFLDRVATRILEFEDGGVREYPGGYDDY 517
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
31-489 |
1.39e-33 |
|
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: 133.52 E-value: 1.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 31 GWKLGFTGRNGRGKTTFLRLLQG-EYPYSG--TISASVEFEYFPYE-VANLSRTGLEVVREIAPEAED------------ 94
Cdd:TIGR03719 31 GAKIGVLGLNGAGKSTLLRIMAGvDKDFNGeaRPQPGIKVGYLPQEpQLDPTKTVRENVEEGVAEIKDaldrfneisaky 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 95 --------------------------WEIQRELgllDLAERSLELP-----FSSLSNGERTKVLLAAMFLKENAFLLIDE 143
Cdd:TIGR03719 111 aepdadfdklaaeqaelqeiidaadaWDLDSQL---EIAMDALRCPpwdadVTKLSGGERRRVALCRLLLSKPDMLLLDE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 144 PTNHLDLEGRRKLGSYLARKRG-FLLVSHDRAFLDQCVDHILAINRTNIEIQRGNFSSWWENRRRQDAFELARQEKLQKD 222
Cdd:TIGR03719 188 PTNHLDAESVAWLERHLQEYPGtVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWLEQKQKRLEQEEKEESARQKT 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 223 IGRLTEsarrasgWSdrtekskfgvdKTGAKAadrgfvghKAAKlmqrSKSIQRRREEAVEEKKQllQNLERQEaLAVTP 302
Cdd:TIGR03719 268 LKRELE-------WV-----------RQSPKG--------RQAK----SKARLARYEELLSQEFQ--KRNETAE-IYIPP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 303 LPcRAGARLAEFRDVAVCYDGRTVCREITFEVLAGERIALQGANGCGKSSLLKLLLGEEIPHSGTVETMSGLVVSYVSQN 382
Cdd:TIGR03719 315 GP-RLGDKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQS 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 383 TDHLRGSLTEF-ARTQGLDgsrfrtILR--KLDVPREQF-----------EKDLADYSSGQKKKVLLAASLCTQAHLYVW 448
Cdd:TIGR03719 394 RDALDPNKTVWeEISGGLD------IIKlgKREIPSRAYvgrfnfkgsdqQKKVGQLSGGERNRVHLAKTLKSGGNVLLL 467
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 2468763893 449 DEPLNFIDVISRMQVEDLLLACRPTLLFVEHDARFCDEIAT 489
Cdd:TIGR03719 468 DEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIAT 508
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
19-480 |
8.57e-27 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 114.11 E-value: 8.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 19 LIFDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQGEYPYSG---TISASVEFEYFPYEVANLSRTGLEVV----RE---- 87
Cdd:PRK10636 15 VLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGgsyTFPGNWQLAWVNQETPALPQPALEYVidgdREyrql 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 88 -----IAPEAED----------------WEIQ-RELGLLD---LAERSLELPFSSLSNGERTKVLLAAMFLKENAFLLID 142
Cdd:PRK10636 95 eaqlhDANERNDghaiatihgkldaidaWTIRsRAASLLHglgFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 143 EPTNHLDLEGRRKLGSYLARKRGFL-LVSHDRAFLDQCVDHILAINRTNIEIQRGNFSSWwenrRRQDAFELARQEKL-- 219
Cdd:PRK10636 175 EPTNHLDLDAVIWLEKWLKSYQGTLiLISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSSF----EVQRATRLAQQQAMye 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 220 --QKDIGRLTESarrasgwsdrtekskfgVDKTGAKAAdrgfvghKAAKLMQRSKSIQRRREEAVEEKKQLLQNLERQ-E 296
Cdd:PRK10636 251 sqQERVAHLQSY-----------------IDRFRAKAT-------KAKQAQSRIKMLERMELIAPAHVDNPFHFSFRApE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 297 ALavtPLPcragarLAEFRDVAVCYDGRTVCREITFEVLAGERIALQGANGCGKSSLLKLLLGEEIPHSGTVETMSGLVV 376
Cdd:PRK10636 307 SL---PNP------LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKL 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 377 SYVSQNTdhlrgslTEFARTqglDGSRFRTILRKldVPREqFEKDLADY------------------SSGQKKKVLLAAS 438
Cdd:PRK10636 378 GYFAQHQ-------LEFLRA---DESPLQHLARL--APQE-LEQKLRDYlggfgfqgdkvteetrrfSGGEKARLVLALI 444
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 2468763893 439 LCTQAHLYVWDEPLNFIDVISRMQVEDLLLACRPTLLFVEHD 480
Cdd:PRK10636 445 VWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGALVVVSHD 486
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-187 |
1.68e-24 |
|
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: 100.20 E-value: 1.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 5 DVSNLTFGYEGSPelIFDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQGEY-PYSGTISasvefeYFPYEVANLSRtgLE 83
Cdd:cd03214 1 EVENLSVGYGGRT--VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLkPSSGEIL------LDGKDLASLSP--KE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 84 VVREIA--PEAEDweiqrELGLLDLAERslelPFSSLSNGERTKVLLAAMFLKENAFLLIDEPTNHLDLEGRRKLGSY-- 159
Cdd:cd03214 71 LARKIAyvPQALE-----LLGLAHLADR----PFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELlr 141
|
170 180 190
....*....|....*....|....*....|...
gi 2468763893 160 -LARKRGF--LLVSHD--RAFldQCVDHILAIN 187
Cdd:cd03214 142 rLARERGKtvVMVLHDlnLAA--RYADRVILLK 172
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
6-191 |
2.26e-24 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 100.69 E-value: 2.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 6 VSNLTFGYEGSPelIFDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQGEY-PYSGTI-------------------SASV 65
Cdd:cd03235 2 VEDLTVSYGGHP--VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLkPTSGSIrvfgkplekerkrigyvpqRRSI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 66 EFEyFPYEVANLSRTGL--EVVREIAPEAEDWEIQRE----LGLLDLAERslelPFSSLSNGERTKVLLAAMFLKENAFL 139
Cdd:cd03235 80 DRD-FPISVRDVVLMGLygHKGLFRRLSKADKAKVDEalerVGLSELADR----QIGELSGGQQQRVLLARALVQDPDLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2468763893 140 LIDEPTNHLDLEGRRKLGSYL----ARKRGFLLVSHDRAFLDQCVDHILAINRTNI 191
Cdd:cd03235 155 LLDEPFAGVDPKTQEDIYELLrelrREGMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
3-188 |
7.47e-24 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 99.93 E-value: 7.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 3 MIDVSNLTFGYEGSPelIFDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQGE-YPYSGTIsaSVEFE------------- 68
Cdd:COG4555 1 MIEVENLSKKYGKVP--ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLlKPDSGSI--LIDGEdvrkeprearrqi 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 69 -YFPYEVANLSR-TGLEVVREIAPEAEDW---------EIQRELGLLDLAERSLelpfSSLSNGERTKVLLAAMFLKENA 137
Cdd:COG4555 77 gVLPDERGLYDRlTVRENIRYFAELYGLFdeelkkrieELIELLGLEEFLDRRV----GELSTGMKKKVALARALVHDPK 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2468763893 138 FLLIDEPTNHLDLEGRRKLGSYLAR----KRGFLLVSHDRAFLDQCVDHILAINR 188
Cdd:COG4555 153 VLLLDEPTNGLDVMARRLLREILRAlkkeGKTVLFSSHIMQEVEALCDRVVILHK 207
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-188 |
2.14e-23 |
|
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: 96.16 E-value: 2.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 6 VSNLTFGYEGSPelIFDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQGEY-PYSGTIsasvefEYFPYEVANLSRtglev 84
Cdd:cd00267 2 IENLSFRYGGRT--ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLkPTSGEI------LIDGKDIAKLPL----- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 85 vreiapeaedWEIQRELGLLdlaerslelpfSSLSNGERTKVLLAAMFLKENAFLLIDEPTNHLDLEGRRKLGSYL---- 160
Cdd:cd00267 69 ----------EELRRRIGYV-----------PQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLrela 127
|
170 180
....*....|....*....|....*...
gi 2468763893 161 ARKRGFLLVSHDRAFLDQCVDHILAINR 188
Cdd:cd00267 128 EEGRTVIIVTHDPELAELAADRVIVLKD 155
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
313-489 |
2.89e-23 |
|
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: 95.59 E-value: 2.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 313 EFRDVAVCYDGRTVCREITFEVLAGERIALQGANGCGKSSLLKLLLGEEIPHSGTVETMSGLVVSYVSQntdhlrgslte 392
Cdd:cd03221 2 ELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ----------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 393 fartqgldgsrfrtilrkldvpreqfekdladYSSGQKKKVLLAASLCTQAHLYVWDEPLNFIDVISRMQVEDLLLACRP 472
Cdd:cd03221 71 --------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPG 118
|
170
....*....|....*..
gi 2468763893 473 TLLFVEHDARFCDEIAT 489
Cdd:cd03221 119 TVILVSHDRYFLDQVAT 135
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
6-188 |
3.08e-23 |
|
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: 97.54 E-value: 3.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 6 VSNLTFGYEGSPELIFDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQG-EYPYSGTISASvEFEYFPYEVANLSRT---- 80
Cdd:cd03225 2 LKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGlLGPTSGEVLVD-GKDLTKLSLKELRRKvglv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 81 ---------GLEVVREIA--------PEAEDWEIQRE----LGLLDLAERSLelpfSSLSNGERTKVLLAAMFLKENAFL 139
Cdd:cd03225 81 fqnpddqffGPTVEEEVAfglenlglPEEEIEERVEEalelVGLEGLRDRSP----FTLSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2468763893 140 LIDEPTNHLDLEGRRKLGSYLAR--KRG--FLLVSHDRAFLDQCVDHILAINR 188
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKlkAEGktIIIVTHDLDLLLELADRVIVLED 209
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-489 |
6.88e-23 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 102.34 E-value: 6.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 1 MSMIDVSN--LTFGYegSPELifDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQGEYP-------YSGTISAS------- 64
Cdd:PRK11147 1 MSLISIHGawLSFSD--APLL--DNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLlddgriiYEQDLIVArlqqdpp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 65 --VEFEYFPY------EVA--------------------NLSRtgLEVVREIAPEAEDWE----IQRELGLLDLaerSLE 112
Cdd:PRK11147 77 rnVEGTVYDFvaegieEQAeylkryhdishlvetdpsekNLNE--LAKLQEQLDHHNLWQlenrINEVLAQLGL---DPD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 113 LPFSSLSNGERTKVLLAAMFLKENAFLLIDEPTNHLDLEGRRKLGSYLARKRGFLL-VSHDRAFLDQCVDHIlainrtnI 191
Cdd:PRK11147 152 AALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIfISHDRSFIRNMATRI-------V 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 192 EIQRGNFSSWWENrrrQDAF-----ELARQEKLQKDI--GRLTES---------ARRAsgwsdRTEkskfgvdktgakaa 255
Cdd:PRK11147 225 DLDRGKLVSYPGN---YDQYllekeEALRVEELQNAEfdRKLAQEevwirqgikARRT-----RNE-------------- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 256 drGFVghKAAKLMQRSKSiqRRREEAVEEKKQLlqnlerQEALavtplpcRAGARLAEFRDVAVCYDGRTVCREITFEVL 335
Cdd:PRK11147 283 --GRV--RALKALRRERS--ERREVMGTAKMQV------EEAS-------RSGKIVFEMENVNYQIDGKQLVKDFSAQVQ 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 336 AGERIALQGANGCGKSSLLKLLLGEEIPHSGTVETMSGLVVSYVSQ--------------------------NTDHLRGS 389
Cdd:PRK11147 344 RGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFDQhraeldpektvmdnlaegkqevmvngRPRHVLGY 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 390 LTEFArtqgLDGSRFRTILRKLdvpreqfekdladySSGQKKKVLLAASLCTQAHLYVWDEPLNFIDVISRMQVEDLLLA 469
Cdd:PRK11147 424 LQDFL----FHPKRAMTPVKAL--------------SGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDS 485
|
570 580
....*....|....*....|
gi 2468763893 470 CRPTLLFVEHDARFCDEIAT 489
Cdd:PRK11147 486 YQGTVLLVSHDRQFVDNTVT 505
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-208 |
1.49e-22 |
|
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: 100.78 E-value: 1.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 4 IDVSNLTFGYEGspELIFDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQG-EYPYSGTIS--ASVEFEYfpyevANLSRT 80
Cdd:TIGR03719 323 IEAENLTKAFGD--KLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGqEQPDSGTIEigETVKLAY-----VDQSRD 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 81 GLEVVREIAPEAEDWEIQRELGLLDLAERSLELPF-----------SSLSNGERTKVLLAAMfLKENA-FLLIDEPTNHL 148
Cdd:TIGR03719 396 ALDPNKTVWEEISGGLDIIKLGKREIPSRAYVGRFnfkgsdqqkkvGQLSGGERNRVHLAKT-LKSGGnVLLLDEPTNDL 474
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2468763893 149 DLEGRRKLGSYLARKRGFLLV-SHDRAFLDQCVDHILAI-NRTNIEIQRGNFSSWWENRRRQ 208
Cdd:TIGR03719 475 DVETLRALEEALLNFAGCAVViSHDRWFLDRIATHILAFeGDSHVEWFEGNFSEYEEDKKRR 536
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
21-146 |
8.96e-21 |
|
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: 88.47 E-value: 8.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 21 FDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQGEY-PYSGTI-------------SASVEFEYFPYEVANLSR-TGLEVV 85
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLsPTEGTIlldgqdltdderkSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 86 RE---------IAPEAEDWEIQRELGLLDLAERSLELPFSSLSNGERTKVLLAAMFLKENAFLLIDEPTN 146
Cdd:pfam00005 81 RLglllkglskREKDARAEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4-198 |
1.04e-20 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 95.67 E-value: 1.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 4 IDVSNLTFGYEGSPELIFDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQGEY-PYSGTIsasvefeYF-PYEVANLSRTG 81
Cdd:COG2274 474 IELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYePTSGRI-------LIdGIDLRQIDPAS 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 82 L---------EV------VRE-IA---PEAED---WEIQRELGLLDLAERsleLPF----------SSLSNGERTKVLLA 129
Cdd:COG2274 547 LrrqigvvlqDVflfsgtIREnITlgdPDATDeeiIEAARLAGLHDFIEA---LPMgydtvvgeggSNLSGGQRQRLAIA 623
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2468763893 130 AMFLKENAFLLIDEPTNHLDLEGRRKLGSYLAR---KRGFLLVSHDRAFLDQCvDHILAINRTNIeIQRGNF 198
Cdd:COG2274 624 RALLRNPRILILDEATSALDAETEAIILENLRRllkGRTVIIIAHRLSTIRLA-DRIIVLDKGRI-VEDGTH 693
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-188 |
1.99e-20 |
|
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: 88.22 E-value: 1.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 4 IDVSNLTFGYEGSPelIFDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQGEY-PYSGTISasvefeyfpYEVANLSRTGL 82
Cdd:cd03230 1 IEVRNLSKRYGKKT--ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLkPDSGEIK---------VLGKDIKKEPE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 83 EVVREIAPEAEDWEIQRELGLLDLAErslelpfssLSNGERTKVLLAAMFLKENAFLLIDEPTNHLDLEGRRKLGSYL-- 160
Cdd:cd03230 70 EVKRRIGYLPEEPSLYENLTVRENLK---------LSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLre 140
|
170 180 190
....*....|....*....|....*....|
gi 2468763893 161 --ARKRGFLLVSHDRAFLDQCVDHILAINR 188
Cdd:cd03230 141 lkKEGKTILLSSHILEEAERLCDRVAILNN 170
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-184 |
3.21e-20 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 89.76 E-value: 3.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 1 MSMIDVSNLTFGYEGSPelIFDHVGFQIDSG--WKLgfTGRNGRGKTTFLRLLQGEYP--YSGTI--------------- 61
Cdd:COG1119 1 DPLLELRNVTVRRGGKT--ILDDISWTVKPGehWAI--LGPNGAGKSTLLSLITGDLPptYGNDVrlfgerrggedvwel 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 62 -------SASVeFEYFPYEVanlsrTGLEVVR-------EIAPEAEDWEIQR------ELGLLDLAERslelPFSSLSNG 121
Cdd:COG1119 77 rkriglvSPAL-QLRFPRDE-----TVLDVVLsgffdsiGLYREPTDEQRERarelleLLGLAHLADR----PFGTLSQG 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2468763893 122 ERTKVLLA-AMfLKENAFLLIDEPTNHLDLEGRRKLGSYLAR-----KRGFLLVSHDRAFLDQCVDHIL 184
Cdd:COG1119 147 EQRRVLIArAL-VKDPELLILDEPTAGLDLGARELLLALLDKlaaegAPTLVLVTHHVEEIPPGITHVL 214
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-188 |
3.88e-20 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 89.72 E-value: 3.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 3 MIDVSNLTFGYEGSPelIFDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQGE-YPYSGTIsasvefEYFPYEVANLSR-- 79
Cdd:COG1120 1 MLEAENLSVGYGGRP--VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLlKPSSGEV------LLDGRDLASLSRre 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 80 ------------------TGLEVV---------REIAPEAEDWEIQRE----LGLLDLAERslelPFSSLSNGERTKVLL 128
Cdd:COG1120 73 larriayvpqeppapfglTVRELValgryphlgLFGRPSAEDREAVEEalerTGLEHLADR----PVDELSGGERQRVLI 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2468763893 129 AAMFLKENAFLLIDEPTNHLDLEGRRKLGSY---LARKRG--FLLVSHDrafLDQ----CvDHILAINR 188
Cdd:COG1120 149 ARALAQEPPLLLLDEPTSHLDLAHQLEVLELlrrLARERGrtVVMVLHD---LNLaaryA-DRLVLLKD 213
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-198 |
8.80e-20 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 92.26 E-value: 8.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 4 IDVSNLTFGYEGSPelIFDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQGEY-PYSGTI--SASVEFEYFPYEVANLSRT 80
Cdd:PRK15064 320 LEVENLTKGFDNGP--LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELePDSGTVkwSENANIGYYAQDHAYDFEN 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 81 GLEVVreiapeaeDWEIQ-RELGLLDLAERSL--ELPFSS---------LSNGERTKVLLAAMFLKENAFLLIDEPTNHL 148
Cdd:PRK15064 398 DLTLF--------DWMSQwRQEGDDEQAVRGTlgRLLFSQddikksvkvLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHM 469
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2468763893 149 DLEGRRKLGSYLARKRGFLL-VSHDRAFLDQCVDHILAINRTNIEIQRGNF 198
Cdd:PRK15064 470 DMESIESLNMALEKYEGTLIfVSHDREFVSSLATRIIEITPDGVVDFSGTY 520
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-488 |
1.09e-19 |
|
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: 91.89 E-value: 1.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 1 MS-MIDVSNLTFGYEGSPELIFDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQGEYPYSGTISASVEFE----------- 68
Cdd:COG1123 1 MTpLLEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRISGEVLLDgrdllelseal 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 69 ------YFPYEVA---NLSRTGLEVV-----REIAPEAEDWEIQRELGLLDLAERSLELPFsSLSNGERTKVLLAAMFLK 134
Cdd:COG1123 81 rgrrigMVFQDPMtqlNPVTVGDQIAealenLGLSRAEARARVLELLEAVGLERRLDRYPH-QLSGGQRQRVAIAMALAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 135 ENAFLLIDEPTNHLDLEGRR---KLGSYLARKRG--FLLVSHDRAFLDQCVDHILAINRtnieiqrgnfsswwenrrrqd 209
Cdd:COG1123 160 DPDLLIADEPTTALDVTTQAeilDLLRELQRERGttVLLITHDLGVVAEIADRVVVMDD--------------------- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 210 afelarqeklqkdiGRLTESArrasgwsdrtekskfgvdktgakaadrgfvghkaaklmqrsksiqrRREEAVEEKKQLL 289
Cdd:COG1123 219 --------------GRIVEDG----------------------------------------------PPEEILAAPQALA 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 290 QNLERQEALAVTPLPCRAGARLAEFRDVAVCYDGR-----TVCREITFEVLAGERIALQGANGC------------GKss 352
Cdd:COG1123 239 AVPRLGAARGRAAPAAAAAEPLLEVRNLSKRYPVRgkggvRAVDDVSLTLRRGETLGLVGESGSgkstlarlllglLR-- 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 353 llklllgeeiPHSGTV----ETMSGLV----------VSYVSQNTDH-------LRGSLTEFARTQGLDGS-----RFRT 406
Cdd:COG1123 317 ----------PTSGSIlfdgKDLTKLSrrslrelrrrVQMVFQDPYSslnprmtVGDIIAEPLRLHGLLSRaerreRVAE 386
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 407 ILRKLDVPREQFEKDLADYSSGQKKKVLLAASLCTQAHLYVWDEPLNFIDVISRMQVEDLLLACRP----TLLFVEHD-- 480
Cdd:COG1123 387 LLERVGLPPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRelglTYLFISHDla 466
|
570
....*....|
gi 2468763893 481 --ARFCDEIA 488
Cdd:COG1123 467 vvRYIADRVA 476
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
3-489 |
2.28e-19 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 91.11 E-value: 2.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 3 MIDVSNLT--FGyegsPELIFDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQGEY-PYSGTISASV----------EFEY 69
Cdd:PRK15064 1 MLSTANITmqFG----AKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLePSAGNVSLDPnerlgklrqdQFAF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 70 FPYEVanlsrtgLEVVreIAPEAEDWEIQRE---------------LGLLDL-----------AE-RSLEL--------- 113
Cdd:PRK15064 77 EEFTV-------LDTV--IMGHTELWEVKQErdriyalpemseedgMKVADLevkfaemdgytAEaRAGELllgvgipee 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 114 ----PFSSLSNGERTKVLLA-AMFLKENaFLLIDEPTNHLDLEGRRKLGSYL-ARKRGFLLVSHDRAFLDQCVDHILAIN 187
Cdd:PRK15064 148 qhygLMSEVAPGWKLRVLLAqALFSNPD-ILLLDEPTNNLDINTIRWLEDVLnERNSTMIIISHDRHFLNSVCTHMADLD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 188 RTNIEIQRGNFSSWWEnrrrqdAFELARqEKLQKD-------IGRLTESARRasgwsdrtekskFGVDKTGAKAAdrgfv 260
Cdd:PRK15064 227 YGELRVYPGNYDEYMT------AATQAR-ERLLADnakkkaqIAELQSFVSR------------FSANASKAKQA----- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 261 ghkaaklMQRSKSIQRRREEAV-------------EEKKqllqnLERQeALavtplpcragarlaEFRDVAVCYDGRTVC 327
Cdd:PRK15064 283 -------TSRAKQIDKIKLEEVkpssrqnpfirfeQDKK-----LHRN-AL--------------EVENLTKGFDNGPLF 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 328 REITFEVLAGERIALQGANGCGKSSLLKLLLGEEIPHSGTVETMSGLVVSYVSQNTDHlrgsltEFA------------R 395
Cdd:PRK15064 336 KNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQDHAY------DFEndltlfdwmsqwR 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 396 TQGLDGSRFRTILRKLDVPREQFEKDLADYSSGQKKKVLLAASLCTQAHLYVWDEPLNFIDVISrmqVEDLLLAC---RP 472
Cdd:PRK15064 410 QEGDDEQAVRGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMES---IESLNMALekyEG 486
|
570
....*....|....*..
