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Conserved domains on  [gi|1512845752|gb|RNQ06007|]
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ABC transporter ATP-binding protein [Klebsiella pneumoniae]

Protein Classification

ATP-binding cassette domain-containing protein( domain architecture ID 1000433)

ATP-binding cassette domain-containing protein

Gene Ontology:  GO:0005524
PubMed:  12370001|11421270

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Uup super family cl33905
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
12-521 1.22e-91

ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];


The actual alignment was detected with superfamily member COG0488:

Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 290.04  E-value: 1.22e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  12 LHQVTCQFAtGQTLFGPLSVSLEPSLC-GLVGRNGVGKTRLLRLLAGLDSPAGGHIERAAAVAWVAQQ--PTLTPETTL- 87
Cdd:COG0488     1 LENLSKSFG-GRPLLDDVSLSINPGDRiGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPqePPLDDDLTVl 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  88 -ATLLGYASVFAALSRLEQGQG--------------LADDFDLLDGhWDLTDRLS-----LAFREADLppfsaDRPAFSL 147
Cdd:COG0488    80 dTVLDGDAELRALEAELEELEAklaepdedlerlaeLQEEFEALGG-WEAEARAEeilsgLGFPEEDL-----DRPVSEL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 148 SGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGREWLYHQLESWQGGALIASHDRELLTRM-PRIIELTPTALRSYGGN 226
Cdd:COG0488   154 SGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVaTRILELDRGKLTLYPGN 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 227 YDEYQRQRmAEQQAARAAlehavtDRRRTRARMQKEHDAAQRRSAQtlrtvdtlniASfervKYKgAAKERPGALRRqhr 306
Cdd:COG0488   234 YSAYLEQR-AERLEQEAA------AYAKQQKKIAKEEEFIRRFRAK----------AR----KAK-QAQSRIKALEK--- 288
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 307 eqnssLNAAVQQARERveeetPVMFTLPGSEvAAGKQVLVVESLQ--------LDHapaapLNWRIDGPMRIALKGPNGC 378
Cdd:COG0488   289 -----LEREEPPRRDK-----TVEIRFPPPE-RLGKKVLELEGLSksygdktlLDD-----LSLRIDRGDRIGLIGPNGA 352
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 379 gkttllktllgLEQAASGDVRL--SVSAAYLDQHLTQLDLSLSVMAHLSLEDTPLDEGLLRTRLAQLQLGADKVTLPLSA 456
Cdd:COG0488   353 gkstllkllagELEPDSGTVKLgeTVKIGYFDQHQEELDPDKTVLDELRDGAPGGTEQEVRGYLGRFLFSGDDAFKPVGV 432
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1512845752 457 LSGGERLKAALACVLWRrePAQLLLLDEPTNHLDLASTQAIESALAAFPGAMLVVSHDEAFLQGL 521
Cdd:COG0488   433 LSGGEKARLALAKLLLS--PPNVLLLDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRV 495
 
Name Accession Description Interval E-value
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
12-521 1.22e-91

ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 290.04  E-value: 1.22e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  12 LHQVTCQFAtGQTLFGPLSVSLEPSLC-GLVGRNGVGKTRLLRLLAGLDSPAGGHIERAAAVAWVAQQ--PTLTPETTL- 87
Cdd:COG0488     1 LENLSKSFG-GRPLLDDVSLSINPGDRiGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPqePPLDDDLTVl 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  88 -ATLLGYASVFAALSRLEQGQG--------------LADDFDLLDGhWDLTDRLS-----LAFREADLppfsaDRPAFSL 147
Cdd:COG0488    80 dTVLDGDAELRALEAELEELEAklaepdedlerlaeLQEEFEALGG-WEAEARAEeilsgLGFPEEDL-----DRPVSEL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 148 SGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGREWLYHQLESWQGGALIASHDRELLTRM-PRIIELTPTALRSYGGN 226
Cdd:COG0488   154 SGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVaTRILELDRGKLTLYPGN 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 227 YDEYQRQRmAEQQAARAAlehavtDRRRTRARMQKEHDAAQRRSAQtlrtvdtlniASfervKYKgAAKERPGALRRqhr 306
Cdd:COG0488   234 YSAYLEQR-AERLEQEAA------AYAKQQKKIAKEEEFIRRFRAK----------AR----KAK-QAQSRIKALEK--- 288
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 307 eqnssLNAAVQQARERveeetPVMFTLPGSEvAAGKQVLVVESLQ--------LDHapaapLNWRIDGPMRIALKGPNGC 378
Cdd:COG0488   289 -----LEREEPPRRDK-----TVEIRFPPPE-RLGKKVLELEGLSksygdktlLDD-----LSLRIDRGDRIGLIGPNGA 352
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 379 gkttllktllgLEQAASGDVRL--SVSAAYLDQHLTQLDLSLSVMAHLSLEDTPLDEGLLRTRLAQLQLGADKVTLPLSA 456
Cdd:COG0488   353 gkstllkllagELEPDSGTVKLgeTVKIGYFDQHQEELDPDKTVLDELRDGAPGGTEQEVRGYLGRFLFSGDDAFKPVGV 432
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1512845752 457 LSGGERLKAALACVLWRrePAQLLLLDEPTNHLDLASTQAIESALAAFPGAMLVVSHDEAFLQGL 521
Cdd:COG0488   433 LSGGEKARLALAKLLLS--PPNVLLLDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRV 495
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
39-533 3.06e-45

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: 167.42  E-value: 3.06e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  39 GLVGRNGVGKTRLLRLLAGLDSPAGGHIERAAAVAW--VAQQPTLTPETTL--ATLLGYASVFAALSRL----------- 103
Cdd:TIGR03719  35 GVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVgyLPQEPQLDPTKTVreNVEEGVAEIKDALDRFneisakyaepd 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 104 --------EQGQgLADDFDLLDGhWDLTDRLSLAFREADLPPFsaDRPAFSLSGGERMKALLCGAFVSGADYLLLDEPTN 175
Cdd:TIGR03719 115 adfdklaaEQAE-LQEIIDAADA-WDLDSQLEIAMDALRCPPW--DADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTN 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 176 HLDRQGREWLYHQLESWQGGALIASHDRELLTRMPR-IIELTPTALRSYGGNYDEYqrqrmAEQQAARAALEhAVTDRRR 254
Cdd:TIGR03719 191 HLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGwILELDRGRGIPWEGNYSSW-----LEQKQKRLEQE-EKEESAR 264
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 255 TRArMQKEHDAAqRRSAQTLRTVDTLNIASFERVkykgaakerpgalrrqhreqnssLNAAVQQARERVEeetpvMFTLP 334
Cdd:TIGR03719 265 QKT-LKRELEWV-RQSPKGRQAKSKARLARYEEL-----------------------LSQEFQKRNETAE-----IYIPP 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 335 GSEVaaGKQVLVVESLQ--------LDHapaapLNWRIDGPMRIALKGPNGCGKTTLLKTLLGLEQAASGDVRL--SVSA 404
Cdd:TIGR03719 315 GPRL--GDKVIEAENLTkafgdkllIDD-----LSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgeTVKL 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 405 AYLDQHLTQLDLSLSVMAHLSledtpldEGLLRTRLAQLQL------------GADKVTLpLSALSGGERLKAALACVLw 472
Cdd:TIGR03719 388 AYVDQSRDALDPNKTVWEEIS-------GGLDIIKLGKREIpsrayvgrfnfkGSDQQKK-VGQLSGGERNRVHLAKTL- 458
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1512845752 473 rREPAQLLLLDEPTNHLDLASTQAIESALAAFPGAMLVVSHDEAFLQGLKlTHSLAWRETS 533
Cdd:TIGR03719 459 -KSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIA-THILAFEGDS 517
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
40-517 1.14e-43