gi 2468763893 473 TLLFVEHDARFCDEIAT 489
Cdd:PRK15064 487 TLIFVSHDREFVSSLAT 503
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
2-201 |
2.46e-19 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 91.46 E-value: 2.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 2 SMIDVSNLTFGYEGSPeLIFDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQGEY-PYSGTI--SASVEFEYFP---YEVA 75
Cdd:PLN03073 507 PIISFSDASFGYPGGP-LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELqPSSGTVfrSAKVRMAVFSqhhVDGL 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 76 NLSRTGLEVVREIAPEAEDWEIQRELGLLDLAERSLELPFSSLSNGERTKVLLAAMFLKENAFLLIDEPTNHLDLEGRRK 155
Cdd:PLN03073 586 DLSSNPLLYMMRCFPGVPEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEA 665
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2468763893 156 LGSYLAR-KRGFLLVSHDRAFLDQCVDHILAINRTNIEIQRGNFSSW 201
Cdd:PLN03073 666 LIQGLVLfQGGVLMVSHDEHLISGSVDELWVVSEGKVTPFHGTFHDY 712
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-207 |
3.31e-19 |
|
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: 90.60 E-value: 3.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 4 IDVSNLTFGYEGSPELIFDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQGEY-PYSGTIS-ASVEFEYFPYE-----VAN 76
Cdd:COG4987 334 LELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLdPQSGSITlGGVDLRDLDEDdlrrrIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 77 LS----------RTGLEVVREIAPEAEDWEIQRELGLLDLAERsleLPF----------SSLSNGERTKVLLAAMFLKEN 136
Cdd:COG4987 414 VPqrphlfdttlRENLRLARPDATDEELWAALERVGLGDWLAA---LPDgldtwlgeggRRLSGGERRRLALARALLRDA 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2468763893 137 AFLLIDEPTNHLDLEGRRKLGSYL---ARKRGFLLVSHDRAFLDQcVDHILAINRTNIeIQRGNFSSWWENRRR 207
Cdd:COG4987 491 PILLLDEPTEGLDAATEQALLADLleaLAGRTVLLITHRLAGLER-MDRILVLEDGRI-VEQGTHEELLAQNGR 562
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
31-489 |
3.45e-19 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 90.56 E-value: 3.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 31 GWKLGFTGRNGRGKTTFLRLLQG-EYPYSGTISASVEFE--YFPYE-VANLSRTGLEVVREIAPE--------------- 91
Cdd:PRK11819 33 GAKIGVLGLNGAGKSTLLRIMAGvDKEFEGEARPAPGIKvgYLPQEpQLDPEKTVRENVEEGVAEvkaaldrfneiyaay 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 92 AED-----------------------WEIQRELgllDLAERSLELP-----FSSLSNGERTKVLLAAMFLKENAFLLIDE 143
Cdd:PRK11819 113 AEPdadfdalaaeqgelqeiidaadaWDLDSQL---EIAMDALRCPpwdakVTKLSGGERRRVALCRLLLEKPDMLLLDE 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 144 PTNHLDLEGRRKLGSYLARKRG-FLLVSHDRAFLDQCVDHILAINRTNIEIQRGNFSSWWENRRRQDAFELARQEKLQKD 222
Cdd:PRK11819 190 PTNHLDAESVAWLEQFLHDYPGtVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWLEQKAKRLAQEEKQEAARQKA 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 223 IGRLTESARrasgwsdrtekskfgvdkTGAKAadrgfvghKAAKlmqrSKS-IQRRREEAVEEKKQLLQNLERQealavT 301
Cdd:PRK11819 270 LKRELEWVR------------------QSPKA--------RQAK----SKArLARYEELLSEEYQKRNETNEIF-----I 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 302 PLPCRAGARLAEFRDVAVCYDGRTVCREITFEVLAGERIALQGANGCGKSSLLKLLLGEEIPHSGTVETMSGLVVSYVSQ 381
Cdd:PRK11819 315 PPGPRLGDKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYVDQ 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 382 NTDHLRGSLTEF-ARTQGLDgsrfrtILR--KLDVP------REQF-----EKDLADYSSGQKKKVLLAASLCTQAHLYV 447
Cdd:PRK11819 395 SRDALDPNKTVWeEISGGLD------IIKvgNREIPsrayvgRFNFkggdqQKKVGVLSGGERNRLHLAKTLKQGGNVLL 468
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 2468763893 448 WDEPLNFIDVISRMQVEDLLLACRPTLLFVEHDARFCDEIAT 489
Cdd:PRK11819 469 LDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRIAT 510
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-184 |
5.60e-19 |
|
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: 83.97 E-value: 5.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 4 IDVSNLTFGYEGSPELIFDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQGEY-PYSGTISASvefeyfpyevanlsrtGL 82
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYdPTSGEILID----------------GV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 83 EvVREIAPEaedwEIQRELGLLD----LAERSLE--LpfssLSNGERTKVLLAAMFLKENAFLLIDEPTNHLDLEGRRKL 156
Cdd:cd03228 65 D-LRDLDLE----SLRKNIAYVPqdpfLFSGTIRenI----LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALI 135
|
170 180 190
....*....|....*....|....*....|.
gi 2468763893 157 GSYLARKRGF---LLVSHDRAFLDQCvDHIL 184
Cdd:cd03228 136 LEALRALAKGktvIVIAHRLSTIRDA-DRII 165
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-207 |
7.40e-18 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 86.33 E-value: 7.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 4 IDVSNLTFGYEGspELIFDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQG-EYPYSGTIS--ASVEFEYfpyevANLSRT 80
Cdd:PRK11819 325 IEAENLSKSFGD--RLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGqEQPDSGTIKigETVKLAY-----VDQSRD 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 81 GLEvvreiaPEAEDWE-IQRELGLLDLAERslELP---------FS---------SLSNGERTKVLLAAMfLKENA-FLL 140
Cdd:PRK11819 398 ALD------PNKTVWEeISGGLDIIKVGNR--EIPsrayvgrfnFKggdqqkkvgVLSGGERNRLHLAKT-LKQGGnVLL 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2468763893 141 IDEPTNHLDLEGRRKLGSYLARKRGFLLV-SHDRAFLDQCVDHILAI-NRTNIEIQRGNFSSWWENRRR 207
Cdd:PRK11819 469 LDEPTNDLDVETLRALEEALLEFPGCAVViSHDRWFLDRIATHILAFeGDSQVEWFEGNFQEYEEDKKR 537
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-191 |
1.11e-16 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 78.70 E-value: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 4 IDVSNLTFGYEGSPelIFDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQG-EYPYSGTIsasvefeYF---PY------- 72
Cdd:COG4619 1 LELEGLSFRVGGKP--ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADlDPPTSGEI-------YLdgkPLsampppe 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 73 ---EVANLS-RTGL--EVVRE-------IAPEAEDWEIQRE-LGLLDLAERSLELPFSSLSNGERTKVLLAAMFLKENAF 138
Cdd:COG4619 72 wrrQVAYVPqEPALwgGTVRDnlpfpfqLRERKFDRERALElLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2468763893 139 LLIDEPTNHLDLEGRRK----LGSYLARK-RGFLLVSHDRAFLDQCVDHILAINRTNI 191
Cdd:COG4619 152 LLLDEPTSALDPENTRRveelLREYLAEEgRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
313-488 |
1.72e-16 |
|
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: 78.34 E-value: 1.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 313 EFRDVAVCYDGRTVCREITFEVLAGERIALQGANGCGKSSLLKLLLGEEIPHSGTVE------TMSGLVVSYVSQNTDHL 386
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRvfgkplEKERKRIGYVPQRRSID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 387 RG---SLTEFARTqGLDGSRFrtILRKLDvpREQFEK-----------DLADY-----SSGQKKKVLLAASLCTQAHLYV 447
Cdd:cd03235 81 RDfpiSVRDVVLM-GLYGHKG--LFRRLS--KADKAKvdealervglsELADRqigelSGGQQQRVLLARALVQDPDLLL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2468763893 448 WDEPLNFIDVISRMQVEDLLLACRP---TLLFVEHD----ARFCDEIA 488
Cdd:cd03235 156 LDEPFAGVDPKTQEDIYELLRELRRegmTILVVTHDlglvLEYFDRVL 203
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
31-480 |
2.21e-16 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 82.22 E-value: 2.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 31 GWKLGFTGRNGRGKTTFLR---------------LLQGEYPYSG--------TISASVEFEYFPYEVANL---------- 77
Cdd:PLN03073 203 GRHYGLVGRNGTGKTTFLRymamhaidgipkncqILHVEQEVVGddttalqcVLNTDIERTQLLEEEAQLvaqqrelefe 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 78 SRTGLEVVREIAPEAEDW------EIQRELGLLDL--AERSLE-----LPFSS---------LSNGERTKVLLAAMFLKE 135
Cdd:PLN03073 283 TETGKGKGANKDGVDKDAvsqrleEIYKRLELIDAytAEARAAsilagLSFTPemqvkatktFSGGWRMRIALARALFIE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 136 NAFLLIDEPTNHLDLEGRRKLGSYLAR-KRGFLLVSHDRAFLDQCVDHILAINRTNIEIQRGNFsswwenrrrqDAFELA 214
Cdd:PLN03073 363 PDLLLLDEPTNHLDLHAVLWLETYLLKwPKTFIVVSHAREFLNTVVTDILHLHGQKLVTYKGDY----------DTFERT 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 215 RQEKLqKDIGRLTESARRAsgwsdRTEKSKFgVDKTGAKAadrgfvghKAAKLMQ-RSKSIQRrreeaVEEKKQLLQNLE 293
Cdd:PLN03073 433 REEQL-KNQQKAFESNERS-----RSHMQAF-IDKFRYNA--------KRASLVQsRIKALDR-----LGHVDAVVNDPD 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 294 RQEALavtPLP-CRAGARLAEFRDVAVCY-DGRTVCREITFEVLAGERIALQGANGCGKSSLLKLLLGEEIPHSGTVETM 371
Cdd:PLN03073 493 YKFEF---PTPdDRPGPPIISFSDASFGYpGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRS 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 372 SGLVVSYVSQNtdHLRG------SLTEFART-QGLDGSRFRTILRKLDVPREQFEKDLADYSSGQKKKVLLAASLCTQAH 444
Cdd:PLN03073 570 AKVRMAVFSQH--HVDGldlssnPLLYMMRCfPGVPEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPH 647
|
490 500 510
....*....|....*....|....*....|....*....
gi 2468763893 445 LYVWDEPLNFIDVISrmqVEDL---LLACRPTLLFVEHD 480
Cdd:PLN03073 648 ILLLDEPSNHLDLDA---VEALiqgLVLFQGGVLMVSHD 683
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-198 |
5.09e-16 |
|
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: 80.57 E-value: 5.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 2 SMIDVSNLTFGYEGSPELIfDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQGEY-PYSGTISASvefeyfPYEVANLSRT 80
Cdd:COG4988 335 PSIELEDVSFSYPGGRPAL-DGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLpPYSGSILIN------GVDLSDLDPA 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 81 GL-------------------EVVREIAPEAEDWEIQRELGLLDLAERSLELPF----------SSLSNGERTKVLLAAM 131
Cdd:COG4988 408 SWrrqiawvpqnpylfagtirENLRLGRPDASDEELEAALEAAGLDEFVAALPDgldtplgeggRGLSGGQAQRLALARA 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 132 FLKENAFLLIDEPTNHLDLEGRRKLGSY---LARKRGFLLVSHDRAFLDQCvDHILAINRTNIeIQRGNF 198
Cdd:COG4988 488 LLRDAPLLLLDEPTAHLDAETEAEILQAlrrLAKGRTVILITHRLALLAQA-DRILVLDDGRI-VEQGTH 555
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
34-184 |
9.37e-16 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 79.85 E-value: 9.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 34 LGFTGRNGRGKTTFLRLLQGEY-PYSGTISASVEFEYFP-YEVANLSRTGLEVVREIAPEAED-W---EIQRELGLLDLA 107
Cdd:PRK13409 368 IGIVGPNGIGKTTFAKLLAGVLkPDEGEVDPELKISYKPqYIKPDYDGTVEDLLRSITDDLGSsYyksEIIKPLQLERLL 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 108 ERSLElpfsSLSNGERTKVLLAAMFLKENAFLLIDEPTNHLDLEGRRKLGSYLAR-----KRGFLLVSHDRAFLDQCVDH 182
Cdd:PRK13409 448 DKNVK----DLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRiaeerEATALVVDHDIYMIDYISDR 523
|
..
gi 2468763893 183 IL 184
Cdd:PRK13409 524 LM 525
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
19-232 |
1.69e-15 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 79.06 E-value: 1.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 19 LIFDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQGEY-PYSGTISAS--VEFEYFP---YEVANLSRTGLEVVREIAPEA 92
Cdd:PRK10636 326 IILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELaPVSGEIGLAkgIKLGYFAqhqLEFLRADESPLQHLARLAPQE 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 93 EDWEIQRELGLLDLAERSLELPFSSLSNGERTKVLLAAMFLKENAFLLIDEPTNHLDLEGRRKLGSYLARKRGFL-LVSH 171
Cdd:PRK10636 406 LEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGALvVVSH 485
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2468763893 172 DRAFLDQCVDHILAINRTNIEIQRG---NFSSWWENRRRQDafelARQEKLQKDIGRLTESARR 232
Cdd:PRK10636 486 DRHLLRSTTDDLYLVHDGKVEPFDGdleDYQQWLSDVQKQE----NQTDEAPKENNANSAQARK 545
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
34-177 |
2.20e-15 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 78.67 E-value: 2.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 34 LGFTGRNGRGKTTFLRLLQGEY-PYSGTISASVEFEYFP-YEVANLSRTGLEVVREIAPEAED--W---EIQRELGLLDL 106
Cdd:COG1245 369 LGIVGPNGIGKTTFAKILAGVLkPDEGEVDEDLKISYKPqYISPDYDGTVEEFLRSANTDDFGssYyktEIIKPLGLEKL 448
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2468763893 107 AERSLelpfSSLSNGERTKVLLAAMFLKENAFLLIDEPTNHLDLEGRRKLGSYLAR-----KRGFLLVSHDRAFLD 177
Cdd:COG1245 449 LDKNV----KDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRfaenrGKTAMVVDHDIYLID 520
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-191 |
4.33e-15 |
|
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: 73.02 E-value: 4.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 4 IDVSNLTFGYEGSPELIFDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQG-EYPYSGTISasvefeyfpYEVANLSRTGL 82
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGlLRPTSGRVR---------LDGADISQWDP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 83 EVVRE-IAPEAEDWEiqrelgLLD--LAErslelpfSSLSNGERTKVLLAAMFLKENAFLLIDEPTNHLDLEGRRKLGSY 159
Cdd:cd03246 72 NELGDhVGYLPQDDE------LFSgsIAE-------NILSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQA 138
|
170 180 190
....*....|....*....|....*....|....*.
gi 2468763893 160 LA--RKRGF--LLVSHDRAFLDQCvDHILAINRTNI 191
Cdd:cd03246 139 IAalKAAGAtrIVIAHRPETLASA-DRILVLEDGRV 173
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-194 |
5.02e-15 |
|
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: 73.12 E-value: 5.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 4 IDVSNLTFGYEGSPELIFDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQGEY-PYSGTISASvefEYFPYEVANLSRTGL 82
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLkPQQGEITLD---GVPVSDLEKALSSLI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 83 EVVREiAPEAEDWEIQRELGLldlaerslelpfsSLSNGERTKVLLAAMFLKENAFLLIDEPTNHLDLEGRRKLGSYL-- 160
Cdd:cd03247 78 SVLNQ-RPYLFDTTLRNNLGR-------------RFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIfe 143
|
170 180 190
....*....|....*....|....*....|....*
gi 2468763893 161 -ARKRGFLLVSHDRAFLDQcVDHILAINRTNIEIQ 194
Cdd:cd03247 144 vLKDKTLIWITHHLTGIEH-MDKILFLENGKIIMQ 177
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
313-488 |
1.45e-14 |
|
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: 71.66 E-value: 1.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 313 EFRDVAVCYDGRTVCREITFEVLAGERIALQGANGcgkssllklllgeeiphSG---TVETMSGLVVSYvsqntdhlRGS 389
Cdd:cd03230 2 EVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNG-----------------AGkttLIKIILGLLKPD--------SGE 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 390 LTEFartqGLD-GSRFRTILRKLDVPREQFE-------KDLADYSSGQKKKVLLAASLCTQAHLYVWDEPLNFIDVISRM 461
Cdd:cd03230 57 IKVL----GKDiKKEPEEVKRRIGYLPEEPSlyenltvRENLKLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRR 132
|
170 180 190
....*....|....*....|....*....|....
gi 2468763893 462 QVEDLLLACR---PTLLFVEHD----ARFCDEIA 488
Cdd:cd03230 133 EFWELLRELKkegKTILLSSHIleeaERLCDRVA 166
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
4-186 |
1.45e-14 |
|
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: 76.17 E-value: 1.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 4 IDVSNLTFGYEGSPELIfDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQGE-YPYSGTIS-ASVEFEYF----------- 70
Cdd:TIGR02857 322 LEFSGVSVAYPGRRPAL-RPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFvDPTEGSIAvNGVPLADAdadswrdqiaw 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 71 ----PYEVANlsrTGLEVVREIAPEAEDWEIQRELGLLDLAERSLELPF----------SSLSNGERTKVLLAAMFLKEN 136
Cdd:TIGR02857 401 vpqhPFLFAG---TIAENIRLARPDASDAEIREALERAGLDEFVAALPQgldtpigeggAGLSGGQAQRLALARAFLRDA 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2468763893 137 AFLLIDEPTNHLD-------LEGRRKlgsyLARKRGFLLVSHDRAFLDQCvDHILAI 186
Cdd:TIGR02857 478 PLLLLDEPTAHLDaeteaevLEALRA----LAQGRTVLLVTHRLALAALA-DRIVVL 529
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-150 |
1.60e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 75.26 E-value: 1.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 1 MSMIDVSNLTFGYEGSPelIFDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQGEY-PYSGTI------------------ 61
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTT--VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLtPTAGTVlvagddvealsaraasrr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 62 ------SASVEFEYFPYEVANLSRTGLEVVREIAPEAEDWEIQRELGLLDLAeRSLELPFSSLSNGERTKVLLAAMFLKE 135
Cdd:PRK09536 79 vasvpqDTSLSFEFDVRQVVEMGRTPHRSRFDTWTETDRAAVERAMERTGVA-QFADRPVTSLSGGERQRVLLARALAQA 157
|
170
....*....|....*
gi 2468763893 136 NAFLLIDEPTNHLDL 150
Cdd:PRK09536 158 TPVLLLDEPTASLDI 172
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-187 |
2.32e-14 |
|
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: 71.86 E-value: 2.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 4 IDVSNLTFGYEGSPELifDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQG-EYPYSGTIS-----------------ASV 65
Cdd:cd03268 1 LKTNDLTKTYGKKRVL--DDISLHVKKGEIYGFLGPNGAGKTTTMKIILGlIKPDSGEITfdgksyqkniealrrigALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 66 EF-EYFPYevanlsRTGLEVVREIA--PEAEDWEIQRELGLLDLAERSlELPFSSLSNGERTKVLLAAMFLKENAFLLID 142
Cdd:cd03268 79 EApGFYPN------LTARENLRLLArlLGIRKKRIDEVLDVVGLKDSA-KKKVKGFSLGMKQRLGIALALLGNPDLLILD 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2468763893 143 EPTNHLDLEG----RRKLGSYLARKRGFLLVSHDRAFLDQCVDHILAIN 187
Cdd:cd03268 152 EPTNGLDPDGikelRELILSLRDQGITVLISSHLLSEIQKVADRIGIIN 200
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
4-187 |
2.79e-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: 72.37 E-value: 2.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 4 IDVSNLTFGYE---------GSPELIF----------DHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQGE-YPYSGTISA 63
Cdd:cd03267 1 IEVSNLSKSYRvyskepgliGSLKSLFkrkyrevealKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLlQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 64 SvefEYFPYE-----VANLS---------------RTGLEVVREI--APEAEDWEIQRELG-LLDLaERSLELPFSSLSN 120
Cdd:cd03267 81 A---GLVPWKrrkkfLRRIGvvfgqktqlwwdlpvIDSFYLLAAIydLPPARFKKRLDELSeLLDL-EELLDTPVRQLSL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2468763893 121 GERTKVLLAAMFLKENAFLLIDEPTNHLDLEGRRKLGSYL---ARKRG--FLLVSHDRAFLDQCVDHILAIN 187
Cdd:cd03267 157 GQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLkeyNRERGttVLLTSHYMKDIEALARRVLVID 228
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
6-172 |
3.93e-14 |
|
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: 74.70 E-value: 3.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 6 VSNLTFGYEGSPElIFDHVGFQIDSGWKLGFTGRNGRGKTTFLRLL-------QGEYPYSGTISASVEFE-------YFP 71
Cdd:TIGR02868 337 LRDLSAGYPGAPP-VLDGVSLDLPPGERVAILGPSGSGKSTLLATLaglldplQGEVTLDGVPVSSLDQDevrrrvsVCA 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 72 YEV---ANLSRTGLEVVREIAPEAEDWEIQRELGLLDLAERsleLPF----------SSLSNGERTKVLLAAMFLKENAF 138
Cdd:TIGR02868 416 QDAhlfDTTVRENLRLARPDATDEELWAALERVGLADWLRA---LPDgldtvlgeggARLSGGERQRLALARALLADAPI 492
|
170 180 190
....*....|....*....|....*....|....*..
gi 2468763893 139 LLIDEPTNHLDLEGRRKLGSYLA---RKRGFLLVSHD 172
Cdd:TIGR02868 493 LLLDEPTEHLDAETADELLEDLLaalSGRTVVLITHH 529
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
34-488 |
4.37e-14 |
|
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: 74.82 E-value: 4.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 34 LGFTGRNGRGKTTFLRLLQGE--------------------------YPY-----SGTISASVEFEYfpyeVANLSR--T 80
Cdd:COG1245 102 TGILGPNGIGKSTALKILSGElkpnlgdydeepswdevlkrfrgtelQDYfkklaNGEIKVAHKPQY----VDLIPKvfK 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 81 GleVVREI---APEAEDW-EIQRELGLLDLAERSLelpfSSLSNGERTKVLLAAMFLKENAFLLIDEPTNHLDLEGRRKL 156
Cdd:COG1245 178 G--TVRELlekVDERGKLdELAEKLGLENILDRDI----SELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNV 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 157 GSY---LARK-RGFLLVSHDRAFLDQCVDhilainrtNIEIQRGnfsswwenrrrqdafelarqeklqkdigrltesarr 232
Cdd:COG1245 252 ARLireLAEEgKYVLVVEHDLAILDYLAD--------YVHILYG------------------------------------ 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 233 asgwsdrtEKSKFGV------DKTGAKAADRGFVghkaaklmqRSKSIqRRREEAVE-EKKQLLQNLERQEalavtplpc 305
Cdd:COG1245 288 --------EPGVYGVvskpksVRVGINQYLDGYL---------PEENV-RIRDEPIEfEVHAPRREKEEET--------- 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 306 ragarLAEFRDVAVCYDGrtvcreitF-------EVLAGERIALQGANGcgkssllklllgeeI--------------PH 364
Cdd:COG1245 341 -----LVEYPDLTKSYGG--------FsleveggEIREGEVLGIVGPNG--------------IgkttfakilagvlkPD 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 365 SGTVETmsGLVVSY----VSQNTDHLRGSLTEFARTQGLDGSRFRT-ILRKLDVPReQFEKDLADYSSGQKKKVLLAASL 439
Cdd:COG1245 394 EGEVDE--DLKISYkpqyISPDYDGTVEEFLRSANTDDFGSSYYKTeIIKPLGLEK-LLDKNVKDLSGGELQRVAIAACL 470
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 2468763893 440 CTQAHLYVWDEPLNFIDVISRMQVEDLL----LACRPTLLFVEHDARFCDEIA 488
Cdd:COG1245 471 SRDADLYLLDEPSAHLDVEQRLAVAKAIrrfaENRGKTAMVVDHDIYLIDYIS 523
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
321-487 |
5.15e-14 |
|
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: 71.81 E-value: 5.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 321 YDGRTVCREITFEVLAGERIALQGANGcgkssllklllgeeiphSG---TVETMSGLV---------------------- 375
Cdd:COG4555 11 YGKVPALKDVSFTAKDGEITGLLGPNG-----------------AGkttLLRMLAGLLkpdsgsilidgedvrkeprear 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 376 --VSYVSQNT---DHL--RGSLTEFARTQGLDGS----RFRTILRKLDVPREQfEKDLADYSSGQKKKVLLAASLCTQAH 444
Cdd:COG4555 74 rqIGVLPDERglyDRLtvRENIRYFAELYGLFDEelkkRIEELIELLGLEEFL-DRRVGELSTGMKKKVALARALVHDPK 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2468763893 445 LYVWDEPLNFIDVISRMQVEDLLLACRP---TLLFVEHD----ARFCDEI 487
Cdd:COG4555 153 VLLLDEPTNGLDVMARRLLREILRALKKegkTVLFSSHImqevEALCDRV 202
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
34-184 |
1.44e-13 |
|
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: 70.51 E-value: 1.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 34 LGFTGRNGRGKTTFLRLLQGEY-PYSGTISASVE-FEYFPYEV-ANLSRTGLEVVREIAPEAEDW-----EIQRELGLLD 105
Cdd:cd03237 28 IGILGPNGIGKTTFIKMLAGVLkPDEGDIEIELDtVSYKPQYIkADYEGTVRDLLSSITKDFYTHpyfktEIAKPLQIEQ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 106 LAERslELPfsSLSNGERTKVLLAAMFLKENAFLLIDEPTNHLDLEGRRKLGSYLAR-----KRGFLLVSHDRAFLDQCV 180
Cdd:cd03237 108 ILDR--EVP--ELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRfaennEKTAFVVEHDIIMIDYLA 183
|
....
gi 2468763893 181 DHIL 184
Cdd:cd03237 184 DRLI 187
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
313-488 |
2.08e-13 |
|
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: 67.66 E-value: 2.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 313 EFRDVAVCYDGRTVCREITFEVLAGERIALQGANGcgkssllklllgeeiphSG---TVETMSGLVVSYvsqntdhlRGS 389
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNG-----------------SGkstLLRAIAGLLKPT--------SGE 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 390 LTefartqgLDGSRFRtilrklDVPREQFEKDLA---DYSSGQKKKVLLAASLCTQAHLYVWDEPLNFIDVISRMQVEDL 466
Cdd:cd00267 56 IL-------IDGKDIA------KLPLEELRRRIGyvpQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLEL 122
|
170 180
....*....|....*....|....*....
gi 2468763893 467 LLACR---PTLLFVEHD----ARFCDEIA 488
Cdd:cd00267 123 LRELAeegRTVIIVTHDpelaELAADRVI 151
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
34-488 |
2.62e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 72.15 E-value: 2.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 34 LGFTGRNGRGKTTFLRLLQGEY-P-----------------YSGTisasvE-FEYFpyevANLSRTGLEVVR-----EIA 89
Cdd:PRK13409 102 TGILGPNGIGKTTAVKILSGELiPnlgdyeeepswdevlkrFRGT-----ElQNYF----KKLYNGEIKVVHkpqyvDLI 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 90 PEAED---WEIQR---ELGLLD-LAERsLEL------PFSSLSNGERTKVLLAAMFLKENAFLLIDEPTNHLDLEGR--- 153
Cdd:PRK13409 173 PKVFKgkvRELLKkvdERGKLDeVVER-LGLenildrDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRlnv 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 154 RKLGSYLARKRGFLLVSHDRAFLDQCVDhilainrtNIEIQRGnfsswwenrrrqdafelarqeklqkdigrltesarra 233
Cdd:PRK13409 252 ARLIRELAEGKYVLVVEHDLAVLDYLAD--------NVHIAYG------------------------------------- 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 234 sgwsdrtEKSKFGV------DKTGAKAADRGFVghkaaklmqRSKSIqRRREEAVE-EKKQllqnlERQEAlavtplpcr 306
Cdd:PRK13409 287 -------EPGAYGVvskpkgVRVGINEYLKGYL---------PEENM-RIRPEPIEfEERP-----PRDES--------- 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 307 AGARLAEFRDVAVCYDGrtvcreitF-------EVLAGERIALQGANGcgkssllklllgeeI--------------PHS 365
Cdd:PRK13409 336 ERETLVEYPDLTKKLGD--------FsleveggEIYEGEVIGIVGPNG--------------IgkttfakllagvlkPDE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 366 GTVETmsGLVVSY----VSQNTDhlrGSLTEFAR--TQGLDGSRFRT-ILRKLDVPReQFEKDLADYSSGQKKKVLLAAS 438
Cdd:PRK13409 394 GEVDP--ELKISYkpqyIKPDYD---GTVEDLLRsiTDDLGSSYYKSeIIKPLQLER-LLDKNVKDLSGGELQRVAIAAC 467
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 2468763893 439 LCTQAHLYVWDEPLNFIDVISRMQVEDlllACR-------PTLLFVEHDARFCDEIA 488
Cdd:PRK13409 468 LSRDADLYLLDEPSAHLDVEQRLAVAK---AIRriaeereATALVVDHDIYMIDYIS 521
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-187 |
4.07e-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: 67.60 E-value: 4.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 4 IDVSNLTFGYEGSpeLIFDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQG-EYPYSGTISASVEfeyfpyEVANLSRTGL 82
Cdd:cd03229 1 LELKNVSKRYGQK--TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGlEEPDSGSILIDGE------DLTDLEDELP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 83 EVVREIAPEAEDWEIQRELGLLDlaerSLELPfssLSNGERTKVLLAAMFLKENAFLLIDEPTNHLDLEGRRKLGSYLAR 162
Cdd:cd03229 73 PLRRRIGMVFQDFALFPHLTVLE----NIALG---LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKS 145
|
170 180 190
....*....|....*....|....*....|
gi 2468763893 163 -----KRGFLLVSHDRAFLDQCVDHILAIN 187
Cdd:cd03229 146 lqaqlGITVVLVTHDLDEAARLADRVVVLR 175
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
313-488 |
4.62e-13 |
|
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: 67.46 E-value: 4.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 313 EFRDVAVCYDGRTVCREITFEVLAGERIALQGANGCGKssllklllgeeiphSGTVETMSGLV------VSYVSQNTDHL 386
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGK--------------STLLKTLAGLLkpssgeILLDGKDLASL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 387 rgSLTEFARTQGLdgsrFRTILRKLDVprEQF-EKDLADYSSGQKKKVLLAASLCTQAHLYVWDEPLNFIDVisRMQVED 465
Cdd:cd03214 67 --SPKELARKIAY----VPQALELLGL--AHLaDRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDI--AHQIEL 136
|
170 180 190
....*....|....*....|....*....|...
gi 2468763893 466 LLLACR------PTLLFVEHD----ARFCDEIA 488
Cdd:cd03214 137 LELLRRlarergKTVVMVLHDlnlaARYADRVI 169
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
3-150 |
1.17e-12 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 67.87 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 3 MIDVSNLTFGYEGSPelIFDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQGE-YPYSGTI-------------------- 61
Cdd:PRK13548 2 MLEARNLSVRLGGRT--LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGElSPDSGEVrlngrpladwspaelarrra 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 62 ----SASVEfeyFPYEVAnlsrtglEVVR------EIAPEAEDWEIQ---RELGLLDLAERSlelpFSSLSNGERTKVLL 128
Cdd:PRK13548 80 vlpqHSSLS---FPFTVE-------EVVAmgraphGLSRAEDDALVAaalAQVDLAHLAGRD----YPQLSGGEQQRVQL 145
|
170 180
....*....|....*....|....*...
gi 2468763893 129 A------AMFLKENAFLLIDEPTNHLDL 150
Cdd:PRK13548 146 ArvlaqlWEPDGPPRWLLLDEPTSALDL 173
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
22-188 |
2.96e-12 |
|
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: 65.76 E-value: 2.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 22 DHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQG-EYPYSGTI---------SASVEFEYFPYE------------------ 73
Cdd:cd03269 17 DDISFSVEKGEIFGLLGPNGAGKTTTIRMILGiILPDSGEVlfdgkpldiAARNRIGYLPEErglypkmkvidqlvylaq 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 74 VANLSRtglevvREIAPEAEDWeIQReLGLLDLAERSLElpfsSLSNGERTKVLLAAMFLKENAFLLIDEPTNHLDLEGR 153
Cdd:cd03269 97 LKGLKK------EEARRRIDEW-LER-LELSEYANKRVE----ELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNV 164
|
170 180 190
....*....|....*....|....*....|....*....
gi 2468763893 154 R----KLGSYLARKRGFLLVSHDRAFLDQCVDHILAINR 188
Cdd:cd03269 165 EllkdVIRELARAGKTVILSTHQMELVEELCDRVLLLNK 203
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
19-150 |
4.04e-12 |
|
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ATP-binding protein components is found as a three gene cassette along with a periplasmic substrate-binding protein (TIGR03868) and a permease (TIGR03869). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this ATP-binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter.
Pssm-ID: 163585 [Multi-domain] Cd Length: 256 Bit Score: 66.38 E-value: 4.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 19 LIFDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQG-EYPYSGTIS-ASVEFEYFPYEVANL--------SRTGLEV-VRE 87
Cdd:TIGR03873 15 LIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGaLRPDAGTVDlAGVDLHGLSRRARARrvalveqdSDTAVPLtVRD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 88 I-------------APEAEDWEIQRE----LGLLDLAERSLelpfSSLSNGERTKVLLAAMFLKENAFLLIDEPTNHLDL 150
Cdd:TIGR03873 95 VvalgriphrslwaGDSPHDAAVVDRalarTELSHLADRDM----STLSGGERQRVHVARALAQEPKLLLLDEPTNHLDV 170
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-192 |
4.82e-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: 65.82 E-value: 4.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 1 MSmIDVSNLTFGYEGSPELifDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQG-EYPYSGTI-----SAS--------VE 66
Cdd:cd03296 1 MS-IEVRNVSKRFGDFVAL--DDVSLDIPSGELVALLGPSGSGKTTLLRLIAGlERPDSGTIlfggeDATdvpvqernVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 67 FEYFPY------EVANLSRTGLEV--VREIAPEAEDWEIQREL----GLLDLAERsleLPfSSLSNGERTKVLLAAMFLK 134
Cdd:cd03296 78 FVFQHYalfrhmTVFDNVAFGLRVkpRSERPPEAEIRAKVHELlklvQLDWLADR---YP-AQLSGGQRQRVALARALAV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2468763893 135 ENAFLLIDEPTNHLDLEGRRKLGSYLARKR-----GFLLVSHDRAFLDQCVDHILAINRTNIE 192
Cdd:cd03296 154 EPKVLLLDEPFGALDAKVRKELRRWLRRLHdelhvTTVFVTHDQEEALEVADRVVVMNKGRIE 216
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
313-488 |
9.30e-12 |
|
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: 65.06 E-value: 9.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 313 EFRDVAVCYDGRTVCREITFEVLAGERIALQGANGCG----------KSSllklllgeeiPHSGTVE-------TMSGL- 374
Cdd:COG1120 3 EAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGkstllralagLLK----------PSSGEVLldgrdlaSLSRRe 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 375 ---VVSYVSQNTDH----------LRG---SLTEFARTQGLDGSRFRTILRKLDVprEQF-EKDLADYSSGQKKKVLLAA 437
Cdd:COG1120 73 larRIAYVPQEPPApfgltvrelvALGrypHLGLFGRPSAEDREAVEEALERTGL--EHLaDRPVDELSGGERQRVLIAR 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2468763893 438 SLCTQAHLYVWDEPLNFIDVISRMQVEDLL--LACRP--TLLFVEHD----ARFCDEIA 488
Cdd:COG1120 151 ALAQEPPLLLLDEPTSHLDLAHQLEVLELLrrLARERgrTVVMVLHDlnlaARYADRLV 209
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-186 |
1.87e-11 |
|
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: 63.66 E-value: 1.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 4 IDVSNLTFGYEGSPELIF--DHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQG-EYPYSGTisasVEFEYFpyEVANLSRT 80
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQalKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGlDRPTSGE----VRVDGT--DISKLSEK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 81 GLEVVR---------------------------EIA----PEAEDWeIQRELGLLDLAERSLELPfSSLSNGERTKVLLA 129
Cdd:cd03255 75 ELAAFRrrhigfvfqsfnllpdltalenvelplLLAgvpkKERRER-AEELLERVGLGDRLNHYP-SELSGGQQQRVAIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2468763893 130 AMFLKENAFLLIDEPTNHLDLEGRRK----LGSyLARKRG--FLLVSHDRAFLDQCvDHILAI 186
Cdd:cd03255 153 RALANDPKIILADEPTGNLDSETGKEvmelLRE-LNKEAGttIVVVTHDPELAEYA-DRIIEL 213
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
313-489 |
2.17e-11 |
|
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: 63.25 E-value: 2.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 313 EFRDVAVCYDGRTVC--REITFEVLAGERIALQGANGCGKSSLLKLLLGEEIPHSGTVeTMSGLVVS------------Y 378
Cdd:cd03225 1 ELKNLSFSYPDGARPalDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEV-LVDGKDLTklslkelrrkvgL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 379 VSQNTDH--LRGSLTE---FA-RTQGLDGS----RFRTILRKLDVpREQFEKDLADYSSGQKKKVLLAASLCTQAHLYVW 448
Cdd:cd03225 80 VFQNPDDqfFGPTVEEevaFGlENLGLPEEeieeRVEEALELVGL-EGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2468763893 449 DEPLNFIDVISRMQVEDLLL---ACRPTLLFVEHDARFCDEIAT 489
Cdd:cd03225 159 DEPTAGLDPAGRRELLELLKklkAEGKTIIIVTHDLDLLLELAD 202
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
20-177 |
5.14e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 62.28 E-value: 5.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 20 IFDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQGEYP-YSGTISASVEFEYFPYEVanlsrTGLEVVREIAPEAEDWEIQ 98
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgTPVAGCVDVPDNQFGREA-----SLIDAIGRKGDFKDAVELL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 99 RELGLLDLAerSLELPFSSLSNGERTKVLLAAMFLKENAFLLIDEPTNHLD----LEGRRKLGSyLARKRG--FLLVSHD 172
Cdd:COG2401 120 NAVGLSDAV--LWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDrqtaKRVARNLQK-LARRAGitLVVATHH 196
|
....*
gi 2468763893 173 RAFLD 177
Cdd:COG2401 197 YDVID 201
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
3-164 |
9.41e-11 |
|
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: 61.61 E-value: 9.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 3 MIDVSNLT--FGYEGSPELIFDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQGEY-PYSGTIS-ASVEFEYFPYEV-ANL 77
Cdd:cd03266 1 MITADALTkrFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLePDAGFATvDGFDVVKEPAEArRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 78 S-----------RTGLEVVREIA------PEAEDWEIQRELGLLDLAErSLELPFSSLSNGERTKVLLAAMFLKENAFLL 140
Cdd:cd03266 81 GfvsdstglydrLTARENLEYFAglyglkGDELTARLEELADRLGMEE-LLDRRVGGFSTGMRQKVAIARALVHDPPVLL 159
|
170 180
....*....|....*....|....
gi 2468763893 141 IDEPTNHLDLEGRRKLGSYLARKR 164
Cdd:cd03266 160 LDEPTTGLDVMATRALREFIRQLR 183
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
4-151 |
2.93e-10 |
|
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: 60.20 E-value: 2.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 4 IDVSNLTFGYEGSPELIFDHVGFQIDSGWKLGFTGRNGRGKTT----FLRLLQgeyPYSGTISasvefeyfpYEVANLSR 79
Cdd:cd03244 3 IEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSlllaLFRLVE---LSSGSIL---------IDGVDISK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 80 TGLEVVRE---IAP------------------EAEDWEIQRELGLLDLAERSLELPF----------SSLSNGERTKVLL 128
Cdd:cd03244 71 IGLHDLRSrisIIPqdpvlfsgtirsnldpfgEYSDEELWQALERVGLKEFVESLPGgldtvveeggENLSVGQRQLLCL 150
|
170 180
....*....|....*....|...
gi 2468763893 129 AAMFLKENAFLLIDEPTNHLDLE 151
Cdd:cd03244 151 ARALLRKSKILVLDEATASVDPE 173
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
4-171 |
3.46e-10 |
|
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: 60.32 E-value: 3.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 4 IDVSNLTFGYEGSPELIFDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQGEY-PYSGTI-------------SASVEFEY 69
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYdVDSGRIlidghdvrdytlaSLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 70 FPYEVANLSRTGLEVVREIAPEAEDWEIQRELGLLDLAERSLELPF----------SSLSNGERTKVLLAAMFLKENAFL 139
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEgydtvigergVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190
....*....|....*....|....*....|....*
gi 2468763893 140 LIDEPTNHLDLEGRRKLG---SYLARKRGFLLVSH 171
Cdd:cd03251 161 ILDEATSALDTESERLVQaalERLMKNRTTFVIAH 195
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-171 |
4.62e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 61.00 E-value: 4.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 4 IDVSNLTFGYEGSPelIFDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQG-EYPYSGTISasVEFEYFPYEvANLSRTGL 82
Cdd:PRK13536 42 IDLAGVSKSYGDKA--VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGmTSPDAGKIT--VLGVPVPAR-ARLARARI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 83 EVVREIAPEAEDWEIQREL-------------------GLLDLA--ERSLELPFSSLSNGERTKVLLAAMFLKENAFLLI 141
Cdd:PRK13536 117 GVVPQFDNLDLEFTVRENLlvfgryfgmstreieavipSLLEFArlESKADARVSDLSGGMKRRLTLARALINDPQLLIL 196
|
170 180 190
....*....|....*....|....*....|....