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 164.35  E-value: 1.14e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  40 LVGRNGVGKTRLLRLLAG---LDSpagGHI--ERAAAVAWVAQQPTLTPETT--------LATLLGYASVFAALSR---- 102
Cdd:PRK11147   34 LVGRNGAGKSTLMKILNGevlLDD---GRIiyEQDLIVARLQQDPPRNVEGTvydfvaegIEEQAEYLKRYHDISHlvet 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 103 ------LEQGQGLADDFDLLDGhWDLTDRLSLAFREADLPPfsaDRPAFSLSGGERMKALLCGAFVSGADYLLLDEPTNH 176
Cdd:PRK11147  111 dpseknLNELAKLQEQLDHHNL-WQLENRINEVLAQLGLDP---DAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNH 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 177 LDRQGREWLYHQLESWQGGALIASHDRELLTRMP-RIIELTPTALRSYGGNYDEYQrqrMAEQQAARA-ALEHAVTDRRR 254
Cdd:PRK11147  187 LDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMAtRIVDLDRGKLVSYPGNYDQYL---LEKEEALRVeELQNAEFDRKL 263
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 255 TrarmQKEhdAAQRRSAQTLRTVDtlniasfE-RVKykgAAKerpgALRRQHREQNSSLNAAVQQarerVEEETpvmftl 333
Cdd:PRK11147  264 A----QEE--VWIRQGIKARRTRN-------EgRVR---ALK----ALRRERSERREVMGTAKMQ----VEEAS------ 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 334 pgsevAAGKQVLVVESLqldhapaaplNWRIDGPM-------------RIALKGPNGCGKTTLLKTLLGLEQAASGDVR- 399
Cdd:PRK11147  314 -----RSGKIVFEMENV----------NYQIDGKQlvkdfsaqvqrgdKIALIGPNGCGKTTLLKLMLGQLQADSGRIHc 378
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 400 ---LSVsaAYLDQHLTQLDLSLSVMAHLSL-EDTPLDEGLLRTRLAQLQ--LGADKVTL-PLSALSGGERLKAALACVLW 472
Cdd:PRK11147  379 gtkLEV--AYFDQHRAELDPEKTVMDNLAEgKQEVMVNGRPRHVLGYLQdfLFHPKRAMtPVKALSGGERNRLLLARLFL 456
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*
gi 1512845752 473 RrePAQLLLLDEPTNHLDLASTQAIESALAAFPGAMLVVSHDEAF 517
Cdd:PRK11147  457 K--PSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQF 499
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
22-217 8.82e-31

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: 116.78  E-value: 8.82e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  22 GQTLFGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIERAaavawvaqqPTLTpettlatlLGYasvfaal 100
Cdd:cd03221    12 GKLLLKDISLTINPgDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG---------STVK--------IGY------- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 101 srLEQgqgladdfdlldghwdltdrlslafreadlppfsadrpafsLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQ 180
Cdd:cd03221    68 --FEQ-----------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLE 104
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1512845752 181 GREWLYHQLESWQGGALIASHDRELLTRMP-RIIELTP 217
Cdd:cd03221   105 SIEALEEALKEYPGTVILVSHDRYFLDQVAtKIIELED 142
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
26-175 3.03e-19

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: 84.62  E-value: 3.03e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  26 FGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIERAAAVAWVAQQ-------------PTLTPETTLATLL 91
Cdd:pfam00005   1 LKNVSLTLNPgEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERkslrkeigyvfqdPQLFPRLTVRENL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  92 GYASVFAALSRLEQGQGLADDFDLLDGhWDLTDRLslafreadlppfsADRPAFSLSGGERMKALLCGAFVSGADYLLLD 171
Cdd:pfam00005  81 RLGLLLKGLSKREKDARAEEALEKLGL-GDLADRP-------------VGERPGTLSGGQRQRVAIARALLTKPKLLLLD 146

                  ....
gi 1512845752 172 EPTN 175
Cdd:pfam00005 147 EPTA 150
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
11-215 3.73e-13

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 68.03  E-value: 3.73e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  11 VLHQVTCQFATGqtlfgplsvslepSLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIERAAAVAWVAQqPTLT--PETTLA 88
Cdd:NF040873    7 VLHGVDLTIPAG-------------SLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYV-PQRSevPDSLPL 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  89 TLLGYASVFAALSRLEQGQGLADDFDLLDghwDLTDRLSLAfreaDLppfsADRPAFSLSGGERMKALLCGAFVSGADYL 168
Cdd:NF040873   73 TVRDLVAMGRWARRGLWRRLTRDDRAAVD---DALERVGLA----DL----AGRQLGELSGGQRQRALLAQGLAQEADLL 141
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1512845752 169 LLDEPTNHLDRQGREWLYHQLESWQG---GALIASHDRELLTRMPRIIEL 215
Cdd:NF040873  142 LLDEPTTGLDAESRERIIALLAEEHArgaTVVVVTHDLELVRRADPCVLL 191
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
453-516 1.57e-08

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 54.55  E-value: 1.57e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1512845752 453 PLSALSGGERLKAALACVLWRRepAQLLLLDEPTNHLDLASTQAIESALAAFPG---AMLVVSHDEA 516
Cdd:NF040873  116 QLGELSGGQRQRALLAQGLAQE--ADLLLLDEPTTGLDAESRERIIALLAEEHArgaTVVVVTHDLE 180
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
31-174 1.93e-04

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 44.35  E-value: 1.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  31 VSLE-PS--LCGLVGRNGVGKTRLLRLLAGLDSPAGGHIE------RAAAVAWVAQQ--------------PTLTPETTL 87
Cdd:NF033858   20 VSLDiPAgcMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEvlggdmADARHRRAVCPriaympqglgknlyPTLSVFENL 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  88 ---ATLLGyasvfaaLSRLEQGQGLADdfdlldghwdLTDRLSLAfreadlpPFsADRPAFSLSGGERMKALLCGAFVSG 164
Cdd:NF033858  100 dffGRLFG-------QDAAERRRRIDE----------LLRATGLA-------PF-ADRPAGKLSGGMKQKLGLCCALIHD 154
                         170
                  ....*....|
gi 1512845752 165 ADYLLLDEPT 174
Cdd:NF033858  155 PDLLILDEPT 164
 
Name Accession Description Interval E-value
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
12-521 1.22e-91

ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 290.04  E-value: 1.22e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  12 LHQVTCQFAtGQTLFGPLSVSLEPSLC-GLVGRNGVGKTRLLRLLAGLDSPAGGHIERAAAVAWVAQQ--PTLTPETTL- 87
Cdd:COG0488     1 LENLSKSFG-GRPLLDDVSLSINPGDRiGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPqePPLDDDLTVl 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  88 -ATLLGYASVFAALSRLEQGQG--------------LADDFDLLDGhWDLTDRLS-----LAFREADLppfsaDRPAFSL 147
Cdd:COG0488    80 dTVLDGDAELRALEAELEELEAklaepdedlerlaeLQEEFEALGG-WEAEARAEeilsgLGFPEEDL-----DRPVSEL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 148 SGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGREWLYHQLESWQGGALIASHDRELLTRM-PRIIELTPTALRSYGGN 226
Cdd:COG0488   154 SGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVaTRILELDRGKLTLYPGN 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 227 YDEYQRQRmAEQQAARAAlehavtDRRRTRARMQKEHDAAQRRSAQtlrtvdtlniASfervKYKgAAKERPGALRRqhr 306
Cdd:COG0488   234 YSAYLEQR-AERLEQEAA------AYAKQQKKIAKEEEFIRRFRAK----------AR----KAK-QAQSRIKALEK--- 288
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 307 eqnssLNAAVQQARERveeetPVMFTLPGSEvAAGKQVLVVESLQ--------LDHapaapLNWRIDGPMRIALKGPNGC 378
Cdd:COG0488   289 -----LEREEPPRRDK-----TVEIRFPPPE-RLGKKVLELEGLSksygdktlLDD-----LSLRIDRGDRIGLIGPNGA 352
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 379 gkttllktllgLEQAASGDVRL--SVSAAYLDQHLTQLDLSLSVMAHLSLEDTPLDEGLLRTRLAQLQLGADKVTLPLSA 456
Cdd:COG0488   353 gkstllkllagELEPDSGTVKLgeTVKIGYFDQHQEELDPDKTVLDELRDGAPGGTEQEVRGYLGRFLFSGDDAFKPVGV 432
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1512845752 457 LSGGERLKAALACVLWRrePAQLLLLDEPTNHLDLASTQAIESALAAFPGAMLVVSHDEAFLQGL 521
Cdd:COG0488   433 LSGGEKARLALAKLLLS--PPNVLLLDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRV 495
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
39-533 3.06e-45

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: 167.42  E-value: 3.06e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  39 GLVGRNGVGKTRLLRLLAGLDSPAGGHIERAAAVAW--VAQQPTLTPETTL--ATLLGYASVFAALSRL----------- 103
Cdd:TIGR03719  35 GVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVgyLPQEPQLDPTKTVreNVEEGVAEIKDALDRFneisakyaepd 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 104 --------EQGQgLADDFDLLDGhWDLTDRLSLAFREADLPPFsaDRPAFSLSGGERMKALLCGAFVSGADYLLLDEPTN 175
Cdd:TIGR03719 115 adfdklaaEQAE-LQEIIDAADA-WDLDSQLEIAMDALRCPPW--DADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTN 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 176 HLDRQGREWLYHQLESWQGGALIASHDRELLTRMPR-IIELTPTALRSYGGNYDEYqrqrmAEQQAARAALEhAVTDRRR 254
Cdd:TIGR03719 191 HLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGwILELDRGRGIPWEGNYSSW-----LEQKQKRLEQE-EKEESAR 264
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 255 TRArMQKEHDAAqRRSAQTLRTVDTLNIASFERVkykgaakerpgalrrqhreqnssLNAAVQQARERVEeetpvMFTLP 334
Cdd:TIGR03719 265 QKT-LKRELEWV-RQSPKGRQAKSKARLARYEEL-----------------------LSQEFQKRNETAE-----IYIPP 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 335 GSEVaaGKQVLVVESLQ--------LDHapaapLNWRIDGPMRIALKGPNGCGKTTLLKTLLGLEQAASGDVRL--SVSA 404
Cdd:TIGR03719 315 GPRL--GDKVIEAENLTkafgdkllIDD-----LSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgeTVKL 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 405 AYLDQHLTQLDLSLSVMAHLSledtpldEGLLRTRLAQLQL------------GADKVTLpLSALSGGERLKAALACVLw 472
Cdd:TIGR03719 388 AYVDQSRDALDPNKTVWEEIS-------GGLDIIKLGKREIpsrayvgrfnfkGSDQQKK-VGQLSGGERNRVHLAKTL- 458
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1512845752 473 rREPAQLLLLDEPTNHLDLASTQAIESALAAFPGAMLVVSHDEAFLQGLKlTHSLAWRETS 533
Cdd:TIGR03719 459 -KSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIA-THILAFEGDS 517
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
40-517 1.14e-43

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 164.35  E-value: 1.14e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  40 LVGRNGVGKTRLLRLLAG---LDSpagGHI--ERAAAVAWVAQQPTLTPETT--------LATLLGYASVFAALSR---- 102
Cdd:PRK11147   34 LVGRNGAGKSTLMKILNGevlLDD---GRIiyEQDLIVARLQQDPPRNVEGTvydfvaegIEEQAEYLKRYHDISHlvet 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 103 ------LEQGQGLADDFDLLDGhWDLTDRLSLAFREADLPPfsaDRPAFSLSGGERMKALLCGAFVSGADYLLLDEPTNH 176
Cdd:PRK11147  111 dpseknLNELAKLQEQLDHHNL-WQLENRINEVLAQLGLDP---DAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNH 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 177 LDRQGREWLYHQLESWQGGALIASHDRELLTRMP-RIIELTPTALRSYGGNYDEYQrqrMAEQQAARA-ALEHAVTDRRR 254
Cdd:PRK11147  187 LDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMAtRIVDLDRGKLVSYPGNYDQYL---LEKEEALRVeELQNAEFDRKL 263
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 255 TrarmQKEhdAAQRRSAQTLRTVDtlniasfE-RVKykgAAKerpgALRRQHREQNSSLNAAVQQarerVEEETpvmftl 333
Cdd:PRK11147  264 A----QEE--VWIRQGIKARRTRN-------EgRVR---ALK----ALRRERSERREVMGTAKMQ----VEEAS------ 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 334 pgsevAAGKQVLVVESLqldhapaaplNWRIDGPM-------------RIALKGPNGCGKTTLLKTLLGLEQAASGDVR- 399
Cdd:PRK11147  314 -----RSGKIVFEMENV----------NYQIDGKQlvkdfsaqvqrgdKIALIGPNGCGKTTLLKLMLGQLQADSGRIHc 378
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 400 ---LSVsaAYLDQHLTQLDLSLSVMAHLSL-EDTPLDEGLLRTRLAQLQ--LGADKVTL-PLSALSGGERLKAALACVLW 472
Cdd:PRK11147  379 gtkLEV--AYFDQHRAELDPEKTVMDNLAEgKQEVMVNGRPRHVLGYLQdfLFHPKRAMtPVKALSGGERNRLLLARLFL 456
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*
gi 1512845752 473 RrePAQLLLLDEPTNHLDLASTQAIESALAAFPGAMLVVSHDEAF 517
Cdd:PRK11147  457 K--PSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQF 499
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
39-519 1.87e-38

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 149.16  E-value: 1.87e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  39 GLVGRNGVGKTRLLRLLAGLDSPAGGHI---ERAAAVAWVAQQPTLTPETTLATLLG---YASVFAALSRL-EQGQGLAd 111
Cdd:PRK10636   31 GLVGKNGCGKSTLLALLKNEISADGGSYtfpGNWQLAWVNQETPALPQPALEYVIDGdreYRQLEAQLHDAnERNDGHA- 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 112 dFDLLDGHWDLTDRLSLAFREADLPP---FSAD---RPAFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGREWL 185
Cdd:PRK10636  110 -IATIHGKLDAIDAWTIRSRAASLLHglgFSNEqleRPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWL 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 186 YHQLESWQGGALIASHDRELLTRM-PRIIELTPTALRSYGGNYDEYQRQR---MAEQQA------ARAALEHAVTDRRRT 255
Cdd:PRK10636  189 EKWLKSYQGTLILISHDRDFLDPIvDKIIHIEQQSLFEYTGNYSSFEVQRatrLAQQQAmyesqqERVAHLQSYIDRFRA 268
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 256 RARMQKEhdaAQRRsaqtlrtvdtlnIASFERVKYKGAAK-ERPgaLRRQHREQNSSLNaavqqarerveeetPVmftLP 334
Cdd:PRK10636  269 KATKAKQ---AQSR------------IKMLERMELIAPAHvDNP--FHFSFRAPESLPN--------------PL---LK 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 335 GSEVAAG-KQVLVVESLQLDHAPAAplnwridgpmRIALKGPNGCGKTTLLKTLLGLEQAASGDVRLS--VSAAYLDQH- 410
Cdd:PRK10636  315 MEKVSAGyGDRIILDSIKLNLVPGS----------RIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAkgIKLGYFAQHq 384
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 411 LTQLDLSLSVMAHLSLEDTPLDEGLLRTRLAQLQLGADKVTLPLSALSGGERLKAALACVLWRRepAQLLLLDEPTNHLD 490
Cdd:PRK10636  385 LEFLRADESPLQHLARLAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQR--PNLLLLDEPTNHLD 462
                         490       500
                  ....*....|....*....|....*....
gi 1512845752 491 LASTQAIESALAAFPGAMLVVSHDEAFLQ 519
Cdd:PRK10636  463 LDMRQALTEALIDFEGALVVVSHDRHLLR 491
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
39-536 7.65e-38