gi 2468763893 142 DEPTNHLDLEGR----RKLGSYLARKRGFLLVSH 171
Cdd:PRK13536 197 DEPTTGLDPHARhliwERLRSLLARGKTILLTTH 230
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
20-171 |
5.64e-10 |
|
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: 58.91 E-value: 5.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 20 IFDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQG-EYPYSGTIS----ASVEFEYFPYEV-ANLSR--------TGLEVV 85
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGlLRPDSGEVRwngtPLAEQRDEPHENiLYLGHlpglkpelSALENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 86 REIAP--EAEDWEIQRELGLLDLAERSlELPFSSLSNGERTKVLLAAMFLKENAFLLIDEPTNHLDLEGRRKLG----SY 159
Cdd:TIGR01189 95 HFWAAihGGAQRTIEDALAAVGLTGFE-DLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAgllrAH 173
|
170
....*....|..
gi 2468763893 160 LARKRGFLLVSH 171
Cdd:TIGR01189 174 LARGGIVLLTTH 185
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
4-198 |
5.87e-10 |
|
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: 59.55 E-value: 5.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 4 IDVSNLTFGYEGSpELIFDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQGEY-PYSGTI-------------SASVEFEY 69
Cdd:cd03254 3 IEFENVNFSYDEK-KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYdPQKGQIlidgidirdisrkSLRSMIGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 70 FPYEVANLSRTGLEVVREIAPEAEDWEIQR---ELGLLDLAERsleLP----------FSSLSNGERTKVLLAAMFLKEN 136
Cdd:cd03254 82 VLQDTFLFSGTIMENIRLGRPNATDEEVIEaakEAGAHDFIMK---LPngydtvlgenGGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2468763893 137 AFLLIDEPTNHLDLEGRRKLGSYLAR---KRGFLLVSHdRAFLDQCVDHILAINRTNIeIQRGNF 198
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKlmkGRTSIIIAH-RLSTIKNADKILVLDDGKI-IEEGTH 221
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
3-178 |
6.53e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 58.81 E-value: 6.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 3 MIDVSNLTFGYEGSPelIFDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQGEY-PYSGTI---SASVEFEYFPYE----- 73
Cdd:PRK13540 1 MLDVIELDFDYHDQP--LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLnPEKGEIlfeRQSIKKDLCTYQkqlcf 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 74 VANlsRTGLE---VVRE-----IAPEAEDWEIQRELGLLDLaERSLELPFSSLSNGERTKVLLAAMFLKENAFLLIDEPT 145
Cdd:PRK13540 79 VGH--RSGINpylTLREnclydIHFSPGAVGITELCRLFSL-EHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPL 155
|
170 180 190
....*....|....*....|....*....|....*..
gi 2468763893 146 NHLD----LEGRRKLGSYLARKRGFLLVSHDRAFLDQ 178
Cdd:PRK13540 156 VALDelslLTIITKIQEHRAKGGAVLLTSHQDLPLNK 192
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
4-149 |
6.64e-10 |
|
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: 61.85 E-value: 6.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 4 IDVSNLTFGYEGSPELIFDHVGFQIDSGWKLGFTGRNGRGKTT----FLRLL--QGEYPYSGTISASVE-------FEYF 70
Cdd:TIGR01271 1218 MDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTllsaLLRLLstEGEIQIDGVSWNSVTlqtwrkaFGVI 1297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 71 PYEVANLS---RTGLEVVREIAPEaEDWEIQRELGLLDLAER-------SLELPFSSLSNGERTKVLLAAMFLKENAFLL 140
Cdd:TIGR01271 1298 PQKVFIFSgtfRKNLDPYEQWSDE-EIWKVAEEVGLKSVIEQfpdkldfVLVDGGYVLSNGHKQLMCLARSILSKAKILL 1376
|
....*....
gi 2468763893 141 IDEPTNHLD 149
Cdd:TIGR01271 1377 LDEPSAHLD 1385
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-172 |
1.15e-09 |
|
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: 58.25 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 4 IDVSNLTFGYEGSPE--LIFDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQG-EYPYSGTIS------------ASVEF- 67
Cdd:cd03293 1 LEVRNVSKTYGGGGGavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGlERPTSGEVLvdgepvtgpgpdRGYVFq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 68 EY--FPYevanlsRT-------GLEVVREIAPEAEDwEIQRELGLLDLAERSLELPfSSLSNGERTKVLLAAMFLKENAF 138
Cdd:cd03293 81 QDalLPW------LTvldnvalGLELQGVPKAEARE-RAEELLELVGLSGFENAYP-HQLSGGMRQRVALARALAVDPDV 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 2468763893 139 LLIDEPTNHLDLEGRRKLGSYLA---RKRGF--LLVSHD 172
Cdd:cd03293 153 LLLDEPFSALDALTREQLQEELLdiwRETGKtvLLVTHD 191
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
18-171 |
1.63e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 59.05 E-value: 1.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 18 ELIFDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQG-EYPYSGTISASVEfeYFPyEVANLSRTGLEVVREIAPEAEDWE 96
Cdd:PRK13537 20 KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGlTHPDAGSISLCGE--PVP-SRARHARQRVGVVPQFDNLDPDFT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 97 IQREL-------------------GLLDLA--ERSLELPFSSLSNGERTKVLLAAMFLKENAFLLIDEPTNHLDLEGR-- 153
Cdd:PRK13537 97 VRENLlvfgryfglsaaaaralvpPLLEFAklENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARhl 176
|
170 180
....*....|....*....|
gi 2468763893 154 --RKLGSYLARKRGFLLVSH 171
Cdd:PRK13537 177 mwERLRSLLARGKTILLTTH 196
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
313-469 |
1.71e-09 |
|
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: 57.49 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 313 EFRDVAVCYDGRTVCREITFEVLAGERIALQGANGcgkssllklllgeeiphSG--TV-ETMSGLV-------------- 375
Cdd:COG4133 4 EAENLSCRRGERLLFSGLSFTLAAGEALALTGPNG-----------------SGktTLlRILAGLLppsagevlwngepi 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 376 ----------VSYVSQNtDHLRGSLT--E----FARTQGL--DGSRFRTILRKLDVpREQFEKDLADYSSGQKKKVLLAA 437
Cdd:COG4133 67 rdaredyrrrLAYLGHA-DGLKPELTvrEnlrfWAALYGLraDREAIDEALEAVGL-AGLADLPVRQLSAGQKRRVALAR 144
|
170 180 190
....*....|....*....|....*....|..
gi 2468763893 438 SLCTQAHLYVWDEPLNFIDVISRMQVEDLLLA 469
Cdd:COG4133 145 LLLSPAPLWLLDEPFTALDAAGVALLAELIAA 176
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-169 |
2.24e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 59.64 E-value: 2.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 1 MSMIDVSNLTFGYEGSPELIFDHvgFQIDSGWKLGFTGRNGRGKTTFLRLLQGEYP-YSGTISAS------VEFEYFPYE 73
Cdd:PRK10938 1 MSSLQISQGTFRLSDTKTLQLPS--LTLNAGDSWAFVGANGSGKSALARALAGELPlLSGERQSQfshitrLSFEQLQKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 74 VAN---------LSR----TGLEVVREIAPEAEDWEIQREL----GLLDLAERslelPFSSLSNGERTKVLLAAMFLKEN 136
Cdd:PRK10938 79 VSDewqrnntdmLSPgeddTGRTTAEIIQDEVKDPARCEQLaqqfGITALLDR----RFKYLSTGETRKTLLCQALMSEP 154
|
170 180 190
....*....|....*....|....*....|....*
gi 2468763893 137 AFLLIDEPTNHLDLEGRRKLGSYLAR--KRGFLLV 169
Cdd:PRK10938 155 DLLILDEPFDGLDVASRQQLAELLASlhQSGITLV 189
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-192 |
3.09e-09 |
|
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: 57.14 E-value: 3.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 4 IDVSNLTFGYEGSPelIFDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQG-EYPYSGTIS---ASV-------------- 65
Cdd:cd03259 1 LELKGLSKTYGSVR--ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGlERPDSGEILidgRDVtgvpperrnigmvf 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 66 -EFEYFP----YE-VA---NLSRTGLEVVREIAPEAEdweiqRELGLLDLAERSlelPfSSLSNGERTKVLLAAMFLKEN 136
Cdd:cd03259 79 qDYALFPhltvAEnIAfglKLRGVPKAEIRARVRELL-----ELVGLEGLLNRY---P-HELSGGQQQRVALARALAREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2468763893 137 AFLLIDEPTNHLDLEGRRKLGSYLAR-----KRGFLLVSHDRAFLDQCVDHILAINRTNIE 192
Cdd:cd03259 150 SLLLLDEPLSALDAKLREELREELKElqrelGITTIYVTHDQEEALALADRIAVMNEGRIV 210
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
22-172 |
3.86e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 58.17 E-value: 3.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 22 DHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQG-EYPYSGTISasVeFEYFPY--EVANLSRTG----------------- 81
Cdd:COG4586 39 DDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGiLVPTSGEVR--V-LGYVPFkrRKEFARRIGvvfgqrsqlwwdlpaid 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 82 -LEVVREI--APEAEDWEIQREL-GLLDLAERsLELPFSSLSNGERTKVLLAAMFLKENAFLLIDEPTNHLDLEGRRKLG 157
Cdd:COG4586 116 sFRLLKAIyrIPDAEYKKRLDELvELLDLGEL-LDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIR 194
|
170 180
....*....|....*....|
gi 2468763893 158 SYLA---RKRG--FLLVSHD 172
Cdd:COG4586 195 EFLKeynRERGttILLTSHD 214
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
4-151 |
4.37e-09 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 58.64 E-value: 4.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 4 IDVSNLTFGYEGSPElIFDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQGEY-PYSGTIS------ASVEFE-------Y 69
Cdd:COG1132 340 IEFENVSFSYPGDRP-VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYdPTSGRILidgvdiRDLTLEslrrqigV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 70 FPYEVANLSRTglevVRE-IA---PEAEDWEIQRELGLLDLAERSLELPF----------SSLSNGERTKVLLAAMFLKE 135
Cdd:COG1132 419 VPQDTFLFSGT----IREnIRygrPDATDEEVEEAAKAAQAHEFIEALPDgydtvvgergVNLSGGQRQRIAIARALLKD 494
|
170
....*....|....*.
gi 2468763893 136 NAFLLIDEPTNHLDLE 151
Cdd:COG1132 495 PPILILDEATSALDTE 510
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
20-184 |
4.41e-09 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 56.77 E-value: 4.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 20 IFDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQGEYPYS-------GTISASVEFEYFpyevANLSRTGLEVVREIA--- 89
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDsgtvtvrGRVSSLLGLGGG----FNPELTGRENIYLNGrll 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 90 --PEAEDWEIQRELglLDLAE--RSLELPFSSLSNGERTKVLLA-AMFLKENaFLLIDEPTNHLDLEGRRK----LGSYL 160
Cdd:cd03220 113 glSRKEIDEKIDEI--IEFSElgDFIDLPVKTYSSGMKARLAFAiATALEPD-ILLIDEVLAVGDAAFQEKcqrrLRELL 189
|
170 180
....*....|....*....|....
gi 2468763893 161 ARKRGFLLVSHDRAFLDQCVDHIL 184
Cdd:cd03220 190 KQGKTVILVSHDPSSIKRLCDRAL 213
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1-194 |
4.99e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 57.36 E-value: 4.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 1 MSmIDVSNLTFGY-EGSP--ELIFDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQGEY-PYSGTI--------------- 61
Cdd:PRK13637 1 MS-IKIENLTHIYmEGTPfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLkPTSGKIiidgvditdkkvkls 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 62 ----SASVEFEYFPYEV-------------ANLSRTGLEVVREIAPEAEDWEIQRElgllDLAERSlelPFsSLSNGERT 124
Cdd:PRK13637 80 dirkKVGLVFQYPEYQLfeetiekdiafgpINLGLSEEEIENRVKRAMNIVGLDYE----DYKDKS---PF-ELSGGQKR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2468763893 125 KVLLAAMFLKENAFLLIDEPTNHLDLEGRRKLGSYLAR-----KRGFLLVSHDRAFLDQCVDHILAINRTNIEIQ 194
Cdd:PRK13637 152 RVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKElhkeyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQ 226
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
313-487 |
5.57e-09 |
|
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: 56.57 E-value: 5.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 313 EFRDVAVCY-DGRTVCREITFEVLAGERIALQGANGcgkssllklllgeeiphSG--T-VETMSGLV------------- 375
Cdd:COG1122 2 ELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNG-----------------SGksTlLRLLNGLLkptsgevlvdgkd 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 376 ------------VSYVSQNTDH-LrgslteFART-----------QGLDGS----RFRTILRKLDVpreqfeKDLADY-- 425
Cdd:COG1122 65 itkknlrelrrkVGLVFQNPDDqL------FAPTveedvafgpenLGLPREeireRVEEALELVGL------EHLADRpp 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2468763893 426 ---SSGQKKKVLLAASLCTQAHLYVWDEPLNFIDVISRMQVEDLLLACRP---TLLFVEHD----ARFCDEI 487
Cdd:COG1122 133 helSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKegkTVIIVTHDldlvAELADRV 204
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-188 |
6.75e-09 |
|
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: 57.99 E-value: 6.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 3 MIDVSNLTFGYEGSPELIF---DHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQG-EYPYSGTIsasvefEYFPYEVANLS 78
Cdd:COG1123 260 LLEVRNLSKRYPVRGKGGVravDDVSLTLRRGETLGLVGESGSGKSTLARLLLGlLRPTSGSI------LFDGKDLTKLS 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 79 RTGLE----------------------VVREIA---------PEAEDWEIQREL----GL-LDLAERSlelPFsSLSNGE 122
Cdd:COG1123 334 RRSLRelrrrvqmvfqdpysslnprmtVGDIIAeplrlhgllSRAERRERVAELlervGLpPDLADRY---PH-ELSGGQ 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2468763893 123 RTKVLLAAMFLKENAFLLIDEPTNHLDLEGRRKLGSYLA---RKRGF--LLVSHDRAFLDQCVDHILAINR 188
Cdd:COG1123 410 RQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRdlqRELGLtyLFISHDLAVVRYIADRVAVMYD 480
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
20-188 |
7.04e-09 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 56.66 E-value: 7.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 20 IFDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQGEY-PYSGTI--SASVEFEYFPYEVANLSRTGLEVVR--EIAPEAED 94
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVaPDEGVIkrNGKLRIGYVPQKLYLDTTLPLTVNRflRLRPGTKK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 95 WEIQRELGLLDlAERSLELPFSSLSNGERTKVLLAAMFLKENAFLLIDEPTNHLDLEGRRKLGSYLARKR-----GFLLV 169
Cdd:PRK09544 99 EDILPALKRVQ-AGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRreldcAVLMV 177
|
170
....*....|....*....
gi 2468763893 170 SHDRAFLDQCVDHILAINR 188
Cdd:PRK09544 178 SHDLHLVMAKTDEVLCLNH 196
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
18-161 |
8.01e-09 |
|
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: 55.58 E-value: 8.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 18 ELIFDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQG-EYPYSGTIS---ASVEFEYFPYEVANL----------SRTGLE 83
Cdd:cd03231 13 RALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGlSPPLAGRVLlngGPLDFQRDSIARGLLylghapgiktTLSVLE 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2468763893 84 VVREIAPEAEDWEIQRELGLLDLaeRSLE-LPFSSLSNGERTKVLLAAMFLKENAFLLIDEPTNHLDLEGRRKLGSYLA 161
Cdd:cd03231 93 NLRFWHADHSDEQVEEALARVGL--NGFEdRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMA 169
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
14-188 |
8.29e-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: 56.13 E-value: 8.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 14 EGSPELIFDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQGEYPYSGTISASVEF-------EYFPYEVANLSRTGLEV-- 84
Cdd:cd03234 16 WNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTTSGQILFngqprkpDQFQKCVAYVRQDDILLpg 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 85 --VRE------------IAPEAEDWEIQRELGLLDLAERSLELP-FSSLSNGERTKVLLAAMFLKENAFLLIDEPTNHLD 149
Cdd:cd03234 96 ltVREtltytailrlprKSSDAIRKKRVEDVLLRDLALTRIGGNlVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2468763893 150 ----LEGRRKLGSYLARKRGFLLVSHD-RAFLDQCVDHILAINR 188
Cdd:cd03234 176 sftaLNLVSTLSQLARRNRIVILTIHQpRSDLFRLFDRILLLSS 219
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
13-187 |
1.04e-08 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 55.44 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 13 YEGSPEL-IFDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQG-EYPYSGTIS---------ASVEFEY-------FPYEV 74
Cdd:TIGR02211 12 QEGKLDTrVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGlDNPTSGEVLfngqslsklSSNERAKlrnkklgFIYQF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 75 ANL--SRTGLEVV-------REIAPEAED--WEIQRELGLldlAERSLELPfSSLSNGERTKVLLAAMFLKENAFLLIDE 143
Cdd:TIGR02211 92 HHLlpDFTALENVamplligKKSVKEAKEraYEMLEKVGL---EHRINHRP-SELSGGERQRVAIARALVNQPSLVLADE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2468763893 144 PTNHLD-------LEGRRKLGSylARKRGFLLVSHDRAfLDQCVDHILAIN 187
Cdd:TIGR02211 168 PTGNLDnnnakiiFDLMLELNR--ELNTSFLVVTHDLE-LAKKLDRVLEMK 215
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
22-188 |
1.33e-08 |
|
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: 55.52 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 22 DHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQGEY-PYSGTIsasvefeYF---------PYEVANL--SRT--------G 81
Cdd:cd03219 17 DDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLrPTSGSV-------LFdgeditglpPHEIARLgiGRTfqiprlfpE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 82 LEV------------------------VREIAPEAEdwEIQRELGLLDLAERslelPFSSLSNGERTKVLLAAMFLKENA 137
Cdd:cd03219 90 LTVlenvmvaaqartgsglllararreEREARERAE--ELLERVGLADLADR----PAGELSYGQQRRLEIARALATDPK 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2468763893 138 FLLIDEPTNHLDLEGRRKLGSYL----ARKRGFLLVSHDRAFLDQCVDHILAINR 188
Cdd:cd03219 164 LLLLDEPAAGLNPEETEELAELIrelrERGITVLLVEHDMDVVMSLADRVTVLDQ 218
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
4-191 |
1.95e-08 |
|
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: 55.18 E-value: 1.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 4 IDVSNLTFGYEGSPELIFDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQGEY-PYSGTI------SASVEFEYFPYEVAN 76
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYvPENGRVlvdghdLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 77 LSRTGLEVVREIA-------PEAEDWEIQRELGLLDLAERSLELPF----------SSLSNGERTKVLLAAMFLKENAFL 139
Cdd:cd03252 81 VLQENVLFNRSIRdnialadPGMSMERVIEAAKLAGAHDFISELPEgydtivgeqgAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2468763893 140 LIDEPTNHLDLEGRRKLGSYLAR---KRGFLLVSHdRAFLDQCVDHILAINRTNI 191
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDicaGRTVIIIAH-RLSTVKNADRIIVMEKGRI 214
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
22-188 |
2.06e-08 |
|
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: 54.72 E-value: 2.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 22 DHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQG-EYPYSGTISASVEfeyfpyEVANLSRTGLEVVRE------------- 87
Cdd:cd03292 18 DGINISISAGEFVFLVGPSGAGKSTLLKLIYKeELPTSGTIRVNGQ------DVSDLRGRAIPYLRRkigvvfqdfrllp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 88 ---------IAPEAED---WEIQRE----LGLLDLAERSLELPfSSLSNGERTKVLLAAMFLKENAFLLIDEPTNHLDLE 151
Cdd:cd03292 92 drnvyenvaFALEVTGvppREIRKRvpaaLELVGLSHKHRALP-AELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2468763893 152 GRRKLGSYLAR--KRGFLLV--SHDRAFLDQCVDHILAINR 188
Cdd:cd03292 171 TTWEIMNLLKKinKAGTTVVvaTHAKELVDTTRHRVIALER 211
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-208 |
2.69e-08 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 54.76 E-value: 2.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 1 MSMIDVSNLTFGYEGspELIFDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQG-EYPYSGTI---------SASV----- 65
Cdd:PRK11264 1 MSAIEVKNLVKKFHG--QTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLlEQPEAGTIrvgditidtARSLsqqkg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 66 --------------EFEYFPYevanlsRTGLEVVRE----IAPEAEDWEIQRELGLL---DLAERSLELPfSSLSNGERT 124
Cdd:PRK11264 79 lirqlrqhvgfvfqNFNLFPH------RTVLENIIEgpviVKGEPKEEATARARELLakvGLAGKETSYP-RRLSGGQQQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 125 KVLLAAMFLKENAFLLIDEPTNHLDLEgrrKLGSYLA-------RKRGFLLVSHDRAFLDQCVDHILAINRTNIEIQ--- 194
Cdd:PRK11264 152 RVAIARALAMRPEVILFDEPTSALDPE---LVGEVLNtirqlaqEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQgpa 228
|
250
....*....|....