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 146.42  E-value: 7.65e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  39 GLVGRNGVGKTRLLRLLAGLDSPAGGHI-------------EraaavawvaqqPTLTPETTL--ATLLGYASVFAALSRL 103
Cdd:PRK11819   37 GVLGLNGAGKSTLLRIMAGVDKEFEGEArpapgikvgylpqE-----------PQLDPEKTVreNVEEGVAEVKAALDRF 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 104 -------------------EQGQgLADDFDLLDGhWDLTDRLSLAfreAD---LPPfsADRPAFSLSGGERMKALLCGAF 161
Cdd:PRK11819  106 neiyaayaepdadfdalaaEQGE-LQEIIDAADA-WDLDSQLEIA---MDalrCPP--WDAKVTKLSGGERRRVALCRLL 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 162 VSGADYLLLDEPTNHLDRQGREWLYHQLESWQGGALIASHDRELLTRMPR-IIELTPTALRSYGGNYDEYqrqrmAEQQA 240
Cdd:PRK11819  179 LEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGwILELDRGRGIPWEGNYSSW-----LEQKA 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 241 ARAALEhAVTDRRRTRArMQKEHD-----AAQRRSAQTLRtvdtlnIASFErvkykgaakerpgalrrqhreqnsSLNAA 315
Cdd:PRK11819  254 KRLAQE-EKQEAARQKA-LKRELEwvrqsPKARQAKSKAR------LARYE------------------------ELLSE 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 316 VQQARERVEEetpvMFTLPGSEVaaGKQVLVVESLQ--------LDHapaapLNWRIDGPMRIALKGPNGCGKTTLLKTL 387
Cdd:PRK11819  302 EYQKRNETNE----IFIPPGPRL--GDKVIEAENLSksfgdrllIDD-----LSFSLPPGGIVGIIGPNGAGKSTLFKMI 370
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 388 LGLEQAASGDVRL--SVSAAYLDQHLTQLDLSLSVMAHLSledtpldEGLLRTRLAQLQL------------GAD---KV 450
Cdd:PRK11819  371 TGQEQPDSGTIKIgeTVKLAYVDQSRDALDPNKTVWEEIS-------GGLDIIKVGNREIpsrayvgrfnfkGGDqqkKV 443
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 451 tlplSALSGGERLKAALACVLwrREPAQLLLLDEPTNHLDLASTQAIESALAAFPGAMLVVSHDEAFLQGLKlTHSLAWR 530
Cdd:PRK11819  444 ----GVLSGGERNRLHLAKTL--KQGGNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRIA-THILAFE 516

                  ....*..
gi 1512845752 531 ETS-WHF 536
Cdd:PRK11819  517 GDSqVEW 523
PLN03073 PLN03073
ABC transporter F family; Provisional
39-520 1.27e-34

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 138.45  E-value: 1.27e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  39 GLVGRNGVGKTRLLRLLA---------------------GLDSPA-----GGHIERAA--AVAWVAQQPTLTPETTLATL 90
Cdd:PLN03073  207 GLVGRNGTGKTTFLRYMAmhaidgipkncqilhveqevvGDDTTAlqcvlNTDIERTQllEEEAQLVAQQRELEFETETG 286
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  91 LGYASVFAALSRLEQGQGLADDFDLLDghwdLTDRLSLAFREADLPP---FSAD---RPAFSLSGGERMKALLCGAFVSG 164
Cdd:PLN03073  287 KGKGANKDGVDKDAVSQRLEEIYKRLE----LIDAYTAEARAASILAglsFTPEmqvKATKTFSGGWRMRIALARALFIE 362
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 165 ADYLLLDEPTNHLDRQGREWLYHQLESWQGGALIASHDRELL-TRMPRIIELTPTALRSYGGNYDEYQR---QRMAEQQA 240
Cdd:PLN03073  363 PDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLnTVVTDILHLHGQKLVTYKGDYDTFERtreEQLKNQQK 442
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 241 ARAALEhavtdrrRTRARMQKEHDAAqRRSAQTLRTVDTlNIASFERVKYKGAAKERPGalrrqhreqnsslnaavqqar 320
Cdd:PLN03073  443 AFESNE-------RSRSHMQAFIDKF-RYNAKRASLVQS-RIKALDRLGHVDAVVNDPD--------------------- 492
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 321 erveeetpVMFTLPGSEVAAGKQVLVVESLQLDHaPAAP-----LNWRIDGPMRIALKGPNGCGKTTLLKTLLGLEQAAS 395
Cdd:PLN03073  493 --------YKFEFPTPDDRPGPPIISFSDASFGY-PGGPllfknLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSS 563
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 396 GDVRLSVS---AAYLDQHLTQLDLSLSVMAHLSLEDTPLDEGLLRTRLAQLQLGADKVTLPLSALSGGERLKAALACVLW 472
Cdd:PLN03073  564 GTVFRSAKvrmAVFSQHHVDGLDLSSNPLLYMMRCFPGVPEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITF 643
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 1512845752 473 RRepAQLLLLDEPTNHLDLASTQAIESALAAFPGAMLVVSHDEAFLQG 520
Cdd:PLN03073  644 KK--PHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISG 689
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
22-217 8.82e-31

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: 116.78  E-value: 8.82e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  22 GQTLFGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIERAaavawvaqqPTLTpettlatlLGYasvfaal 100
Cdd:cd03221    12 GKLLLKDISLTINPgDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG---------STVK--------IGY------- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 101 srLEQgqgladdfdlldghwdltdrlslafreadlppfsadrpafsLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQ 180
Cdd:cd03221    68 --FEQ-----------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLE 104
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1512845752 181 GREWLYHQLESWQGGALIASHDRELLTRMP-RIIELTP 217
Cdd:cd03221   105 SIEALEEALKEYPGTVILVSHDRYFLDQVAtKIIELED 142
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
39-233 7.89e-29

ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 119.78  E-value: 7.89e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  39 GLVGRNGVGKTRLLRLLAGLDSPAGGHIERAaavawvaqqPTLTpettlatlLGYasvfaalsrleqgqgLADDFDLLDG 118
Cdd:COG0488   345 GLIGPNGAGKSTLLKLLAGELEPDSGTVKLG---------ETVK--------IGY---------------FDQHQEELDP 392
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 119 HWDLTDRLSLAFREAD------------LPPFSADRPAFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGREWLY 186
Cdd:COG0488   393 DKTVLDELRDGAPGGTeqevrgylgrflFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALE 472
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1512845752 187 HQLESWQGGALIASHDRELLTRM-PRIIELTPTALRSYGGNYDEYQRQ 233
Cdd:COG0488   473 EALDDFPGTVLLVSHDRYFLDRVaTRILEFEDGGVREYPGGYDDYLEK 520
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
8-219 1.87e-27

ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443308 [Multi-domain]  Cd Length: 206  Bit Score: 109.49  E-value: 1.87e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752   8 PAFVLHQVTCQFAtGQTLFGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIERAAAVAWVAQQptlTPETT 86
Cdd:COG4133     1 MMLEAENLSCRRG-ERLLFSGLSFTLAAgEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARE---DYRRR 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  87 LATLLGYASVFAALSRLEQGQGLADdfdlLDGHWDLTDRLSLAFREADLPPFsADRPAFSLSGGERMKALLCGAFVSGAD 166
Cdd:COG4133    77 LAYLGHADGLKPELTVRENLRFWAA----LYGLRADREAIDEALEAVGLAGL-ADLPVRQLSAGQKRRVALARLLLSPAP 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1512845752 167 YLLLDEPTNHLDRQGREWLYHQLESW--QGGA-LIASHDRELLTRMpRIIELTPTA 219
Cdd:COG4133   152 LWLLDEPFTALDAAGVALLAELIAAHlaRGGAvLLTTHQPLELAAA-RVLDLGDFK 206
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
39-521 5.96e-26

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 111.52  E-value: 5.96e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  39 GLVGRNGVGKTRLLRLLAGLDSPAGGHIeraaavawvaqqpTLTPETTLATLlgyasvfaalsrlEQGQGLADDFDLLD- 117
Cdd:PRK15064   31 GLIGANGCGKSTFMKILGGDLEPSAGNV-------------SLDPNERLGKL-------------RQDQFAFEEFTVLDt 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 118 ---GHWDL------TDR-----------------LSLAFREAD----------------LP------PFSADRPAFSLsg 149
Cdd:PRK15064   85 vimGHTELwevkqeRDRiyalpemseedgmkvadLEVKFAEMDgytaearagelllgvgIPeeqhygLMSEVAPGWKL-- 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 150 germKALLCGAFVSGADYLLLDEPTNHLDRQGREWLYHQLESWQGGALIASHDRELL----TRMPriiELTPTALRSYGG 225
Cdd:PRK15064  163 ----RVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLnsvcTHMA---DLDYGELRVYPG 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 226 NYDEYqrqrMaeqQAARAALEHAVTDRRRTRARMQKEHDAAQRRSAQT---------LRTVDTLNIasfERVKykgaAKE 296
Cdd:PRK15064  236 NYDEY----M---TAATQARERLLADNAKKKAQIAELQSFVSRFSANAskakqatsrAKQIDKIKL---EEVK----PSS 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 297 RpgalrrqhreQNSSLnaavqqareRVEEETPvMFtlpgsevaagKQVLVVESLQ--LDHAPA-APLNWRIDGPMRIALK 373
Cdd:PRK15064  302 R----------QNPFI---------RFEQDKK-LH----------RNALEVENLTkgFDNGPLfKNLNLLLEAGERLAII 351
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 374 GPNGCGKTTLLKTLLGLEQAASGDVRLSVSAA--YLDQ-HLTQLDLSLSVMAHLSLEDTPL-DEGLLRTRLAQLQLGADK 449
Cdd:PRK15064  352 GENGVGKTTLLRTLVGELEPDSGTVKWSENANigYYAQdHAYDFENDLTLFDWMSQWRQEGdDEQAVRGTLGRLLFSQDD 431
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1512845752 450 VTLPLSALSGGE--RLkaalacvLWRR---EPAQLLLLDEPTNHLDLASTQAIESALAAFPGAMLVVSHDEAFLQGL 521
Cdd:PRK15064  432 IKKSVKVLSGGEkgRM-------LFGKlmmQKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSL 501
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
454-519 9.41e-24

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: 97.13  E-value: 9.41e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1512845752 454 LSALSGGERLKAALACVLWrrEPAQLLLLDEPTNHLDLASTQAIESALAAFPGAMLVVSHDEAFLQ 519
Cdd:cd03221    68 FEQLSGGEKMRLALAKLLL--ENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLD 131
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
9-190 9.52e-20

ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];


Pssm-ID: 440737 [Multi-domain]  Cd Length: 254  Bit Score: 88.95  E-value: 9.52e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752   9 AFVLHQVTCQFAtGQTLFGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIeraaavawvaqqpTL------ 81
Cdd:COG1120     1 MLEAENLSVGYG-GRPVLDDVSLSLPPgEVTALLGPNGSGKSTLLRALAGLLKPSSGEV-------------LLdgrdla 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  82 -TPETTLATLLGYasvfaalsrLEQGQGLADDFDLLD-------------GHWDLTDRL--SLAFREADLPPFsADRPAF 145
Cdd:COG1120    67 sLSRRELARRIAY---------VPQEPPAPFGLTVRElvalgryphlglfGRPSAEDREavEEALERTGLEHL-ADRPVD 136
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1512845752 146 SLSGGERMKALLCGAFVSGADYLLLDEPTNHLDrqgrewLYHQLE 190
Cdd:COG1120   137 ELSGGERQRVLIARALAQEPPLLLLDEPTSHLD------LAHQLE 175
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
10-220 2.30e-19

ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 86.41  E-value: 2.30e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  10 FVLHQVTCQFaTGQTLFGPLSVSLEPSLC-GLVGRNGVGKTRLLRLLAGLDSPAGGHIeraaaVAWVAQQPTLTPETtLA 88
Cdd:COG4619     1 LELEGLSFRV-GGKPILSPVSLTLEAGECvAITGPSGSGKSTLLRALADLDPPTSGEI-----YLDGKPLSAMPPPE-WR 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  89 TLLGYasVFAALSRLEQ--GQGLADDFDLLDGHWDlTDRLSLAFREADLPPFSADRPAFSLSGGERMKALLCGAFVSGAD 166
Cdd:COG4619    74 RQVAY--VPQEPALWGGtvRDNLPFPFQLRERKFD-RERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPD 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1512845752 167 YLLLDEPTNHLDRQGR----EWLYHQLESWQGGALIASHDRELLTRMP-RIIELTPTAL 220
Cdd:COG4619   151 VLLLDEPTSALDPENTrrveELLREYLAEEGRAVLWVSHDPEQIERVAdRVLTLEAGRL 209
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
26-175 3.03e-19

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: 84.62  E-value: 3.03e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  26 FGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIERAAAVAWVAQQ-------------PTLTPETTLATLL 91
Cdd:pfam00005   1 LKNVSLTLNPgEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERkslrkeigyvfqdPQLFPRLTVRENL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  92 GYASVFAALSRLEQGQGLADDFDLLDGhWDLTDRLslafreadlppfsADRPAFSLSGGERMKALLCGAFVSGADYLLLD 171
Cdd:pfam00005  81 RLGLLLKGLSKREKDARAEEALEKLGL-GDLADRP-------------VGERPGTLSGGQRQRVAIARALLTKPKLLLLD 146

                  ....
gi 1512845752 172 EPTN 175
Cdd:pfam00005 147 EPTA 150
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
22-202 9.47e-19

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: 84.02  E-value: 9.47e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  22 GQTLFGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIEraaavaWVAQQPTLTPETTLATLLGYasVFAAL 100
Cdd:cd03214    11 GRTVLDDLSLSIEAgEIVGILGPNGAGKSTLLKTLAGLLKPSSGEIL------LDGKDLASLSPKELARKIAY--VPQAL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 101 SRLEqgqglADDFdlldghwdltdrlslafreadlppfsADRPAFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDrq 180
Cdd:cd03214    83 ELLG-----LAHL--------------------------ADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLD-- 129
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1512845752 181 grewLYHQLE----------SWQGGALIASHD 202
Cdd:cd03214   130 ----IAHQIEllellrrlarERGKTVVMVLHD 157
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
22-237 1.75e-18

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 88.41  E-value: 1.75e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  22 GQTLFGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIERAAAVAwvaqqptltpettlatlLGYasvFAal 100
Cdd:PRK15064  331 NGPLFKNLNLLLEAgERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENAN-----------------IGY---YA-- 388
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 101 srleqgQGLADDFDlldGHWDLTDRLSLAFREAD------------LppFSAD---RPAFSLSGGERMKALLCGAFVSGA 165
Cdd:PRK15064  389 ------QDHAYDFE---NDLTLFDWMSQWRQEGDdeqavrgtlgrlL--FSQDdikKSVKVLSGGEKGRMLFGKLMMQKP 457
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1512845752 166 DYLLLDEPTNHLDRQGREWLYHQLESWQGGALIASHDRELLTRMP-RIIELTPTALRSYGGNYDEYQRQRMAE 237
Cdd:PRK15064  458 NVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLAtRIIEITPDGVVDFSGTYEEYLRSQGIE 530
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
12-209 2.35e-18

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: 84.52  E-value: 2.35e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  12 LHQVTCQFATGQTLfGPLSVSLEPS-LCGLVGRNGVGKTRLLRLLAGLDSPAGGHI---------ERAAAVAWVAQQPTL 81
Cdd:COG4555     4 VENLSKKYGKVPAL-KDVSFTAKDGeITGLLGPNGAGKTTLLRMLAGLLKPDSGSIlidgedvrkEPREARRQIGVLPDE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  82 TPETTLATLLGYASVFAALSRLeQGQGLADDFDlldghwDLTDRLslafreaDLPPFsADRPAFSLSGGERMKALLCGAF 161
Cdd:COG4555    83 RGLYDRLTVRENIRYFAELYGL-FDEELKKRIE------ELIELL-------GLEEF-LDRRVGELSTGMKKKVALARAL 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1512845752 162 VSGADYLLLDEPTNHLDRQGREWLYHQLESW--QGGA-LIASHDRELLTRM 209
Cdd:COG4555   148 VHDPKVLLLDEPTNGLDVMARRLLREILRALkkEGKTvLFSSHIMQEVEAL 198
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
11-215 2.64e-18