gi 2468763893 195 RGNFSSWWENRRRQ 208
Cdd:PRK11264 229 KALFADPQQPRTRQ 242
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
4-197 |
2.98e-08 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 56.18 E-value: 2.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 4 IDVSNLTFGYEGSPELIFDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQGEYP-YSGTISA-SVEFEyfPYEVANLsRTG 81
Cdd:PRK11176 342 IEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDiDEGEILLdGHDLR--DYTLASL-RNQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 82 LEVVRE------------IAPEAEDW----EIQRE------LGLLDLAERSLELPF----SSLSNGERTKVLLAAMFLKE 135
Cdd:PRK11176 419 VALVSQnvhlfndtiannIAYARTEQysreQIEEAarmayaMDFINKMDNGLDTVIgengVLLSGGQRQRIAIARALLRD 498
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2468763893 136 NAFLLIDEPTNHLDLEGRRKLGSYLA---RKRGFLLVSHDRAFLDQcVDHILAINRTNIeIQRGN 197
Cdd:PRK11176 499 SPILILDEATSALDTESERAIQAALDelqKNRTSLVIAHRLSTIEK-ADEILVVEDGEI-VERGT 561
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-149 |
3.05e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 55.11 E-value: 3.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 3 MIDVSNLT--FGyegsPELIFDHVGFQIDSGWKLGFTGRNGRGKTTFLR-LLQGEYPYSGTISasveFEYFPYEVANLSR 79
Cdd:COG4152 1 MLELKGLTkrFG----DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRiILGILAPDSGEVL----WDGEPLDPEDRRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 80 TG--------------LEVV-----------REIAPEAEDWeIQReLGLLDLAERSLElpfsSLSNGERTKVLLAAMFLK 134
Cdd:COG4152 73 IGylpeerglypkmkvGEQLvylarlkglskAEAKRRADEW-LER-LGLGDRANKKVE----ELSKGNQQKVQLIAALLH 146
|
170
....*....|....*
gi 2468763893 135 ENAFLLIDEPTNHLD 149
Cdd:COG4152 147 DPELLILDEPFSGLD 161
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
311-480 |
4.37e-08 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 53.96 E-value: 4.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 311 LAEFRDVAVCYDGRTVCREITFEVLAGERIALQGANGCGKSSLLKLLLGEEIPHSGTVETMSGLVVSYVSQNTdHLRGSL 390
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKL-YLDTTL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 391 ----TEFARTQGldGSRFRTILRKLDvpREQ----FEKDLADYSSGQKKKVLLAASLCTQAHLYVWDEPLNFIDVISRMQ 462
Cdd:PRK09544 83 pltvNRFLRLRP--GTKKEDILPALK--RVQaghlIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVA 158
|
170 180
....*....|....*....|..
gi 2468763893 463 VEDLLLACRPTL----LFVEHD 480
Cdd:PRK09544 159 LYDLIDQLRRELdcavLMVSHD 180
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
28-183 |
5.94e-08 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 52.57 E-value: 5.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 28 IDSGWKLGFTGRNGRGKTTFLRLLQGEypysgtisasvefeyfpyevanlsrtglevvreIAPEAEDWEiqrelglLDLA 107
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQ---------------------------------LIPNGDNDE-------WDGI 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 108 ERSLELPFSSLSNGERTKVLLAAMFLKENAFLLIDEPTNHLDLEGRRKLGSYLAR-----KRGFLLVSHDRAFLDQCVDH 182
Cdd:cd03222 62 TPVYKPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRlseegKKTALVVEHDLAVLDYLSDR 141
|
.
gi 2468763893 183 I 183
Cdd:cd03222 142 I 142
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
8-183 |
6.02e-08 |
|
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: 53.27 E-value: 6.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 8 NLTFGYEGSPELIFDhvgFQIDSGWKLGFTGRNGRGKTTFLRLLQG-EYPYSGTISAS-VEFEYFP---------YEVAN 76
Cdd:cd03298 4 DKIRFSYGEQPMHFD---LTFAQGEITAIVGPSGSGKSTLLNLIAGfETPQSGRVLINgVDVTAAPpadrpvsmlFQENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 77 L-------SRTGLEVVREIAPEAEDWE-IQRELGLLDLAERSLELPfSSLSNGERTKVLLAAMFLKENAFLLIDEPTNHL 148
Cdd:cd03298 81 LfahltveQNVGLGLSPGLKLTAEDRQaIEVALARVGLAGLEKRLP-GELSGGERQRVALARVLVRDKPVLLLDEPFAAL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2468763893 149 DlEGRRK------LGSYLARKRGFLLVSH---DRAFLDQCVDHI 183
Cdd:cd03298 160 D-PALRAemldlvLDLHAETKMTVLMVTHqpeDAKRLAQRVVFL 202
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
330-453 |
9.15e-08 |
|
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: 51.49 E-value: 9.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 330 ITFEVLAGERIALQGANGCGKSSLLKLLLGEEIPHSGTV-----------ETMSGLVVSYVSQNT---------DHLRGS 389
Cdd:pfam00005 4 VSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTIlldgqdltddeRKSLRKEIGYVFQDPqlfprltvrENLRLG 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2468763893 390 LTEFARTQGLDGSRFRTILRKLDvpREQFEKDLADY-----SSGQKKKVLLAASLCTQAHLYVWDEPLN 453
Cdd:pfam00005 84 LLLKGLSKREKDARAEEALEKLG--LGDLADRPVGErpgtlSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
4-149 |
9.48e-08 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 53.32 E-value: 9.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 4 IDVSNLTFGYEGSPELIFDHVGFQIDSGWKLGFTGRNGRGKTT----FLRLL--QGEYPYSGTISASVE-------FEYF 70
Cdd:cd03289 3 MTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTllsaFLRLLntEGDIQIDGVSWNSVPlqkwrkaFGVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 71 PYEVANLS---RTGLEVVREIAPEaEDWEIQRELGLLDLAER-------SLELPFSSLSNGERTKVLLAAMFLKENAFLL 140
Cdd:cd03289 83 PQKVFIFSgtfRKNLDPYGKWSDE-EIWKVAEEVGLKSVIEQfpgqldfVLVDGGCVLSHGHKQLMCLARSVLSKAKILL 161
|
....*....
gi 2468763893 141 IDEPTNHLD 149
Cdd:cd03289 162 LDEPSAHLD 170
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
321-487 |
1.10e-07 |
|
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: 52.26 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 321 YDGRTVCREITFEVLAGERIALQGANGCGKSSLLKLLLGEEIPHSGTV--------ETMSGLVVSYVSQNTDH------L 386
Cdd:cd03226 10 KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSIllngkpikAKERRKSIGYVMQDVDYqlftdsV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 387 RGSLTEFARTQGLDGSRFRTILRKLDVPREQfEKDLADYSSGQKKKVLLAASLCTQAHLYVWDEPLNFIDVISRMQVEDL 466
Cdd:cd03226 90 REELLLGLKELDAGNEQAETVLKDLDLYALK-ERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGEL 168
|
170 180
....*....|....*....|....*...
gi 2468763893 467 LLACRP---TLLFVEHD----ARFCDEI 487
Cdd:cd03226 169 IRELAAqgkAVIVITHDyeflAKVCDRV 196
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-200 |
1.17e-07 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 54.06 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 4 IDVSNLTFGYEGSPELIFDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQGEY-PYSGTISASVEfeyfP---YEVANLsR 79
Cdd:PRK11160 339 LTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWdPQQGEILLNGQ----PiadYSEAAL-R 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 80 TGLEVV-----------RE----IAPEAED---WEIQRELGLLDLAERslELPFSS--------LSNGERTKVLLAAMFL 133
Cdd:PRK11160 414 QAISVVsqrvhlfsatlRDnlllAAPNASDealIEVLQQVGLEKLLED--DKGLNAwlgeggrqLSGGEQRRLGIARALL 491
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 134 KENAFLLIDEPTNHLDLEGRRKLGSYL---ARKRGFLLVSHDRAFLDQcVDHILAINRTNIeIQRGNFSS 200
Cdd:PRK11160 492 HDAPLLLLDEPTEGLDAETERQILELLaehAQNKTVLMITHRLTGLEQ-FDRICVMDNGQI-IEQGTHQE 559
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
26-149 |
1.30e-07 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 52.63 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 26 FQIDSGWKLGFTGRNGRGKTTFLRLLQGEYPYSGTI---SASVEfEYFPYEVAN--------------------LSRTGL 82
Cdd:PRK03695 17 AEVRAGEILHLVGPNGAGKSTLLARMAGLLPGSGSIqfaGQPLE-AWSAAELARhraylsqqqtppfampvfqyLTLHQP 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2468763893 83 EVVREIAPEAEDWEIQRELGLLDLAERSLelpfSSLSNGERTKVLLAAMFLK-------ENAFLLIDEPTNHLD 149
Cdd:PRK03695 96 DKTRTEAVASALNEVAEALGLDDKLGRSV----NQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSLD 165
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
8-191 |
1.68e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 52.68 E-value: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 8 NLTFGYegSPELIFDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQG-EYPYSGTISASVEF--EYFPYEVA--------N 76
Cdd:PRK10253 12 QLTLGY--GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRlMTPAHGHVWLDGEHiqHYASKEVArrigllaqN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 77 LSRTGLEVVREIA--------PEAEDWEIQ---------RELGLLDLAERSLElpfsSLSNGERTKVLLAAMFLKENAFL 139
Cdd:PRK10253 90 ATTPGDITVQELVargryphqPLFTRWRKEdeeavtkamQATGITHLADQSVD----TLSGGQRQRAWIAMVLAQETAIM 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 140 LIDEPTNHLDLEGR---RKLGSYLARKRGFLL--VSHDrafLDQC---VDHILAINRTNI 191
Cdd:PRK10253 166 LLDEPTTWLDISHQidlLELLSELNREKGYTLaaVLHD---LNQAcryASHLIALREGKI 222
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
313-488 |
1.85e-07 |
|
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: 51.03 E-value: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 313 EFRDVAVCYDGRTVCREITFEVLAGERIALQGANGCGKssllklllgeeiphSGTVETMSGLV------VSYVSQNTDHL 386
Cdd:cd03229 2 ELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGK--------------STLLRCIAGLEepdsgsILIDGEDLTDL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 387 RGSLTEFARTQGL---DGSRFR--TILRKLDVPreqfekdladYSSGQKKKVLLAASLCTQAHLYVWDEPLNFIDVISRM 461
Cdd:cd03229 68 EDELPPLRRRIGMvfqDFALFPhlTVLENIALG----------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRR 137
|
170 180 190
....*....|....*....|....*....|....*
gi 2468763893 462 QVEDLLLACRP----TLLFVEHD----ARFCDEIA 488
Cdd:cd03229 138 EVRALLKSLQAqlgiTVVLVTHDldeaARLADRVV 172
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
22-195 |
2.18e-07 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 51.45 E-value: 2.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 22 DHVGFQIDSGWKLgFTGRNGRGKTTFLRLLqgEYPYSGTISASVEFEYFPYEVANLSRTGLEV-VREIAPEAEDWEIQRE 100
Cdd:cd03240 14 ERSEIEFFSPLTL-IVGQNGAGKTTIIEAL--KYALTGELPPNSKGGAHDPKLIREGEVRAQVkLAFENANGKKYTITRS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 101 LGLLDLA-----ERS---LELPFSSLSNGERTKVLLA-----AMFLKENA-FLLIDEPTNHLDLEGRRK----LGSYLAR 162
Cdd:cd03240 91 LAILENVifchqGESnwpLLDMRGRCSGGEKVLASLIirlalAETFGSNCgILALDEPTTNLDEENIEEslaeIIEERKS 170
|
170 180 190
....*....|....*....|....*....|....*
gi 2468763893 163 KRGFLL--VSHDRAFLDQcVDHILAINRTNIEIQR 195
Cdd:cd03240 171 QKNFQLivITHDEELVDA-ADHIYRVEKDGRQKSR 204
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
8-156 |
2.41e-07 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 53.43 E-value: 2.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 8 NLTFGYEGSPELIFDhVGFQIDSGWKLGFTGRNGRGKTTFLRLLQGEY-PYSGTISASVEfeyfpyEVANLSRTGLE--- 83
Cdd:PRK13657 339 DVSFSYDNSRQGVED-VSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFdPQSGRILIDGT------DIRTVTRASLRrni 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 84 -VV--------REIA-------PEAEDWEIQRELGL---LDLAERSlELPF--------SSLSNGERTKVLLAAMFLKEN 136
Cdd:PRK13657 412 aVVfqdaglfnRSIEdnirvgrPDATDEEMRAAAERaqaHDFIERK-PDGYdtvvgergRQLSGGERQRLAIARALLKDP 490
|
170 180
....*....|....*....|
gi 2468763893 137 AFLLIDEPTNHLDLEGRRKL 156
Cdd:PRK13657 491 PILILDEATSALDVETEAKV 510
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
35-186 |
2.62e-07 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 52.10 E-value: 2.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 35 GFTGRNGRGKTTFLRLL-------QGEYPYSGTISASVEFEYFPYEVANLSRT-----GLeVVREIAP------------ 90
Cdd:PRK10575 41 GLIGHNGSGKSTLLKMLgrhqppsEGEILLDAQPLESWSSKAFARKVAYLPQQlpaaeGM-TVRELVAigrypwhgalgr 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 91 -EAEDWEIQRE----LGLLDLAERSLElpfsSLSNGERTKVLLAAMFLKENAFLLIDEPTNHLDLEGRRK---LGSYLAR 162
Cdd:PRK10575 120 fGAADREKVEEaislVGLKPLAHRLVD----SLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDvlaLVHRLSQ 195
|
170 180
....*....|....*....|....*.
gi 2468763893 163 KRGFLLVS--HDRAFLDQCVDHILAI 186
Cdd:PRK10575 196 ERGLTVIAvlHDINMAARYCDYLVAL 221
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
3-171 |
2.65e-07 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 51.51 E-value: 2.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 3 MIDVSNLTFGYEGSPeLIFDhvgFQIDSGWKLGFTGRNGRGKTTFLRLLQG-EYPYSGTIS---------------ASVE 66
Cdd:PRK10771 1 MLKLTDITWLYHHLP-MRFD---LTVERGERVAILGPSGAGKSTLLNLIAGfLTPASGSLTlngqdhtttppsrrpVSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 67 FE---YFPY-EVAN-----------LSRTGLEVVREIApeaedweiqRELGLLDLAERsleLPfSSLSNGERTKVLLAAM 131
Cdd:PRK10771 77 FQennLFSHlTVAQniglglnpglkLNAAQREKLHAIA---------RQMGIEDLLAR---LP-GQLSGGQRQRVALARC 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2468763893 132 FLKENAFLLIDEPTNHLDLEGRRKLGSYLA-----RKRGFLLVSH 171
Cdd:PRK10771 144 LVREQPILLLDEPFSALDPALRQEMLTLVSqvcqeRQLTLLMVSH 188
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
20-172 |
2.94e-07 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 51.60 E-value: 2.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 20 IFDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQG-EYPYSGTISASvefeyfpyevanlsRTGLEVVRE----IAPEAE- 93
Cdd:PRK11247 27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGlETPSAGELLAG--------------TAPLAEAREdtrlMFQDARl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 94 ----------------DW--EIQRELGLLDLAERSLELPfSSLSNGERTKVLLAAMFLKENAFLLIDEPTNHLDLEGR-- 153
Cdd:PRK11247 93 lpwkkvidnvglglkgQWrdAALQALAAVGLADRANEWP-AALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRie 171
|
170 180
....*....|....*....|..
gi 2468763893 154 -RKLGSYLARKRGF--LLVSHD 172
Cdd:PRK11247 172 mQDLIESLWQQHGFtvLLVTHD 193
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
24-172 |
3.27e-07 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 51.36 E-value: 3.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 24 VGFQIDSGWKLGFTGRNGRGKTTFLRLLQG-EYPYSG----------TISASVEFEY------FPYEVANL--SRTGLEV 84
Cdd:PRK11629 28 VSFSIGEGEMMAIVGSSGSGKSTLLHLLGGlDTPTSGdvifngqpmsKLSSAAKAELrnqklgFIYQFHHLlpDFTALEN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 85 VREI-----APEAEDWEIQRE-LGLLDLAERSLELPfSSLSNGERTKVLLAAMFLKENAFLLIDEPTNHLDLEGRR---K 155
Cdd:PRK11629 108 VAMPlligkKKPAEINSRALEmLAAVGLEHRANHRP-SELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADsifQ 186
|
170
....*....|....*....
gi 2468763893 156 LGSYLARKRG--FLLVSHD 172
Cdd:PRK11629 187 LLGELNRLQGtaFLVVTHD 205
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-172 |
3.38e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 51.53 E-value: 3.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 2 SMIDVSNLTFGYEGSPELIFDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQGEY-PYSGTIS---ASVEFEYFPYEVANL 77
Cdd:PRK13632 6 VMIKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLkPQSGEIKidgITISKENLKEIRKKI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 78 ---------SRTGLEVVREIA--------PEAEDWEIQREL----GLLDLAERSlelPfSSLSNGERTKVLLAAMFLKEN 136
Cdd:PRK13632 86 giifqnpdnQFIGATVEDDIAfglenkkvPPKKMKDIIDDLakkvGMEDYLDKE---P-QNLSGGQKQRVAIASVLALNP 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2468763893 137 AFLLIDEPTNHLDLEGRRKLGSY---LARKRGFLLVS--HD 172
Cdd:PRK13632 162 EIIIFDESTSMLDPKGKREIKKImvdLRKTRKKTLISitHD 202
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-194 |
3.95e-07 |
|
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: 50.96 E-value: 3.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 4 IDVSNLTFGYEGSPelIFDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQGEY-PYSGTIsasvefEYFPYEVANLSRTGL 82
Cdd:cd03261 1 IELRGLTKSFGGRT--VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLrPDSGEV------LIDGEDISGLSEAEL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 83 EVVRE--------------------IA-PEAE-----DWEIqRELGLLDLAERSLE-----LPfSSLSNGERTKVLLA-A 130
Cdd:cd03261 73 YRLRRrmgmlfqsgalfdsltvfenVAfPLREhtrlsEEEI-REIVLEKLEAVGLRgaedlYP-AELSGGMKKRVALArA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2468763893 131 MFLkENAFLLIDEPTNHLD-----------LEGRRKLGSylarkrGFLLVSHDRAFLDQCVDHILAINRTNIEIQ 194
Cdd:cd03261 151 LAL-DPELLLYDEPTAGLDpiasgviddliRSLKKELGL------TSIMVTHDLDTAFAIADRIAVLYDGKIVAE 218
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
30-183 |
4.25e-07 |
|
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: 51.21 E-value: 4.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 30 SGWKLGFTGRNGRGKTTFLRLLQGEY-PYSGTISASVEF-------------EYFpyevANLSRTGLEVVR-----EIAP 90
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLkPNLGKFDDPPDWdeildefrgselqNYF----TKLLEGDVKVIVkpqyvDLIP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 91 EAEDWEIQR------ELGLLDLAERSLEL------PFSSLSNGERTKVLLAAMFLKENAFLLIDEPTNHLDLEGR----R 154
Cdd:cd03236 101 KAVKGKVGEllkkkdERGKLDELVDQLELrhvldrNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRlnaaR 180
|
170 180
....*....|....*....|....*....
gi 2468763893 155 KLGSYLARKRGFLLVSHDRAFLDQCVDHI 183
Cdd:cd03236 181 LIRELAEDDNYVLVVEHDLAVLDYLSDYI 209
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
22-179 |
4.39e-07 |
|
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: 52.50 E-value: 4.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 22 DHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQGEY-PYSGTISASV---------------------------EFEYFPYE 73
Cdd:TIGR03269 301 DNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLePTSGEVNVRVgdewvdmtkpgpdgrgrakryigilhqEYDLYPHR 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 74 --VANLSRT-GLEVVREIAPEAEDWEIQRELGLLDLAERSLELPFSSLSNGERTKVLLAAMFLKENAFLLIDEPTNHLDL 150
Cdd:TIGR03269 381 tvLDNLTEAiGLELPDELARMKAVITLKMVGFDEEKAEEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDP 460
|
170 180 190
....*....|....*....|....*....|....*
gi 2468763893 151 EGRRKLGSYLARKR-----GFLLVSHDRAF-LDQC 179
Cdd:TIGR03269 461 ITKVDVTHSILKAReemeqTFIIVSHDMDFvLDVC 495
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
3-149 |
5.15e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 50.26 E-value: 5.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 3 MIDVSNLTfGYEGsPELIFDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQG-EYPYSGTISASVEFEYFPYEVA------ 75
Cdd:PRK13539 2 MLEGEDLA-CVRG-GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGlLPPAAGTIKLDGGDIDDPDVAEachylg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 76 -------NLS-RTGLEVVREIApEAEDWEIQRELGLLDLAeRSLELPFSSLSNGERTKVLLAAMFLKENAFLLIDEPTNH 147
Cdd:PRK13539 80 hrnamkpALTvAENLEFWAAFL-GGEELDIAAALEAVGLA-PLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAA 157
|
..