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: 83.74  E-value: 2.64e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  11 VLHQVTCQFATGqtlfgplsvslepSLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIERAAAvawvaqqptltPETTLATL 90
Cdd:cd03235    14 VLEDVSFEVKPG-------------EFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK-----------PLEKERKR 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  91 LGYASVFAALSRleqgqgladDFDL---------LDGHWDLTDRLSLAFREA-----------DLppfsADRPAFSLSGG 150
Cdd:cd03235    70 IGYVPQRRSIDR---------DFPIsvrdvvlmgLYGHKGLFRRLSKADKAKvdealervglsEL----ADRQIGELSGG 136
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1512845752 151 ERMKALLCGAFVSGADYLLLDEPTNHLDRQGREWLYHQLESWQG---GALIASHDRELLTR-MPRIIEL 215
Cdd:cd03235   137 QQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRRegmTILVVTHDLGLVLEyFDRVLLL 205
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
8-215 4.85e-18

ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 83.60  E-value: 4.85e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752   8 PAFVLHQVTCQFAtGQTLFGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIERAAavawvaqqptlTPETT 86
Cdd:COG1121     5 PAIELENLTVSYG-GRPVLEDVSLTIPPgEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFG-----------KPPRR 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  87 LATLLGYasvfaalsrLEQGQGLADDF-----DL----LDGHWDLTDRLSLAFREA--------DLPPFsADRPAFSLSG 149
Cdd:COG1121    73 ARRRIGY---------VPQRAEVDWDFpitvrDVvlmgRYGRRGLFRRPSRADREAvdealervGLEDL-ADRPIGELSG 142
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 150 GERMKALLCGAFVSGADYLLLDEPTNHLDRQGREWLYHQLESW--QGGALIA-SHDRELLTRM-PRIIEL 215
Cdd:COG1121   143 GQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELrrEGKTILVvTHDLGAVREYfDRVLLL 212
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
29-215 5.74e-17

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: 78.59  E-value: 5.74e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  29 LSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIERaaavawvaqqptltpettlatllgyasvfaalsrleqgq 107
Cdd:cd03230    19 ISLTVEKgEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKV--------------------------------------- 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 108 glaDDFDLLDGHWDLTDRLSLAFREADLPP-FSAdRPAFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGREWLY 186
Cdd:cd03230    60 ---LGKDIKKEPEEVKRRIGYLPEEPSLYEnLTV-RENLKLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFW 135
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1512845752 187 HQLESW--QGGA-LIASHD-RELLTRMPRIIEL 215
Cdd:cd03230   136 ELLRELkkEGKTiLLSSHIlEEAERLCDRVAIL 168
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
12-201 3.79e-16

heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]


Pssm-ID: 273491 [Multi-domain]  Cd Length: 198  Bit Score: 77.01  E-value: 3.79e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  12 LHQVTCQfATGQTLFGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIEraaavAWVAQQPTLTPETTLATL 90
Cdd:TIGR01189   3 ARNLACS-RGERMLFEGLSFTLNAgEALQVTGPNGIGKTTLLRILAGLLRPDSGEVR-----WNGTPLAEQRDEPHENIL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  91 -LGYAS-VFAALSRLEQGQGLADDFDLLDGH-WDLTDRLSLAFREadlppfsaDRPAFSLSGGERMKALLCGAFVSGADY 167
Cdd:TIGR01189  77 yLGHLPgLKPELSALENLHFWAAIHGGAQRTiEDALAAVGLTGFE--------DLPAAQLSAGQQRRLALARLWLSRRPL 148
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1512845752 168 LLLDEPTNHLDRQGREWLYHQLESW---QGGALIASH 201
Cdd:TIGR01189 149 WILDEPTTALDKAGVALLAGLLRAHlarGGIVLLTTH 185
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
12-215 5.82e-16

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: 75.36  E-value: 5.82e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  12 LHQVTCQFAtGQTLFGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIEraaavawvaqqptltpettlatl 90
Cdd:cd00267     2 IENLSFRYG-GRTALDNVSLTLKAgEIVALVGPNGSGKSTLLRAIAGLLKPTSGEIL----------------------- 57
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  91 lgyasvfaalsrleqgqgladdfdlLDGHwDLTDRLSLAFReadlppfsaDRPA--FSLSGGERMKALLCGAFVSGADYL 168
Cdd:cd00267    58 -------------------------IDGK-DIAKLPLEELR---------RRIGyvPQLSGGQRQRVALARALLLNPDLL 102
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1512845752 169 LLDEPTNHLDRQGREWLYHQLESW-QGGA--LIASHDRELLTRMP-RIIEL 215
Cdd:cd00267   103 LLDEPTSGLDPASRERLLELLRELaEEGRtvIIVTHDPELAELAAdRVIVL 153
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
10-215 1.03e-15

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: 76.60  E-value: 1.03e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  10 FVLHQVTCQFATGQTLFGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIEraaavaWVAQQPTLTPETTLA 88
Cdd:COG1122     1 IELENLSFSYPGGTPALDDVSLSIEKgEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVL------VDGKDITKKNLRELR 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  89 TLLGY-----------ASVFA--ALSrLEQgQGLADDfdlldghwDLTDRLSLAFREADLPPFsADRPAFSLSGGERMKA 155
Cdd:COG1122    75 RKVGLvfqnpddqlfaPTVEEdvAFG-PEN-LGLPRE--------EIRERVEEALELVGLEHL-ADRPPHELSGGQKQRV 143
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1512845752 156 LLCGAFVSGADYLLLDEPTNHLDRQGREWLYHQLESW--QGGALI-ASHDRELLTRM-PRIIEL 215
Cdd:COG1122   144 AIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLnkEGKTVIiVTHDLDLVAELaDRVIVL 207
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
29-202 1.61e-15

ABC-type multidrug transport system, ATPase component [Defense mechanisms];


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 75.87  E-value: 1.61e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  29 LSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIE------RAAAVAWVAQ------QPTLTPETTLATLLGYas 95
Cdd:COG1131    19 VSLTVEPgEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRvlgedvARDPAEVRRRigyvpqEPALYPDLTVRENLRF-- 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  96 vFAALSRLEQGQGLADDFDLLDgHWDLTDRlslafreadlppfsADRPAFSLSGGERMKALLCGAFVSGADYLLLDEPTN 175
Cdd:COG1131    97 -FARLYGLPRKEARERIDELLE-LFGLTDA--------------ADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
                         170       180       190
                  ....*....|....*....|....*....|
gi 1512845752 176 HLDRQGREWLYHQLESW--QGGA-LIASHD 202
Cdd:COG1131   161 GLDPEARRELWELLRELaaEGKTvLLSTHY 190
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
11-206 2.88e-15

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: 74.81  E-value: 2.88e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  11 VLHQVTCQFATGQT-LFGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIERAAAVAWVAQQPTLT------ 82
Cdd:cd03225     1 ELKNLSFSYPDGARpALDDISLTIKKgEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRrkvglv 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  83 ---PETTLATLlgyaSVFA--ALSrLEQgQGLADDfdlldghwDLTDRLSLAFREADLPPFsADRPAFSLSGGERMKALL 157
Cdd:cd03225    81 fqnPDDQFFGP----TVEEevAFG-LEN-LGLPEE--------EIEERVEEALELVGLEGL-RDRSPFTLSGGQKQRVAI 145
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1512845752 158 CGAFVSGADYLLLDEPTNHLDRQGREWLYHQLESWQG---GALIASHDRELL 206
Cdd:cd03225   146 AGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAegkTIIIVTHDLDLL 197
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
419-519 1.82e-13

ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 69.46  E-value: 1.82e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 419 SVMAHL----SLEDTPLDEGLLRTRLAQLQLGADKVTLPLSALSGGERLKAALACVLwRREPaQLLLLDEPTNHLDLAST 494
Cdd:COG4619    89 TVRDNLpfpfQLRERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRAL-LLQP-DVLLLDEPTSALDPENT 166
                          90       100
                  ....*....|....*....|....*....
gi 1512845752 495 QAIESALAAFP----GAMLVVSHDEAFLQ 519
Cdd:COG4619   167 RRVEELLREYLaeegRAVLWVSHDPEQIE 195
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
11-215 3.73e-13

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 68.03  E-value: 3.73e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  11 VLHQVTCQFATGqtlfgplsvslepSLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIERAAAVAWVAQqPTLT--PETTLA 88
Cdd:NF040873    7 VLHGVDLTIPAG-------------SLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYV-PQRSevPDSLPL 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  89 TLLGYASVFAALSRLEQGQGLADDFDLLDghwDLTDRLSLAfreaDLppfsADRPAFSLSGGERMKALLCGAFVSGADYL 168
Cdd:NF040873   73 TVRDLVAMGRWARRGLWRRLTRDDRAAVD---DALERVGLA----DL----AGRQLGELSGGQRQRALLAQGLAQEADLL 141
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1512845752 169 LLDEPTNHLDRQGREWLYHQLESWQG---GALIASHDRELLTRMPRIIEL 215
Cdd:NF040873  142 LLDEPTTGLDAESRERIIALLAEEHArgaTVVVVTHDLELVRRADPCVLL 191
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
39-213 4.43e-13

ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.


Pssm-ID: 213212 [Multi-domain]  Cd Length: 220  Bit Score: 68.39  E-value: 4.43e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  39 GLVGRNGVGKTRLLRLLAGLDSPAGGHIeraaavawvaqqptLTPETTLATL--------LGY----ASVFAALSR--LE 104
Cdd:cd03245    34 AIIGRVGSGKSTLLKLLAGLYKPTSGSV--------------LLDGTDIRQLdpadlrrnIGYvpqdVTLFYGTLRdnIT 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 105 QGQGLADDFDLLDghwdltdrlslAFREADLPPFSADRPA----------FSLSGGERMKALLCGAFVSGADYLLLDEPT 174
Cdd:cd03245   100 LGAPLADDERILR-----------AAELAGVTDFVNKHPNgldlqigergRGLSGGQRQAVALARALLNDPPILLLDEPT 168
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1512845752 175 NHLDRQGREWLYHQLESWQGG--ALIASHDRELLTRMPRII 213
Cdd:cd03245   169 SAMDMNSEERLKERLRQLLGDktLIIITHRPSLLDLVDRII 209
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
25-235 5.90e-13

ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.


Pssm-ID: 274744 [Multi-domain]  Cd Length: 552  Bit Score: 71.12  E-value: 5.90e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  25 LFGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIEraaavawvaqqptlTPETT-LA-------TLLGYAS 95
Cdd:TIGR03719 337 LIDDLSFKLPPgGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIE--------------IGETVkLAyvdqsrdALDPNKT 402
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  96 VFAALSrleqgqglaDDFDLLD-GHWDLTDRLSLA---FREADlppfsADRPAFSLSGGERMKALLCGAFVSGADYLLLD 171
Cdd:TIGR03719 403 VWEEIS---------GGLDIIKlGKREIPSRAYVGrfnFKGSD-----QQKKVGQLSGGERNRVHLAKTLKSGGNVLLLD 468
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1512845752 172 EPTNHLDRQGREWLYHQLESWQGGALIASHDRELLTRMP-RIIELTPTA-LRSYGGNYDEYQRQRM 235
Cdd:TIGR03719 469 EPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIAtHILAFEGDShVEWFEGNFSEYEEDKK 534
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
39-208 7.85e-13

Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.


Pssm-ID: 213193 [Multi-domain]  Cd Length: 205  Bit Score: 67.67  E-value: 7.85e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  39 GLVGRNGVGKTRLLRLLAGLDSPAGGHIE---RAAAVAWVAQQPTLTPETTlATLLGYASVFAAL--------SRLEQGQ 107
Cdd:cd03226    30 ALTGKNGAGKTTLAKILAGLIKESSGSILlngKPIKAKERRKSIGYVMQDV-DYQLFTDSVREELllglkeldAGNEQAE 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 108 GLADDFDLldghWDLtdrlslafreadlppfsADRPAFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGREW--- 184
Cdd:cd03226   109 TVLKDLDL----YAL-----------------KERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERvge 167
                         170       180
                  ....*....|....*....|....*
gi 1512845752 185 LYHQLESwQGGA-LIASHDRELLTR 208
Cdd:cd03226   168 LIRELAA-QGKAvIVITHDYEFLAK 191
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
5-215 1.56e-12

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: 69.79  E-value: 1.56e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752   5 AHIPAFVLHQVTCQFATGQTLFGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIEraaavAWVAQQPTLTP 83
Cdd:COG4988   332 AGPPSIELEDVSFSYPGGRPALDGLSLTIPPgERVALVGPSGAGKSTLLNLLLGFLPPYSGSIL-----INGVDLSDLDP 406
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  84 ETtLATLLGYAS----VFAAlsrleqgqGLADDfdLLDGHWDLTD-RLSLAFREADLPPFSADRP----------AFSLS 148
Cdd:COG4988   407 AS-WRRQIAWVPqnpyLFAG--------TIREN--LRLGRPDASDeELEAALEAAGLDEFVAALPdgldtplgegGRGLS 475
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1512845752 149 GGERMKALLCGAFVSGADYLLLDEPTNHLDRQGREWLYHQLESWQGGA--LIASHDRELLTRMPRIIEL 215
Cdd:COG4988   476 GGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRtvILITHRLALLAQADRILVL 544
LolD_lipo_ex TIGR02211
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ...
29-215 1.76e-12

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: 66.99  E-value: 1.76e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  29 LSVSLEPS-LCGLVGRNGVGKTRLLRLLAGLDSPAGGHIERAAAVAWVAQqptltpETTLATL----LGYasVFaalsrl 103
Cdd:TIGR02211  24 VSLSIGKGeIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLS------SNERAKLrnkkLGF--IY------ 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 104 eQGQGLADDFD--------LLDGHWDLTDRLSLAF---READLPPFSADRPAfSLSGGERMKALLCGAFVSGADYLLLDE 172
Cdd:TIGR02211  90 -QFHHLLPDFTalenvampLLIGKKSVKEAKERAYemlEKVGLEHRINHRPS-ELSGGERQRVAIARALVNQPSLVLADE 167
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1512845752 173 PTNHLDRQGREWLYH---QLESWQGGA-LIASHDRELLTRMPRIIEL 215
Cdd:TIGR02211 168 PTGNLDNNNAKIIFDlmlELNRELNTSfLVVTHDLELAKKLDRVLEM 214
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
11-201 1.87e-12

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: 66.47  E-value: 1.87e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  11 VLHQVTCQFATGQtlfgplsvslepsLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIERAAAVAWVAQQPTltpeTTLATL 90
Cdd:cd03268    15 VLDDISLHVKKGE-------------IYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAL----RRIGAL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  91 LGYASVFAALSRLEQGQGLADDFDLLDGHWD-LTDRLSLAFReadlppfsADRPAFSLSGGerMKALLC--GAFVSGADY 167
Cdd:cd03268    78 IEAPGFYPNLTARENLRLLARLLGIRKKRIDeVLDVVGLKDS--------AKKKVKGFSLG--MKQRLGiaLALLGNPDL 147
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1512845752 168 LLLDEPTNHLDRQGREWLYHQLESWQ---GGALIASH 201
Cdd:cd03268   148 LILDEPTNGLDPDGIKELRELILSLRdqgITVLISSH 184
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
5-215 4.11e-12

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: 68.47  E-value: 4.11e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752   5 AHIPAFVLHQVTCQFATGQTLFGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPAGGHI-------------ERAA 70
Cdd:TIGR02857 317 APASSLEFSGVSVAYPGRRPALRPVSFTVPPgERVALVGPSGAGKSTLLNLLLGFVDPTEGSIavngvpladadadSWRD 396
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  71 AVAWVAQQPTLTPETTLATLlgyasvfaALSRLEqgqglADDfdlldghwdltDRLSLAFREADLPPFSADRPAF----- 145
Cdd:TIGR02857 397 QIAWVPQHPFLFAGTIAENI--------RLARPD-----ASD-----------AEIREALERAGLDEFVAALPQGldtpi 452
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1512845752 146 -----SLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGREWLYHQLESWQGGA--LIASHDRELLTRMPRIIEL 215
Cdd:TIGR02857 453 geggaGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRtvLLVTHRLALAALADRIVVL 529
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
34-208 9.68e-12