gi 2468763893 148 LD 149
Cdd:PRK13539 158 LD 159
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
3-162 |
5.77e-07 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 50.19 E-value: 5.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 3 MIDVSNLTFGYEGspELIFDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQG-EYPYSGTIS------ASVEFEYFpyevA 75
Cdd:PRK13538 1 MLEARNLACERDE--RILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGlARPDAGEVLwqgepiRRQRDEYH----Q 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 76 NL-----------SRTGLEVVR---EIAPEAEDWEIQRELGLLDLAERsLELPFSSLSNGERTKVLLAAMFLKENAFLLI 141
Cdd:PRK13538 75 DLlylghqpgiktELTALENLRfyqRLHGPGDDEALWEALAQVGLAGF-EDVPVRQLSAGQQRRVALARLWLTRAPLWIL 153
|
170 180
....*....|....*....|.
gi 2468763893 142 DEPTNHLDLEGRRKLGSYLAR 162
Cdd:PRK13538 154 DEPFTAIDKQGVARLEALLAQ 174
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3-156 |
6.88e-07 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 51.37 E-value: 6.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 3 MIDVSNLTFGYEGSPELifDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQG-EYPYSGTIS------ASV---------- 65
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAV--DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGfEQPTAGQIMldgvdlSHVppyqrpinmm 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 66 --EFEYFPYevanlsrtgLEVVREIA--------PEAE-DWEIQRELGLLDLAERSLELPfSSLSNGERTKVLLAAMFLK 134
Cdd:PRK11607 97 fqSYALFPH---------MTVEQNIAfglkqdklPKAEiASRVNEMLGLVHMQEFAKRKP-HQLSGGQRQRVALARSLAK 166
|
170 180
....*....|....*....|..
gi 2468763893 135 ENAFLLIDEPTNHLDLEGRRKL 156
Cdd:PRK11607 167 RPKLLLLDEPMGALDKKLRDRM 188
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-149 |
7.87e-07 |
|
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: 51.73 E-value: 7.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 4 IDVSNLTFGYEGSPELifDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQG--EY-PYSGTISASV--------------- 65
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVL--KNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYePTSGRIIYHValcekcgyverpskv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 66 ---------EFEYFPYEVANLSR------------------------TGLEVVREIAPEAE---DWEIQRELGLLD---L 106
Cdd:TIGR03269 79 gepcpvcggTLEPEEVDFWNLSDklrrrirkriaimlqrtfalygddTVLDNVLEALEEIGyegKEAVGRAVDLIEmvqL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2468763893 107 AERSLELPfSSLSNGERTKVLLAAMFLKENAFLLIDEPTNHLD 149
Cdd:TIGR03269 159 SHRITHIA-RDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLD 200
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-172 |
8.39e-07 |
|
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: 49.87 E-value: 8.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 4 IDVSNLTFGYEGspELIFDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQG------EYPYSGTIsasvefEYFPYEVANL 77
Cdd:cd03260 1 IELRDLNVYYGD--KHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndlipGAPDEGEV------LLDGKDIYDL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 78 SRTGLEVVREIA--------------------PEAEDweIQRELGLLDLAERSLE-----------LPFSSLSNGERTKV 126
Cdd:cd03260 73 DVDVLELRRRVGmvfqkpnpfpgsiydnvaygLRLHG--IKLKEELDERVEEALRkaalwdevkdrLHALGLSGGQQQRL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2468763893 127 LLA---AMflkENAFLLIDEPTNHLDLEGRRK---LGSYLARKRGFLLVSHD 172
Cdd:cd03260 151 CLAralAN---EPEVLLLDEPTSALDPISTAKieeLIAELKKEYTIVIVTHN 199
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
18-189 |
8.68e-07 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 51.35 E-value: 8.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 18 ELIFDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQGEYPY-SGTIS----ASVEF----EYFPyeVANLsrtglevvREI 88
Cdd:COG4178 376 RPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYgSGRIArpagARVLFlpqrPYLP--LGTL--------REA 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 89 ------APEAEDWEIQ---RELGLLDLAER-SLELPFSS-LSNGERTKVLLAAMFLKENAFLLIDEPTNHLDLEGRRKLG 157
Cdd:COG4178 446 llypatAEAFSDAELRealEAVGLGHLAERlDEEADWDQvLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALY 525
|
170 180 190
....*....|....*....|....*....|....*
gi 2468763893 158 SYLARKR---GFLLVSHdRAFLDQCVDHILAINRT 189
Cdd:COG4178 526 QLLREELpgtTVISVGH-RSTLAAFHDRVLELTGD 559
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
4-151 |
1.12e-06 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 49.33 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 4 IDVSNLTFGYegSPEL--IFDHVGFQIDSGWKLGFTGRNGRGKTT----FLRLLQGEypySGTISasvefeyfpYEVANL 77
Cdd:cd03369 7 IEVENLSVRY--APDLppVLKNVSFKVKAGEKIGIVGRTGAGKSTlilaLFRFLEAE---EGKIE---------IDGIDI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 78 SRTGLEVVRE---IAP------------------EAEDWEIqreLGLLDLAERSLelpfsSLSNGERTKVLLAAMFLKEN 136
Cdd:cd03369 73 STIPLEDLRSsltIIPqdptlfsgtirsnldpfdEYSDEEI---YGALRVSEGGL-----NLSQGQRQLLCLARALLKRP 144
|
170
....*....|....*
gi 2468763893 137 AFLLIDEPTNHLDLE 151
Cdd:cd03369 145 RVLVLDEATASIDYA 159
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
34-172 |
1.16e-06 |
|
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: 49.22 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 34 LGFTGRNGRGKTTFLRLLQG-EYPYSGTISAS------------------------VEFEYFPyevaNLS-RTGLEVVRE 87
Cdd:cd03297 26 TGIFGASGAGKSTLLRCIAGlEKPDGGTIVLNgtvlfdsrkkinlppqqrkiglvfQQYALFP----HLNvRENLAFGLK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 88 IAPEAEDWEIQRE-LGLLDLaERSLELPFSSLSNGERTKVLLAAMFLKENAFLLIDEPTNHLDLEGRRKLGSYLAR-KRG 165
Cdd:cd03297 102 RKRNREDRISVDElLDLLGL-DHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQiKKN 180
|
170
....*....|.
gi 2468763893 166 F----LLVSHD 172
Cdd:cd03297 181 LnipvIFVTHD 191
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
3-191 |
1.46e-06 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 49.62 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 3 MIDVSNLTFGYEGSPELifdhVGFQIDSGWK--LGFTGRNGRGKTTF-------LRLLQGEYPYSGtisasvefeyfpyE 73
Cdd:PRK13638 1 MLATSDLWFRYQDEPVL----KGLNLDFSLSpvTGLVGANGCGKSTLfmnlsglLRPQKGAVLWQG-------------K 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 74 VANLSRTGLEVVRE-IAPEAEDWEIQ--------------RELG---------------LLDlAERSLELPFSSLSNGER 123
Cdd:PRK13638 64 PLDYSKRGLLALRQqVATVFQDPEQQifytdidsdiafslRNLGvpeaeitrrvdealtLVD-AQHFRHQPIQCLSHGQK 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2468763893 124 TKVLLAAMFLKENAFLLIDEPTNHLDLEGRRKLGSYLAR----KRGFLLVSHDRAFLDQCVDHILAINRTNI 191
Cdd:PRK13638 143 KRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRivaqGNHVIISSHDIDLIYEISDAVYVLRQGQI 214
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
2-188 |
2.35e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 48.98 E-value: 2.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 2 SMIDVSNLTFGYEGSPELIFDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQG-EYPYSGTISasveFEYFPYEVANLSRT 80
Cdd:PRK13648 6 SIIVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGiEKVKSGEIF----YNNQAITDDNFEKL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 81 --------------------------GLE-------VVREIAPEAedweiQRELGLLDLAERSLElpfsSLSNGERTKVL 127
Cdd:PRK13648 82 rkhigivfqnpdnqfvgsivkydvafGLEnhavpydEMHRRVSEA-----LKQVDMLERADYEPN----ALSGGQKQRVA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2468763893 128 LAAMFLKENAFLLIDEPTNHLDLEGRRKLGSYLARKRG-----FLLVSHDrafLDQCV--DHILAINR 188
Cdd:PRK13648 153 IAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSehnitIISITHD---LSEAMeaDHVIVMNK 217
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
321-488 |
2.59e-06 |
|
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: 48.52 E-value: 2.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 321 YDGRTVCREITFEVLAGERIALQGANGCGKSSLLKLLLGEEIPHSGTVeTMSGL-----------VVSYVSQNT---DHL 386
Cdd:cd03265 10 YGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRA-TVAGHdvvreprevrrRIGIVFQDLsvdDEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 387 RG--SLTEFARTQGLDGS----RFRTILRKLDVpREQFEKDLADYSSGQKKKVLLAASLCTQAHLYVWDEPLNFIDVISR 460
Cdd:cd03265 89 TGweNLYIHARLYGVPGAerreRIDELLDFVGL-LEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTR 167
|
170 180 190
....*....|....*....|....*....|....*.
gi 2468763893 461 MQV----EDLLLACRPTLLFVEHDA----RFCDEIA 488
Cdd:cd03265 168 AHVweyiEKLKEEFGMTILLTTHYMeeaeQLCDRVA 203
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-156 |
2.60e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 48.96 E-value: 2.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 1 MSMIDVSNLTFGY-EGSPELIFDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQGEY-PYSGTISASVEfEYFPYEVANLS 78
Cdd:PRK13650 2 SNIIEVKNLTFKYkEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLeAESGQIIIDGD-LLTEENVWDIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 79 R-------------TGLEVVREIAPEAEDWEIQRE------------LGLLDLAERSlelPfSSLSNGERTKVLLAAMFL 133
Cdd:PRK13650 81 HkigmvfqnpdnqfVGATVEDDVAFGLENKGIPHEemkervnealelVGMQDFKERE---P-ARLSGGQKQRVAIAGAVA 156
|
170 180
....*....|....*....|...
gi 2468763893 134 KENAFLLIDEPTNHLDLEGRRKL 156
Cdd:PRK13650 157 MRPKIIILDEATSMLDPEGRLEL 179
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-186 |
2.67e-06 |
|
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: 47.42 E-value: 2.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 4 IDVSNLTFGYEGSPELifDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQGEY-PYSGTISasVEFEyfpyEVANLS---- 78
Cdd:cd03216 1 LELRGITKRFGGVKAL--DGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYkPDSGEIL--VDGK----EVSFASprda 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 79 -RTGLEVVreiapeaedweiqrelglldlaerslelpfSSLSNGERTKVLLAAMFLKENAFLLIDEPTNHLDLEGRRKLG 157
Cdd:cd03216 73 rRAGIAMV------------------------------YQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLF 122
|
170 180 190
....*....|....*....|....*....|...
gi 2468763893 158 SYLARKR----GFLLVSHDrafldqcVDHILAI 186
Cdd:cd03216 123 KVIRRLRaqgvAVIFISHR-------LDEVFEI 148
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
26-189 |
2.77e-06 |
|
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: 47.53 E-value: 2.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 26 FQIDSGWKLGFTGRNGRGKTTFLRLLQGEYPY-SGTIsasvefeyfpyevanlsrtglevvreIAPEAEDweiqrelgLL 104
Cdd:cd03223 22 FEIKPGDRLLITGPSGTGKSSLFRALAGLWPWgSGRI--------------------------GMPEGED--------LL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 105 DLAERSLeLPFSSL------------SNGERTKVLLAAMFLKENAFLLIDEPTNHLDLEGRRKLgsY-LARKRGFLLVS- 170
Cdd:cd03223 68 FLPQRPY-LPLGTLreqliypwddvlSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRL--YqLLKELGITVISv 144
|
170 180
....*....|....*....|
gi 2468763893 171 -HdRAFLDQCVDHILAINRT 189
Cdd:cd03223 145 gH-RPSLWKFHDRVLDLDGE 163
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
20-176 |
3.03e-06 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 48.54 E-value: 3.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 20 IFDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQG-EYPYSGTIS-----ASvefeyfPYEVA---NLSRTGLEVVR---- 86
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGiLEPTSGRVEvngrvSA------LLELGagfHPELTGRENIYlngr 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 87 -------EIApEAEDwEIqrelglLDLAE--RSLELPFSSLSNGERTKVLLAAMFLKENAFLLIDEPTNHLDLEGRRK-- 155
Cdd:COG1134 115 llglsrkEID-EKFD-EI------VEFAElgDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKcl 186
|
170 180
....*....|....*....|...
gi 2468763893 156 --LGSYLARKRGFLLVSHDRAFL 176
Cdd:COG1134 187 arIRELRESGRTVIFVSHSMGAV 209
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
24-144 |
3.05e-06 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 48.42 E-value: 3.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 24 VGFQIDSGWKLGFTGRNGRGKTTFLRLLQGEY-PYSGTIS--------------ASVEFEYFPYEVA---NLS-RTGLEV 84
Cdd:TIGR04406 20 VSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVrPDAGKILidgqdithlpmherARLGIGYLPQEASifrKLTvEENIMA 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2468763893 85 VREIAPEAEDWEIQRELGLLdLAE----RSLELPFSSLSNGERTKVLLAAMFLKENAFLLIDEP 144
Cdd:TIGR04406 100 VLEIRKDLDRAEREERLEAL-LEEfqisHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEP 162
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
295-487 |
3.21e-06 |
|
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: 49.59 E-value: 3.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 295 QEALAVTPLPC-------RAGARLAEFRDVAVCYDGRT-VCREITFEVLAGERIALQGANGCGKSSLLKLLLGEEIPHSG 366
Cdd:TIGR02857 298 FAVLDAAPRPLagkapvtAAPASSLEFSGVSVAYPGRRpALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEG 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 367 TV----ETMSGLV-------VSYVSQNTDHLRGSLTE---FARtQGLDGSRFRTILRKLDVprEQFEKDL---------- 422
Cdd:TIGR02857 378 SIavngVPLADADadswrdqIAWVPQHPFLFAGTIAEnirLAR-PDASDAEIREALERAGL--DEFVAALpqgldtpige 454
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2468763893 423 --ADYSSGQKKKVLLAASLCTQAHLYVWDEPLNFIDVISRMQVEDLL--LACRPTLLFVEHD---ARFCDEI 487
Cdd:TIGR02857 455 ggAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALraLAQGRTVLLVTHRlalAALADRI 526
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
4-151 |
3.29e-06 |
|
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: 48.30 E-value: 3.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 4 IDVSNLTFGYEGSPE-LIFDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQGEY-PYSGTI-------------SASVEFE 68
Cdd:cd03249 1 IEFKNVSFRYPSRPDvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYdPTSGEIlldgvdirdlnlrWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 69 YFPYEVANLSRTGLEVVREIAPEAEDWEIQRELGLLDLAERSLELPF----------SSLSNGERTKVLLAAMFLKENAF 138
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDgydtlvgergSQLSGGQKQRIAIARALLRNPKI 160
|
170
....*....|...
gi 2468763893 139 LLIDEPTNHLDLE 151
Cdd:cd03249 161 LLLDEATSALDAE 173
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
313-487 |
3.64e-06 |
|
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: 46.99 E-value: 3.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 313 EFRDVAVCYDGRT--VCREITFEVLAGERIALQGANGC-------------GkssllklllgeeiPHSGTVeTMSGL--- 374
Cdd:cd03228 2 EFKNVSFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSgkstllklllrlyD-------------PTSGEI-LIDGVdlr 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 375 ---------VVSYVSQNTdHLrgsltefartqgLDGSRFRTILrkldvpreqfekdladySSGQKKKVLLAASLCTQAHL 445
Cdd:cd03228 68 dldleslrkNIAYVPQDP-FL------------FSGTIRENIL-----------------SGGQRQRIAIARALLRDPPI 117
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2468763893 446 YVWDEPLNFIDVISRMQVEDLL--LACRPTLLFVEHD---ARFCDEI 487
Cdd:cd03228 118 LILDEATSALDPETEALILEALraLAKGKTVIVIAHRlstIRDADRI 164
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
2-150 |
4.88e-06 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 48.09 E-value: 4.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 2 SMIDVSNLTFGYEGSPelIFDHVGFQIDSGWKLGFTGRNGRGKTTFL----RLLQgeyPYSGTISASVEfEYFPYEVANL 77
Cdd:PRK11231 1 MTLRTENLTVGYGTKR--ILNDLSLSLPTGKITALIGPNGCGKSTLLkcfaRLLT---PQSGTVFLGDK-PISMLSSRQL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 78 SRT------------GLEVVREIA----P--------EAED-----WEIQReLGLLDLAERslelPFSSLSNGERTKVLL 128
Cdd:PRK11231 75 ARRlallpqhhltpeGITVRELVAygrsPwlslwgrlSAEDnarvnQAMEQ-TRINHLADR----RLTDLSGGQRQRAFL 149
|
170 180
....*....|....*....|...
gi 2468763893 129 AaMFLKENA-FLLIDEPTNHLDL 150
Cdd:PRK11231 150 A-MVLAQDTpVVLLDEPTTYLDI 171
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-192 |
5.40e-06 |
|
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: 47.62 E-value: 5.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 4 IDVSNLTFGYEGSPELifDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQG-EYPYSGTI----------------SASVE 66
Cdd:cd03300 1 IELENVSKFYGGFVAL--DGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGfETPTSGEIlldgkditnlpphkrpVNTVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 67 FEY-------------FPYEVANLSRTglEVVREIApeaedwEIQRELGLLDLAERSLelpfSSLSNGERTKVLLAAMFL 133
Cdd:cd03300 79 QNYalfphltvfeniaFGLRLKKLPKA--EIKERVA------EALDLVQLEGYANRKP----SQLSGGQQQRVAIARALV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2468763893 134 KENAFLLIDEPTNHLDLEGRRKLG---SYLARKRG--FLLVSHDRAFLDQCVDHILAINRTNIE 192
Cdd:cd03300 147 NEPKVLLLDEPLGALDLKLRKDMQlelKRLQKELGitFVFVTHDQEEALTMSDRIAVMNKGKIQ 210
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
22-150 |
7.03e-06 |
|
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: 48.67 E-value: 7.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 22 DHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQGEYPysGTISASVEFEYFPYEVANLS---RTGLEVVRE------IAP-- 90
Cdd:TIGR02633 277 DDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYP--GKFEGNVFINGKPVDIRNPAqaiRAGIAMVPEdrkrhgIVPil 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 91 ----------------------EAEDWEIQRELGLLDLAERSLELPFSSLSNGERTKVLLAAMFLKENAFLLIDEPTNHL 148
Cdd:TIGR02633 355 gvgknitlsvlksfcfkmridaAAELQIIGSAIQRLKVKTASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGV 434
|
..
gi 2468763893 149 DL 150
Cdd:TIGR02633 435 DV 436
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
313-487 |
8.37e-06 |
|
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: 46.89 E-value: 8.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 313 EFRDVAVCYDGRTVCREITFEVLAGERIALQGANGCGKSSLLKLLLGEEIPHSGTVEtMSGLVVSYVSQNT-DHL---RG 388
Cdd:cd03269 2 EVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVL-FDGKPLDIAARNRiGYLpeeRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 389 ---------SLTEFARTQGLDGS----RFRTILRKLDVpREQFEKDLADYSSGQKKKVLLAASLCTQAHLYVWDEPLNFI 455
Cdd:cd03269 81 lypkmkvidQLVYLAQLKGLKKEearrRIDEWLERLEL-SEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGL 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 2468763893 456 DVISRMQVEDLLLACR---PTLLFVEHD----ARFCDEI 487
Cdd:cd03269 160 DPVNVELLKDVIRELAragKTVILSTHQmelvEELCDRV 198
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
311-488 |
8.46e-06 |
|
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: 47.12 E-value: 8.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 311 LAEFRDVAVCYDGR----TVCREITFEVLAGERIALQGANGCGKSSLLKLLLGEEIPHSGTVE-------TMS------- 372
Cdd:cd03257 1 LLEVKNLSVSFPTGggsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIfdgkdllKLSrrlrkir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 373 GLVVSYVSQN-------------------TDHLRGSLTEFARTQGLDgsrfrtILRKLDVPREQFEKDLADYSSGQKKKV 433
Cdd:cd03257 81 RKEIQMVFQDpmsslnprmtigeqiaeplRIHGKLSKKEARKEAVLL------LLVGVGLPEEVLNRYPHELSGGQRQRV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2468763893 434 LLAASLCTQAHLYVWDEPLNFIDVISRMQVEDLLLACRP----TLLFVEHD----ARFCDEIA 488
Cdd:cd03257 155 AIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelglTLLFITHDlgvvAKIADRVA 217
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
14-183 |
1.00e-05 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 46.63 E-value: 1.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 14 EGSPELIFDHVGFQIDSG--------------WKLgFTGRNGRGKTTFLRLL-------QGEYPYSGTISASVEFEYFPY 72
Cdd:PRK10247 3 ENSPLLQLQNVGYLAGDAkilnnisfslrageFKL-ITGPSGCGKSTLLKIVaslisptSGTLLFEGEDISTLKPEIYRQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 73 EVANLSRT----GLEV---------VREIAPEAEdwEIQRELGLLDLAERSLELPFSSLSNGERTKVLLAA--MFLKEna 137
Cdd:PRK10247 82 QVSYCAQTptlfGDTVydnlifpwqIRNQQPDPA--IFLDDLERFALPDTILTKNIAELSGGEKQRISLIRnlQFMPK-- 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2468763893 138 FLLIDEPTNHLDLEGRRKLGS---YLARKRGF--LLVSHDRAFLDQCVDHI 183
Cdd:PRK10247 158 VLLLDEITSALDESNKHNVNEiihRYVREQNIavLWVTHDKDEINHADKVI 208
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
299-487 |
1.17e-05 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 47.52 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 299 AVTPLPCRAGARLAEFRDVAVCYDGRTVCREITFEVLAGERIALQGANGCGKSSLLKLLLGEEIPHSGTVETMSGLV--- 375
Cdd:PRK13536 29 AKASIPGSMSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVpar 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 376 -------VSYVSQ--NTDH---LRGSLTEFARTQGLDGSRFRTILRK-LDVPREQFEKD--LADYSSGQKKKVLLAASLC 440
Cdd:PRK13536 109 arlararIGVVPQfdNLDLeftVRENLLVFGRYFGMSTREIEAVIPSlLEFARLESKADarVSDLSGGMKRRLTLARALI 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2468763893 441 TQAHLYVWDEPLNFIDVISRMQV-EDL--LLACRPTLL----FVEHDARFCDEI 487
Cdd:PRK13536 189 NDPQLLILDEPTTGLDPHARHLIwERLrsLLARGKTILltthFMEEAERLCDRL 242
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
21-188 |
1.39e-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: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 21 FDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQGEY-PYSGTISasvefeyfpyevanlsRTGLEVVREIAPEAedweIQR 99
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRpPASGEIT----------------LDGKPVTRRSPRDA----IRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 100 ELGLL--DLAERSLELPFS---------SLSNGERTKVLLAAMFLKENAFLLIDEPTNHLDLEGR----RKLGSYLARKR 164
Cdd:cd03215 76 GIAYVpeDRKREGLVLDLSvaenialssLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKaeiyRLIRELADAGK 155
|
170 180
....*....|....*....|....
gi 2468763893 165 GFLLVSHDRAFLDQCVDHILAINR 188
Cdd:cd03215 156 AVLLISSELDELLGLCDRILVMYE 179
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
3-156 |
1.69e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 46.62 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 3 MIDVSNLTFGYEGSPEL-IFDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQGEY-PYSGTIsaSVEFEYFPYE-VANLSR 79
Cdd:PRK13642 4 ILEVENLVFKYEKESDVnQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFeEFEGKV--KIDGELLTAEnVWNLRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 80 -------------TGLEVVREIAPEAEDWEIQRE------------LGLLDLAERSLelpfSSLSNGERTKVLLAAMFLK 134
Cdd:PRK13642 82 kigmvfqnpdnqfVGATVEDDVAFGMENQGIPREemikrvdeallaVNMLDFKTREP----ARLSGGQKQRVAVAGIIAL 157
|
170 180
....*....|....*....|..
gi 2468763893 135 ENAFLLIDEPTNHLDLEGRRKL 156
Cdd:PRK13642 158 RPEIIILDESTSMLDPTGRQEI 179
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
4-185 |
1.73e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 47.32 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 4 IDVSNLTFGYEGSPelIFDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQGEYP--YS----------------------- 58
Cdd:PRK10938 261 IVLNNGVVSYNDRP--ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPqgYSndltlfgrrrgsgetiwdikkhi 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 59 GTISASVEFEYfpyevaNLSRTGLEV----------VREIAPEAEDWEIQRELGLLDLAERSLELPFSSLSNGERTKVLL 128
Cdd:PRK10938 339 GYVSSSLHLDY------RVSTSVRNVilsgffdsigIYQAVSDRQQKLAQQWLDILGIDKRTADAPFHSLSWGQQRLALI 412
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2468763893 129 AAMFLKENAFLLIDEPTNHLDLEGRRKLGSYLARKRG-----FLLVSHDRAFLDQCVDHILA 185
Cdd:PRK10938 413 VRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISegetqLLFVSHHAEDAPACITHRLE 474
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
3-172 |
1.87e-05 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 46.23 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 3 MIDVSNLTFGYEGSPELifDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQGEYPYS-GTISAS------------VEFEY 69
Cdd:PRK11248 1 MLQISHLYADYGGKPAL--EDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQhGSITLDgkpvegpgaergVVFQN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 70 ---FPYE--VANLSrTGLEVVReiAPEAEDWEIQRE-LGLLDLAERSLELPFsSLSNGERTKVLLAAMFLKENAFLLIDE 143
Cdd:PRK11248 79 eglLPWRnvQDNVA-FGLQLAG--VEKMQRLEIAHQmLKKVGLEGAEKRYIW-QLSGGQRQRVGIARALAANPQLLLLDE 154
|
170 180 190
....*....|....*....|....*....|....
gi 2468763893 144 PTNHLDLEGRRKLGSYLAR-----KRGFLLVSHD 172
Cdd:PRK11248 155 PFGALDAFTREQMQTLLLKlwqetGKQVLLITHD 188
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-191 |
1.89e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 46.33 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 1 MSMIDVSNLTFGYEGSPELIfDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQGEY-PYSGTISASVEfeyfPYEVANLSR 79
Cdd:PRK13652 1 MHLIETRDLCYSYSGSKEAL-NNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILkPTSGSVLIRGE----PITKENIRE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 80 ----TGL------------EVVREIA---------PEAEDWEIQRELGLLDLAERSLELPfSSLSNGERTKVLLAAMFLK 134
Cdd:PRK13652 76 vrkfVGLvfqnpddqifspTVEQDIAfgpinlgldEETVAHRVSSALHMLGLEELRDRVP-HHLSGGEKKRVAIAGVIAM 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2468763893 135 ENAFLLIDEPTNHLDLEGRRKLGSY---LARKRGFLLV--SHDRAFLDQCVDHILAINRTNI 191
Cdd:PRK13652 155 EPQVLVLDEPTAGLDPQGVKELIDFlndLPETYGMTVIfsTHQLDLVPEMADYIYVMDKGRI 216
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
4-156 |
2.53e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 45.89 E-value: 2.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 4 IDVSNLTFGYE-GSP---ELIFDhVGFQIDSGWKLGFTGRNGRGKTTFLRLLQGEY-PYSGTISAsvefeyFPYEVANLS 78
Cdd:PRK13649 3 INLQNVSYTYQaGTPfegRALFD-VNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHvPTQGSVRV------DDTLITSTS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 79 RT----------GL------------EVVREIA----------PEAEdwEIQRE-LGLLDLAERSLEL-PFSsLSNGERT 124
Cdd:PRK13649 76 KNkdikqirkkvGLvfqfpesqlfeeTVLKDVAfgpqnfgvsqEEAE--ALAREkLALVGISESLFEKnPFE-LSGGQMR 152
|
170 180 190
....*....|....*....|....*....|..
gi 2468763893 125 KVLLAAMFLKENAFLLIDEPTNHLDLEGRRKL 156
Cdd:PRK13649 153 RVAIAGILAMEPKILVLDEPTAGLDPKGRKEL 184
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
264-480 |
2.78e-05 |
|
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: 46.58 E-value: 2.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 264 AAKLMQRSKSIQRRREEAVEekkqllQNLERQEALAVTPLPCRAGARLAEFRDVAVCYDG-RTVCREITFEVLAGERIAL 342
Cdd:TIGR02868 293 AAQQLTRVRAAAERIVEVLD------AAGPVAEGSAPAAGAVGLGKPTLELRDLSAGYPGaPPVLDGVSLDLPPGERVAI 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 343 QGANGCGKSSLLKLLLGEEIPHSGTVeTMSGLVVSYVSQNTDHLRGSLteFARTQGLDGSRFRTILR--KLDVPREQFEK 420
Cdd:TIGR02868 367 LGPSGSGKSTLLATLAGLLDPLQGEV-TLDGVPVSSLDQDEVRRRVSV--CAQDAHLFDTTVRENLRlaRPDATDEELWA 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 421 -----DLADY-------------------SSGQKKKVLLAASLCTQAHLYVWDEPLNFIDVISRMQVEDLLLACRP--TL 474
Cdd:TIGR02868 444 alervGLADWlralpdgldtvlgeggarlSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSgrTV 523
|
....*.
gi 2468763893 475 LFVEHD 480
Cdd:TIGR02868 524 VLITHH 529
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-191 |
3.02e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 45.95 E-value: 3.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 2 SMIDVSNLTFGYEGSPELIFDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQG-----EYPYS------------------ 58
Cdd:PRK13640 4 NIVEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGlllpdDNPNSkitvdgitltaktvwdir 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 59 ---GTISASVEFEYFPYEVANLSRTGLEvvREIAPEAEDWEIQR----ELGLLDLAERSlelPfSSLSNGERTKVLLAAM 131
Cdd:PRK13640 84 ekvGIVFQNPDNQFVGATVGDDVAFGLE--NRAVPRPEMIKIVRdvlaDVGMLDYIDSE---P-ANLSGGQKQRVAIAGI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2468763893 132 FLKENAFLLIDEPTNHLDLEGRR---KLGSYLARKRGFLLVS--HDrafLDQCV--DHILAINRTNI 191
Cdd:PRK13640 158 LAVEPKIIILDESTSMLDPAGKEqilKLIRKLKKKNNLTVISitHD---IDEANmaDQVLVLDDGKL 221
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
313-457 |
3.19e-05 |
|
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: 45.04 E-value: 3.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 313 EFRDVAVCYDGRTVCREITFEVLAGERIALQGANGCGKSSLLKLLLGEEIPHSGTVETMSGLVVSYVSQNTD------HL 386
Cdd:TIGR01189 2 AARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHEnilylgHL 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2468763893 387 RGSLTEFARTQGLD------GSRFRTILRKLD-VPREQFEKDLADY-SSGQKKKVLLAASLCTQAHLYVWDEPLNFIDV 457
Cdd:TIGR01189 82 PGLKPELSALENLHfwaaihGGAQRTIEDALAaVGLTGFEDLPAAQlSAGQQRRLALARLWLSRRPLWILDEPTTALDK 160
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
20-172 |
3.59e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 45.59 E-value: 3.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 20 IFDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQGEYPYSG-----TISASVEFEYFPyeVANLSRTGLEVVREIAPEAED 94
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGaprgaRVTGDVTLNGEP--LAAIDAPRLARLRAVLPQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 95 WEIQ---RELGLL-----------------DLAERSLELP---------FSSLSNGERTKV----LLAAMFLKENA---- 137
Cdd:PRK13547 94 PAFAfsaREIVLLgrypharragalthrdgEIAWQALALAgatalvgrdVTTLSGGELARVqfarVLAQLWPPHDAaqpp 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2468763893 138 -FLLIDEPTNHLDLEGRRKLGSY---LAR--KRGFLLVSHD 172
Cdd:PRK13547 174 rYLLLDEPTAALDLAHQHRLLDTvrrLARdwNLGVLAIVHD 214
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
313-488 |
3.66e-05 |
|
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: 44.82 E-value: 3.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 313 EFRDVAVCYDGRTVCREITFEVLAGERIALQGANGCGKSSLLKLLLGEEIPHSGTV----ETMSGLV-----VSYVSQNT 383
Cdd:cd03259 2 ELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEIlidgRDVTGVPperrnIGMVFQDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 384 ---DHLrgsltefartqgldgSRFRTI---LRKLDVPREQFEK---------DLADY--------SSGQKKKVLLAASLC 440
Cdd:cd03259 82 alfPHL---------------TVAENIafgLKLRGVPKAEIRArvrellelvGLEGLlnryphelSGGQQQRVALARALA 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2468763893 441 TQAHLYVWDEPLNFIDVISRMQ----VEDLLLACRPTLLFVEHD----ARFCDEIA 488
Cdd:cd03259 147 REPSLLLLDEPLSALDAKLREElreeLKELQRELGITTIYVTHDqeeaLALADRIA 202
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
89-183 |
4.63e-05 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 45.08 E-value: 4.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 89 APEAEDWEIQRELGLLDlAERSLEL-PFSsLSNGERTKVLLAAMFLKENAFLLIDEPTNHLDLEGRRKLGSYLA---RKR 164
Cdd:PRK10418 113 ADDATLTAALEAVGLEN-AARVLKLyPFE-MSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLEsivQKR 190
|
90 100
....*....|....*....|.
gi 2468763893 165 --GFLLVSHDRAFLDQCVDHI 183
Cdd:PRK10418 191 alGMLLVTHDMGVVARLADDV 211
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
313-487 |
5.18e-05 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 45.18 E-value: 5.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 313 EFRDVAVCYDGRTVCREITFEVLAGERIALQGANGCGKSSLLKLLLGEEIPHSGTV----ETMSG------LVVSYVSQ- 381
Cdd:PRK13537 9 DFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSIslcgEPVPSrarharQRVGVVPQf 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 382 -NTD---HLRGSLTEFARTQGLDGSRFRTILRK-LDVPREQFEKD--LADYSSGQKKKVLLAASLCTQAHLYVWDEPLNF 454
Cdd:PRK13537 89 dNLDpdfTVRENLLVFGRYFGLSAAAARALVPPlLEFAKLENKADakVGELSGGMKRRLTLARALVNDPDVLVLDEPTTG 168
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2468763893 455 IDVISRMQV-EDL--LLACRPTLL----FVEHDARFCDEI 487
Cdd:PRK13537 169 LDPQARHLMwERLrsLLARGKTILltthFMEEAERLCDRL 208
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
22-172 |
5.24e-05 |
|
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: 44.55 E-value: 5.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 22 DHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQG-EYPYSGTIS----------------ASVEFEY-------------FP 71
Cdd:cd03301 17 DDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGlEEPTSGRIYiggrdvtdlppkdrdiAMVFQNYalyphmtvydniaFG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 72 YEVANLSRTGL-EVVREIApeaedweiqRELGLLDLAERsleLPfSSLSNGERTKVLLAAMFLKENAFLLIDEPTNHLDL 150
Cdd:cd03301 97 LKLRKVPKDEIdERVREVA---------ELLQIEHLLDR---KP-KQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDA 163
|
170 180
....*....|....*....|....*..
gi 2468763893 151 EGRRKLGSYLAR-----KRGFLLVSHD 172
Cdd:cd03301 164 KLRVQMRAELKRlqqrlGTTTIYVTHD 190
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
313-488 |
5.28e-05 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 45.60 E-value: 5.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 313 EFRDVAVCYDGRTVCREITFEVLAGERIALQGANGCGKSSLLKLLLGEEIPHSGTV-------ETMS----GLVVSYVSQ 381
Cdd:PRK09536 5 DVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVlvagddvEALSaraaSRRVASVPQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 382 NT----DHLRGSLTEFARTQGLdgSRF--------RTILRKLD-VPREQF-EKDLADYSSGQKKKVLLAASLCTQAHLYV 447
Cdd:PRK09536 85 DTslsfEFDVRQVVEMGRTPHR--SRFdtwtetdrAAVERAMErTGVAQFaDRPVTSLSGGERQRVLLARALAQATPVLL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2468763893 448 WDEPLNFIDVisRMQVEDLLLACR-----PTLLFVEHD----ARFCDEIA 488
Cdd:PRK09536 163 LDEPTASLDI--NHQVRTLELVRRlvddgKTAVAAIHDldlaARYCDELV 210
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
112-177 |
6.59e-05 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 44.69 E-value: 6.59e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2468763893 112 ELPFSSLSNGERTKVLLAAMFL---KENAFLLIDEPTNHLDLEGRRKLG---SYLARKRG-FLLVSHDRAFLD 177
Cdd:pfam13304 231 ELPAFELSDGTKRLLALLAALLsalPKGGLLLIDEPESGLHPKLLRRLLellKELSRNGAqLILTTHSPLLLD 303
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
313-488 |
1.17e-04 |
|
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: 43.32 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 313 EFRDVAVCYDGRTVCREITFEVLAGERIALQGANGC-----GKSSLLKLLLGEEIPHSGTVETMSGLV------------ 375
Cdd:cd03260 2 ELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCgkstlLRLLNRLNDLIPGAPDEGEVLLDGKDIydldvdvlelrr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 376 -VSYVSQNTDHLRGS----------LTEFARTQGLDGsRFRTILRKLDVPREqfEKDLADY---SSGQKKKVLLAASLCT 441
Cdd:cd03260 82 rVGMVFQKPNPFPGSiydnvayglrLHGIKLKEELDE-RVEEALRKAALWDE--VKDRLHAlglSGGQQQRLCLARALAN 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2468763893 442 QAHLYVWDEPLNFIDVISRMQVEDLL--LACRPTLLFVEHD----ARFCDEIA 488
Cdd:cd03260 159 EPEVLLLDEPTSALDPISTAKIEELIaeLKKEYTIVIVTHNmqqaARVADRTA 211
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
402-488 |
1.51e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.39 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 402 SRFRTILRKLDVPREQFEKDLADYSSGQKKKVLLAASLCTQAHLYVWDEPLNFIDVISRMQVEDLLLACRPTLLFVEHDA 481
Cdd:PRK10636 127 SRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDR 206
|
....*..
gi 2468763893 482 RFCDEIA 488
Cdd:PRK10636 207 DFLDPIV 213
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-145 |
1.63e-04 |
|
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: 43.19 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 4 IDVSNLTFGYEGSPELiFDhVGFQIDSGWKLGFTGRNGRGKTTFLRLLQGEY-PYSGTIsasvefEYFPYEVANLS---- 78
Cdd:cd03224 1 LEVENLNAGYGKSQIL-FG-VSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLpPRSGSI------RFDGRDITGLPpher 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 79 -RTGLEVV---REI-----------------APEAEDWEIQRELGLL-DLAERsLELPFSSLSNGERTKVLLAAMFLKEN 136
Cdd:cd03224 73 aRAGIGYVpegRRIfpeltveenlllgayarRRAKRKARLERVYELFpRLKER-RKQLAGTLSGGEQQMLAIARALMSRP 151
|
....*....
gi 2468763893 137 AFLLIDEPT 145
Cdd:cd03224 152 KLLLLDEPS 160
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
292-487 |
2.36e-04 |
|
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: 43.67 E-value: 2.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 292 LERQEALAVTPLPCRAGArlAEFRDVAVCYDGRT--VCREITFEVLAGERIALQGANGC-------------Gkssllkl 356
Cdd:COG2274 456 PEREEGRSKLSLPRLKGD--IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSgkstllklllglyE------- 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 357 llgeeiPHSGTVetmsgLV----------------VSYVSQNTDHLRGSLTE---FARTQgLDGSRFRTILRKLDVprEQ 417
Cdd:COG2274 527 ------PTSGRI-----LIdgidlrqidpaslrrqIGVVLQDVFLFSGTIREnitLGDPD-ATDEEIIEAARLAGL--HD 592
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 418 FEKDLAD-Y-----------SSGQKKKVLLAASLCTQAHLYVWDEPLNFIDVISRMQVEDLL--LACRPTLLFVEHD--- 480
Cdd:COG2274 593 FIEALPMgYdtvvgeggsnlSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLrrLLKGRTVIIIAHRlst 672
|
....*..
gi 2468763893 481 ARFCDEI 487
Cdd:COG2274 673 IRLADRI 679
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-172 |
2.63e-04 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 42.75 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 1 MSMIDVSNLTFGYEGSPEL-------IFDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQG-EYPYSGTIS-ASVEFEYFP 71
Cdd:PRK10419 1 MTLLNVSGLSHHYAHGGLSgkhqhqtVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGlESPSQGNVSwRGEPLAKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 72 YEVANLSRTGLEVVREIAPEAED------WEIQ---RELGLLDLAERS---------LELPFS-------SLSNGERTKV 126
Cdd:PRK10419 81 RAQRKAFRRDIQMVFQDSISAVNprktvrEIIReplRHLLSLDKAERLarasemlraVDLDDSvldkrppQLSGGQLQRV 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2468763893 127 LLAAMFLKENAFLLIDEPTNHLDLEGRRKLGSYLARKR-----GFLLVSHD 172
Cdd:PRK10419 161 CLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQqqfgtACLFITHD 211
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
311-349 |
2.98e-04 |
|
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: 42.38 E-value: 2.98e-04
10 20 30
....*....|....*....|....*....|....*....
gi 2468763893 311 LAEFRDVAVCYDGRTVCREITFEVLAGERIALQGANGCG 349
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAG 41
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
33-195 |
3.08e-04 |
|
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: 41.20 E-value: 3.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 33 KLGFTGRNGRGKTTFLRLLQGEYPYSGtisasvefeyfpyevanlsrtglEVVREIAPEaedweIQRELGLLDLAERSLE 112
Cdd:smart00382 4 VILIVGPPGSGKTTLARALARELGPPG-----------------------GGVIYIDGE-----DILEEVLDQLLLIIVG 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 113 LPFSSLSNGERTKVLLAAMFLKENAFLLIDEPTNHLDLEGRRKLGSYLARKRGFLLVSHDRAFLdqcvdhILAINRTNIE 192
Cdd:smart00382 56 GKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLTV------ILTTNDEKDL 129
|
...
gi 2468763893 193 IQR 195
Cdd:smart00382 130 GPA 132
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
26-171 |
3.51e-04 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 43.20 E-value: 3.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 26 FQIDSGWKLGFTGRNGRGKTTFLRLLQGEYP-YSGTISASVEFEYF-----PYevanlsrTGLEVVRE--IAPEAEDWEI 97
Cdd:TIGR00954 473 FEVPSGNNLLICGPNGCGKSSLFRILGELWPvYGGRLTKPAKGKLFyvpqrPY-------MTLGTLRDqiIYPDSSEDMK 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 98 QRELG------------LLDLAERslELPFSS-------LSNGERTKVLLAAMFLKENAFLLIDEPTN--HLDLEGRrkl 156
Cdd:TIGR00954 546 RRGLSdkdleqildnvqLTHILER--EGGWSAvqdwmdvLSGGEKQRIAMARLFYHKPQFAILDECTSavSVDVEGY--- 620
|
170
....*....|....*...
gi 2468763893 157 gSY-LARKRGFLL--VSH 171
Cdd:TIGR00954 621 -MYrLCREFGITLfsVSH 637
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
387-488 |
3.61e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 43.16 E-value: 3.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 387 RGSLTEFARTQgldgsrfrtILRKLD-VPREQFEKDLADY----SSGQKKKVLLAASLCTQAHLYVWDEPLNFIDVISRM 461
Cdd:PRK15134 123 RGMRREAARGE---------ILNCLDrVGIRQAAKRLTDYphqlSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQA 193
|
90 100 110
....*....|....*....|....*....|.
gi 2468763893 462 QVEDLLLACRP----TLLFVEHDARFCDEIA 488
Cdd:PRK15134 194 QILQLLRELQQelnmGLLFITHNLSIVRKLA 224
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
3-181 |
3.69e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 42.38 E-value: 3.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 3 MIDVSNLTFGY----EGSPELIFDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQGEY-PYSGTI---SASVEFEYFPYEV 74
Cdd:PRK13633 4 MIKCKNVSYKYesneESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLiPSEGKVyvdGLDTSDEENLWDI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 75 ANlsRTGL-----------EVVRE----------IAPEAEDWEIQRELGLLDLAERSLELPfSSLSNGERTKVLLAAMFL 133
Cdd:PRK13633 84 RN--KAGMvfqnpdnqivaTIVEEdvafgpenlgIPPEEIRERVDESLKKVGMYEYRRHAP-HLLSGGQKQRVAIAGILA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2468763893 134 KENAFLLIDEPTNHLDLEGRRKLGSY---LARKRGF--LLVSHdraFLDQCVD 181
Cdd:PRK13633 161 MRPECIIFDEPTAMLDPSGRREVVNTikeLNKKYGItiILITH---YMEEAVE 210
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
22-149 |
4.18e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 42.99 E-value: 4.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 22 DHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQGEYPysGTISASVEFEYFPYEVANLS---RTGLEVVRE------IAP-- 90
Cdd:PRK13549 279 DDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYP--GRWEGEIFIDGKPVKIRNPQqaiAQGIAMVPEdrkrdgIVPvm 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 91 ----------------------EAEDWEIQRELGLLDLAERSLELPFSSLSNGERTKVLLAAMFLKENAFLLIDEPTNHL 148
Cdd:PRK13549 357 gvgknitlaaldrftggsriddAAELKTILESIQRLKVKTASPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGI 436
|
.
gi 2468763893 149 D 149
Cdd:PRK13549 437 D 437
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
77-183 |
4.85e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 41.96 E-value: 4.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 77 LSRTGLEVVREIAPEAEdwEIQRELGLLDLAERSLELPFSSLSNGERTKVLLAAMFLKENAFLLIDEPTNHLDL---EGR 153
Cdd:PRK14246 115 LKSHGIKEKREIKKIVE--ECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIvnsQAI 192
|
90 100 110
....*....|....*....|....*....|
gi 2468763893 154 RKLGSYLARKRGFLLVSHDRAFLDQCVDHI 183
Cdd:PRK14246 193 EKLITELKNEIAIVIVSHNPQQVARVADYV 222
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
316-485 |
5.15e-04 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 41.79 E-value: 5.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 316 DVAVCY-DGRTVCREITFEVLAGERIALQGANGCGKSSLLKLLLGEEIPHSGTVETMSGLV--------VSYVSQNTD-- 384
Cdd:PRK15056 11 DVTVTWrNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTrqalqknlVAYVPQSEEvd 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 385 -------------HLRGSLTEFARTQGLDGSRFRTILRKLDVpREQFEKDLADYSSGQKKKVLLAASLCTQAHLYVWDEP 451
Cdd:PRK15056 91 wsfpvlvedvvmmGRYGHMGWLRRAKKRDRQIVTAALARVDM-VEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2468763893 452 LNFIDVISRMQVEDLLLACRP---TLLFVEHD----ARFCD 485
Cdd:PRK15056 170 FTGVDVKTEARIISLLRELRDegkTMLVSTHNlgsvTEFCD 210
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
112-172 |
5.28e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 5.28e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2468763893 112 ELPFSSLSNGERTKVLLA-----AMFLKENAFLLI-DEPTNHLDLEGRRKL----GSYLARKRGFLLVSHD 172
Cdd:PRK03918 783 ERPLTFLSGGERIALGLAfrlalSLYLAGNIPLLIlDEPTPFLDEERRRKLvdimERYLRKIPQVIIVSHD 853
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
313-488 |
5.70e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 41.64 E-value: 5.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 313 EFRDVAVCY-DGRTVCREITFEVLAGERIALQGANGCGKSSLLKLLLGEEIPHSGTVETMSGLV-----------VSYVS 380
Cdd:PRK13647 6 EVEDLHFRYkDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVnaenekwvrskVGLVF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 381 QNTDHLRGSLTEF------ARTQGLDG----SRFRTILRKLDVprEQFeKDLADY--SSGQKKKVLLAASLCTQAHLYVW 448
Cdd:PRK13647 86 QDPDDQVFSSTVWddvafgPVNMGLDKdeveRRVEEALKAVRM--WDF-RDKPPYhlSYGQKKRVAIAGVLAMDPDVIVL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2468763893 449 DEPLNFIDVISR---MQVEDLLLACRPTLLFVEHDARFCDEIA 488
Cdd:PRK13647 163 DEPMAYLDPRGQetlMEILDRLHNQGKTVIVATHDVDLAAEWA 205
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
311-480 |
6.31e-04 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 42.13 E-value: 6.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 311 LAEFRDVAVCYDGRTVCREITFEVLAGERIALQGANGCGKSSLLKLLLGEEIPHSGTVeTMSGLVVSY------------ 378
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQI-MLDGVDLSHvppyqrpinmmf 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 379 ----------VSQNtdhLRGSLTEFARTQGLDGSRFRTILRKldVPREQFEKDLA-DYSSGQKKKVLLAASLCTQAHLYV 447
Cdd:PRK11607 98 qsyalfphmtVEQN---IAFGLKQDKLPKAEIASRVNEMLGL--VHMQEFAKRKPhQLSGGQRQRVALARSLAKRPKLLL 172
|
170 180 190
....*....|....*....|....*....|....*..
gi 2468763893 448 WDEPLNFID--VISRMQVE--DLLLACRPTLLFVEHD 480
Cdd:PRK11607 173 LDEPMGALDkkLRDRMQLEvvDILERVGVTCVMVTHD 209
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
101-179 |
7.74e-04 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 40.92 E-value: 7.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 101 LGLLDLAERSLELPfSSLSNGERTKVLLAAMFLKENAFLLIDEPTNHLDlegrRKLGSYLA-------RKRG--FLLVSH 171
Cdd:PRK10584 131 LEQLGLGKRLDHLP-AQLSGGEQQRVALARAFNGRPDVLFADEPTGNLD----RQTGDKIAdllfslnREHGttLILVTH 205
|
....*...
gi 2468763893 172 DRAFLDQC 179
Cdd:PRK10584 206 DLQLAARC 213
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
423-480 |
8.59e-04 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 41.20 E-value: 8.59e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2468763893 423 ADYSSGQKKKVLLAASLCTQAHLYVWDEPLNFIDVISR--MQ--VEDLLLACRPTLLFVEHD 480
Cdd:PRK11247 132 AALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRieMQdlIESLWQQHGFTVLLVTHD 193
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
324-484 |
8.99e-04 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 41.21 E-value: 8.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 324 RTVCREITFEVLAGERIALQGANGCGKSSLLKLLLGEEIPHSGTV----ETMSGL----------VVSYVSQ------NT 383
Cdd:PRK10419 25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVswrgEPLAKLnraqrkafrrDIQMVFQdsisavNP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 384 DH-LRGSLTEFAR-TQGLDGS----RFRTILRKLDVPREQFEKDLADYSSGQKKKVLLAASLCTQAHLYVWDEPLNFIDV 457
Cdd:PRK10419 105 RKtVREIIREPLRhLLSLDKAerlaRASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDL 184
|
170 180 190
....*....|....*....|....*....|....*
gi 2468763893 458 ISRMQVEDLLLACRPTL----LFVEHDAR----FC 484
Cdd:PRK10419 185 VLQAGVIRLLKKLQQQFgtacLFITHDLRlverFC 219
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
322-489 |
1.01e-03 |
|
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: 40.57 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 322 DGRTVCREITFEVLAGERIALQGANGCGKSSLLKLLLGEEIPHSGTVeTMSGL-----------VVSYVSQN-------- 382
Cdd:cd03263 13 GTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTA-YINGYsirtdrkaarqSLGYCPQFdalfdelt 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 383 -TDHLRgsltEFARTQGL-DGSRFRTILRKLDVPR-EQFEKDLA-DYSSGQKKKVLLAASLCTQAHLYVWDEPLNFIDVI 458
Cdd:cd03263 92 vREHLR----FYARLKGLpKSEIKEEVELLLRVLGlTDKANKRArTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPA 167
|
170 180 190
....*....|....*....|....*....|...
gi 2468763893 459 SRMQVEDLLLACRP--TLLFVEHDARFCDEIAT 489
Cdd:cd03263 168 SRRAIWDLILEVRKgrSIILTTHSMDEAEALCD 200
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
426-489 |
1.05e-03 |
|
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: 40.36 E-value: 1.05e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2468763893 426 SSGQKKKVLLAASLCTQAHLYVWDEPLNFIDVISRMQ----VEDLLLACRPTLLFVEHDA----RFCDEIAT 489
Cdd:cd03297 133 SGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQllpeLKQIKKNLNIPVIFVTHDLseaeYLADRIVV 204
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
22-148 |
1.17e-03 |
|
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: 41.35 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 22 DHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQGEYPYsGTISASVEFEYFPYEVANLSRT---GLEVVRE---IAPE---A 92
Cdd:TIGR02633 18 DGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPH-GTWDGEIYWSGSPLKASNIRDTeraGIVIIHQeltLVPElsvA 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2468763893 93 EDW----EIQRELGLLD-----------LAERSLE-----LPFSSLSNGERTKVLLAAMFLKENAFLLIDEPTNHL 148
Cdd:TIGR02633 97 ENIflgnEITLPGGRMAynamylraknlLRELQLDadnvtRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSL 172
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
363-488 |
2.12e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 40.03 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 363 PHSGTVETMSGLVVSYVSQNTDHLRGSLTEFARTQGLdgsrFRTILRKLDVPREQFekdladySSGQKKKVLLAASLCTQ 442
Cdd:PRK14246 103 PHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGL----WKEVYDRLNSPASQL-------SGGQQQRLTIARALALK 171
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2468763893 443 AHLYVWDEPLNFIDVISRMQVEDLL--LACRPTLLFVEHD----ARFCDEIA 488
Cdd:PRK14246 172 PKVLLMDEPTSMIDIVNSQAIEKLIteLKNEIAIVIVSHNpqqvARVADYVA 223
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
320-463 |
2.12e-03 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 40.23 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 320 CYDGRTVCREITFEVLAGERIALQGANGCGKSSLLKLLLGEEIPHSGTVEtMSGLvVSYVSQNTDHLRGSLTE---FART 396
Cdd:cd03291 46 CLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIK-HSGR-ISFSSQFSWIMPGTIKEniiFGVS 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 397 qgLDGSRFRTILRKLdvpreQFEKDLADY---------------SSGQKKKVLLAASLCTQAHLYVWDEPLNFIDVISRM 461
Cdd:cd03291 124 --YDEYRYKSVVKAC-----QLEEDITKFpekdntvlgeggitlSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEK 196
|
..
gi 2468763893 462 QV 463
Cdd:cd03291 197 EI 198
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
313-480 |
2.25e-03 |
|
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: 39.38 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 313 EFRDVAVCYDGR----TVCREITFEVLAGERIALQGANGCGKSSLLKLLLGEEIPHSGTVeTMSGLVVS-------YVSQ 381
Cdd:cd03293 2 EVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEV-LVDGEPVTgpgpdrgYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 382 NtDHLRGSLT-----EFA-RTQGLDGSRFRTILRKL--DVPREQFEKDL-ADYSSGQKKKVLLAASLCTQAHLYVWDEPL 452
Cdd:cd03293 81 Q-DALLPWLTvldnvALGlELQGVPKAEARERAEELleLVGLSGFENAYpHQLSGGMRQRVALARALAVDPDVLLLDEPF 159
|
170 180 190
....*....|....*....|....*....|..
gi 2468763893 453 NFIDVISRMQVEDLLLAC----RPTLLFVEHD 480
Cdd:cd03293 160 SALDALTREQLQEELLDIwretGKTVLLVTHD 191
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
4-223 |
2.31e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 40.15 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 4 IDVSNLTFGYE-GSP--ELIFDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQGEY-PYSGTISASvefeyfpyEVANLSR 79
Cdd:PRK13646 3 IRFDNVSYTYQkGTPyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLkPTTGTVTVD--------DITITHK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 80 TGLEVVREIA---------PEAEDWE--IQRE---------LGLLDLAERS----LELPFS---------SLSNGERTKV 126
Cdd:PRK13646 75 TKDKYIRPVRkrigmvfqfPESQLFEdtVEREiifgpknfkMNLDEVKNYAhrllMDLGFSrdvmsqspfQMSGGQMRKI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 127 LLAAMFLKENAFLLIDEPTNHLDLEGRRKLGSYLAR-----KRGFLLVSHDRAFLDQCVDHILAINRTNIEIQ---RGNF 198
Cdd:PRK13646 155 AIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSlqtdeNKTIILVSHDMNEVARYADEVIVMKEGSIVSQtspKELF 234
|
250 260
....*....|....*....|....*
gi 2468763893 199 SSwwENRRRQDAFELARQEKLQKDI 223
Cdd:PRK13646 235 KD--KKKLADWHIGLPEIVQLQYDF 257
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
367-479 |
2.61e-03 |
|
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: 39.40 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 367 TVETMSGLVVSYVSQNTDHLRGSLTEFARTQGLDGsrfrtilrkldvpreqFEKDLAD-YSSGQKKKVLLAASLCTQAHL 445
Cdd:cd03298 86 TVEQNVGLGLSPGLKLTAEDRQAIEVALARVGLAG----------------LEKRLPGeLSGGERQRVALARVLVRDKPV 149
|
90 100 110
....*....|....*....|....*....|....*...
gi 2468763893 446 YVWDEPLNFIDVISRMQVEDLLL-ACRP---TLLFVEH 479
Cdd:cd03298 150 LLLDEPFAALDPALRAEMLDLVLdLHAEtkmTVLMVTH 187
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
22-148 |
2.74e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 40.30 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 22 DHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQGEYPYsGTISASVEFEYFPYEVANLSRT---GLEVV-REIA--PE---A 92
Cdd:PRK13549 22 DNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPH-GTYEGEIIFEGEELQASNIRDTeraGIAIIhQELAlvKElsvL 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2468763893 93 EDWEIQREL---GLLD-----------LAERSLE----LPFSSLSNGERTKVLLAAMfLKENAFLLI-DEPTNHL 148
Cdd:PRK13549 101 ENIFLGNEItpgGIMDydamylraqklLAQLKLDinpaTPVGNLGLGQQQLVEIAKA-LNKQARLLIlDEPTASL 174
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
117-200 |
2.90e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 40.27 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 117 SLSNGERTKVLLA-----AMFLKEN-AFLLIDEPTNHLDLEGRRKLGS---YLARKRG----FLLVSHDRafldqcvdHI 183
Cdd:PRK01156 801 SLSGGEKTAVAFAlrvavAQFLNNDkSLLIMDEPTAFLDEDRRTNLKDiieYSLKDSSdipqVIMISHHR--------EL 872
|
90
....*....|....*..
gi 2468763893 184 LAINRTNIEIQRGNFSS 200
Cdd:PRK01156 873 LSVADVAYEVKKSSGSS 889
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
313-459 |
2.91e-03 |
|
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: 38.93 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 313 EFRDVAVCY--DGRTVCREITFEVLAGERIALQGANGCGKSSLLKLLLGEEIPHSGTVEtMSGLVVSYVSQNTdhLRGSL 390
Cdd:cd03369 8 EVENLSVRYapDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIE-IDGIDISTIPLED--LRSSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 391 TEFARTQGL-DGsrfrTILRKLDVPREQFEKDL----------ADYSSGQKKKVLLAASLCTQAHLYVWDEPLNFIDVIS 459
Cdd:cd03369 85 TIIPQDPTLfSG----TIRSNLDPFDEYSDEEIygalrvseggLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYAT 160
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
426-467 |
3.77e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 39.61 E-value: 3.77e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2468763893 426 SSGQKKKVLLAASLCTQAHLYVWDEPLNFIDVISRMQVEDLL 467
Cdd:PRK10938 137 STGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELL 178
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
3-199 |
4.19e-03 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 39.00 E-value: 4.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 3 MIDVSNLTFGYEGSPelIFDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQGEYPYSGTiSASVEFE-------------- 68
Cdd:PRK09580 1 MLSIKDLHVSVEDKA--ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEVT-GGTVEFKgkdllelspedrag 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 69 -------YFPYEVANLS-----RTGLEVVREIAPEAE----DWE--IQRELGLL----DLAERSLELPFSSlsnGERTKV 126
Cdd:PRK09580 78 egifmafQYPVEIPGVSnqfflQTALNAVRSYRGQEPldrfDFQdlMEEKIALLkmpeDLLTRSVNVGFSG---GEKKRN 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2468763893 127 LLAAMFLKENAFLLIDEPTNHLDLEGRR----KLGSYLARKRGFLLVSHDRAFLDQCV-DHILAINRTNIeIQRGNFS 199
Cdd:PRK09580 155 DILQMAVLEPELCILDESDSGLDIDALKivadGVNSLRDGKRSFIIVTHYQRILDYIKpDYVHVLYQGRI-VKSGDFT 231
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
313-479 |
5.72e-03 |
|
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: 37.68 E-value: 5.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 313 EFRDVAVCYDG--RTVCREITFEVLAGERIALQGANGCGKSSLLKLLLGEEIPHSGTVeTMSGLVVSYVSQNTDHLRGSL 390
Cdd:cd03247 2 SINNVSFSYPEqeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEI-TLDGVPVSDLEKALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 391 TE----FARTQGLD-GSRFrtilrkldvpreqfekdladySSGQKKKVLLAASLCTQAHLYVWDEPLNFIDVISRMQVED 465
Cdd:cd03247 81 NQrpylFDTTLRNNlGRRF---------------------SGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLS 139
|
170
....*....|....*.
gi 2468763893 466 LLL--ACRPTLLFVEH 479
Cdd:cd03247 140 LIFevLKDKTLIWITH 155
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
4-197 |
6.42e-03 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 38.93 E-value: 6.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 4 IDVSNLTFGYEGSPELIFDHVGFQIDSGWKLGFTGRNGRGKTTFLRLLQ-------GEYPYSGTISASVEFEYFPYEVAN 76
Cdd:PRK10789 314 LDVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQrhfdvseGDIRFHDIPLTKLQLDSWRSRLAV 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 77 LSRTGL----EVVREIA---PEAEDWEIQRELGLLDLAERSLELPFS----------SLSNGERTKVLLAAMFLKENAFL 139
Cdd:PRK10789 394 VSQTPFlfsdTVANNIAlgrPDATQQEIEHVARLASVHDDILRLPQGydtevgergvMLSGGQKQRISIARALLLNAEIL 473
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2468763893 140 LIDEP-------TNHLDLEGRRKLGsylaRKRGFLLVSHDRAFLDQcVDHILAINRTNIeIQRGN 197
Cdd:PRK10789 474 ILDDAlsavdgrTEHQILHNLRQWG----EGRTVIISAHRLSALTE-ASEILVMQHGHI-AQRGN 532
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
328-480 |
7.87e-03 |
|
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: 38.08 E-value: 7.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 328 REITFEVLAGERIALQGANGCGKSSLLKLLLGEEIPHSGTVETMsGLVVSyvSQNTDHLR------GSLTEF-------- 393
Cdd:cd03267 38 KGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVA-GLVPW--KRRKKFLRrigvvfGQKTQLwwdlpvid 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 394 -----ARTQGLDGSRFRTILRK----------LDVPREQFekdladySSGQKKKVLLAASLCTQAHLYVWDEPLNFIDVI 458
Cdd:cd03267 115 sfyllAAIYDLPPARFKKRLDElselldleelLDTPVRQL-------SLGQRMRAEIAAALLHEPEILFLDEPTIGLDVV 187
|
170 180
....*....|....*....|....*.
gi 2468763893 459 SRMQVEDLLLA-CR---PTLLFVEHD 480
Cdd:cd03267 188 AQENIRNFLKEyNRergTTVLLTSHY 213
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-61 |
8.68e-03 |
|
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: 38.04 E-value: 8.68e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2468763893 1 MSMIDVSNLTFGYEGSPelIFDHVGFQIDSGWKLGFTGRNGRGKTTFLR----LLQgeyPYSGTI 61
Cdd:COG0410 1 MPMLEVENLHAGYGGIH--VLHGVSLEVEEGEIVALLGRNGAGKTTLLKaisgLLP---PRSGSI 60
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
402-489 |
9.84e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 38.69 E-value: 9.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468763893 402 SRFRTILRKLDVPREQFEKDLADYSSGQKKKVLLAASLCTQAHLYVWDEPLNFIDVISRMQVEDLLLACRPTLLFVEHDA 481
Cdd:PLN03073 322 ARAASILAGLSFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAR 401
|
....*...
gi 2468763893 482 RFCDEIAT 489
Cdd:PLN03073 402 EFLNTVVT 409
|
|
| |