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 66.79  E-value: 9.68e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  34 EPSLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIeraaavawvaqqptltpetTLATLLGYASVFAALSRL----EQGQGL 109
Cdd:PRK09536   28 EGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTV-------------------LVAGDDVEALSARAASRRvasvPQDTSL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 110 ADDFDLLD-------------GHWDLTDRLSL--AFREADLPPFsADRPAFSLSGGERMKALLCGAFVSGADYLLLDEPT 174
Cdd:PRK09536   89 SFEFDVRQvvemgrtphrsrfDTWTETDRAAVerAMERTGVAQF-ADRPVTSLSGGERQRVLLARALAQATPVLLLDEPT 167
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1512845752 175 NHLDrqgrewLYHQ---LESWQ-----GGALIAS-HDRELLTR 208
Cdd:PRK09536  168 ASLD------INHQvrtLELVRrlvddGKTAVAAiHDLDLAAR 204
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
22-204 1.16e-11

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: 64.08  E-value: 1.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  22 GQTLFGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIERAAAVAWVAQQ-----------PTLTPETTLAT 89
Cdd:cd03259    12 SVRALDDLSLTVEPgEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPerrnigmvfqdYALFPHLTVAE 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  90 LLGYASVFAALSRLEQgqgladdfdlldghwdlTDRLSLAFREADLPPFsADRPAFSLSGGERMKALLCGAFVSGADYLL 169
Cdd:cd03259    92 NIAFGLKLRGVPKAEI-----------------RARVRELLELVGLEGL-LNRYPHELSGGQQQRVALARALAREPSLLL 153
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1512845752 170 LDEPTNHLDRQGREWLYHQLESWQGG----ALIASHDRE 204
Cdd:cd03259   154 LDEPLSALDAKLREELREELKELQRElgitTIYVTHDQE 192
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
29-224 2.30e-11

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: 63.47  E-value: 2.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  29 LSVSLEPSLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIERAAAVAWVAQQPTLTP--ETTLATLLGYASVFAALS---RL 103
Cdd:cd03297    17 IDFDLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPpqQRKIGLVFQQYALFPHLNvreNL 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 104 EQGQGLADDFDLLDGHWDLTDRLSLAFREadlppfsaDRPAFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGRE 183
Cdd:cd03297    97 AFGLKRKRNREDRISVDELLDLLGLDHLL--------NRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRL 168
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1512845752 184 WLYHQLES----WQGGALIASHDRELLTRM-PRIIELTPTALRSYG 224
Cdd:cd03297   169 QLLPELKQikknLNIPVIFVTHDLSEAEYLaDRIVVMEDGRLQYIG 214
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
40-261 4.52e-11

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 65.36  E-value: 4.52e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  40 LVGRNGVGKTRLLRLLAGLDSPAGGHIE-------------RAAavawvaqqptLTPETTLATLLGyasvfaalsrleqg 106
Cdd:PRK11147  350 LIGPNGCGKTTLLKLMLGQLQADSGRIHcgtklevayfdqhRAE----------LDPEKTVMDNLA-------------- 405
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 107 qgladdfdllDGHWDLT----DRLSLAFREADL-PPFSADRPAFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQG 181
Cdd:PRK11147  406 ----------EGKQEVMvngrPRHVLGYLQDFLfHPKRAMTPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVET 475
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 182 REWLYHQLESWQGGALIASHDRELltrmpriIELTPT---------ALRSYGGNYDEYQRQR---MAEQQAARAALEHAV 249
Cdd:PRK11147  476 LELLEELLDSYQGTVLLVSHDRQF-------VDNTVTecwifegngKIGRYVGGYHDARQQQaqyLALKQPAVKKKEEAA 548
                         250
                  ....*....|..
gi 1512845752 250 TDRRRTRARMQK 261
Cdd:PRK11147  549 APKAETVKRSSK 560
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
22-216 8.07e-11

Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.


Pssm-ID: 213198 [Multi-domain]  Cd Length: 201  Bit Score: 61.74  E-value: 8.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  22 GQTLFGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIeRAAAVAWVAQQPTLTPEttLATLLGYASVFAAL 100
Cdd:cd03231    12 GRALFSGLSFTLAAgEALQVTGPNGSGKTTLLRILAGLSPPLAGRV-LLNGGPLDFQRDSIARG--LLYLGHAPGIKTTL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 101 SRLEQGQGLADDFDlLDGHWDLTDRLSLAFREadlppfsaDRPAFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQ 180
Cdd:cd03231    89 SVLENLRFWHADHS-DEQVEEALARVGLNGFE--------DRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKA 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1512845752 181 GREWLYHQLESW--QGGALIAS--HDRELLTRMPRIIELT 216
Cdd:cd03231   160 GVARFAEAMAGHcaRGGMVVLTthQDLGLSEAGARELDLG 199
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
36-275 1.66e-10

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 63.65  E-value: 1.66e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  36 SLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIERAAAVAWVAQQptltpETTLATLLGYASVFAALSRL---EQGQGLADd 112
Cdd:PRK10636  339 SRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFA-----QHQLEFLRADESPLQHLARLapqELEQKLRD- 412
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 113 fdLLDGHWDLTDRLSlafreadlppfsadRPAFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGREWLYHQLESW 192
Cdd:PRK10636  413 --YLGGFGFQGDKVT--------------EETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDF 476
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 193 QGGALIASHDRELLTRMPRIIELTPTA-LRSYGGNYDEYQrQRMAEQQAARAALEHAVTDRRRTRARM---QKEHDAAQR 268
Cdd:PRK10636  477 EGALVVVSHDRHLLRSTTDDLYLVHDGkVEPFDGDLEDYQ-QWLSDVQKQENQTDEAPKENNANSAQArkdQKRREAELR 555

                  ....*..
gi 1512845752 269 RSAQTLR 275
Cdd:PRK10636  556 TQTQPLR 562
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
457-519 1.80e-10

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: 59.57  E-value: 1.80e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1512845752 457 LSGGERLKAALACVLWRRepAQLLLLDEPTNHLDLASTQAIESALAAFPG---AMLVVSHDEAFLQ 519
Cdd:cd00267    81 LSGGQRQRVALARALLLN--PDLLLLDEPTSGLDPASRERLLELLRELAEegrTVIIVTHDPELAE 144
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
29-215 2.05e-10

ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.


Pssm-ID: 213213 [Multi-domain]  Cd Length: 173  Bit Score: 59.54  E-value: 2.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  29 LSVSLEPS-LCGLVGRNGVGKTRLLRLLAGLDSPAGGHIeraaavawvaqqptltpettlatLLGYASVFA-ALSRLEQG 106
Cdd:cd03246    21 VSFSIEPGeSLAIIGPSGSGKSTLARLILGLLRPTSGRV-----------------------RLDGADISQwDPNELGDH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 107 QG-LADDFDLLDGhwDLTDRLslafreadlppfsadrpafsLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGREWL 185
Cdd:cd03246    78 VGyLPQDDELFSG--SIAENI--------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERAL 135
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1512845752 186 YHQLESWQGG---ALIASHDRELLTRMPRIIEL 215
Cdd:cd03246   136 NQAIAALKAAgatRIVIAHRPETLASADRILVL 168
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
22-219 2.29e-10

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 60.27  E-value: 2.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  22 GQTLFGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIEraaavaWVAQQPTLTPETTLATLLGYASVF-AA 99
Cdd:PRK13539   14 GRVLFSGLSFTLAAgEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIK------LDGGDIDDPDVAEACHYLGHRNAMkPA 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 100 LSRLEQGQGLAddfDLLDGHwDLTDRLSLAFreADLPPFsADRPAFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDR 179
Cdd:PRK13539   88 LTVAENLEFWA---AFLGGE-ELDIAAALEA--VGLAPL-AHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1512845752 180 QGREWL-----YHqLEswQGGALIASHDRELLTRMPRIIELTPTA 219
Cdd:PRK13539  161 AAVALFaelirAH-LA--QGGIVIAATHIPLGLPGARELDLGPFA 202
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
39-200 2.40e-10

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: 60.46  E-value: 2.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  39 GLVGRNGVGKTRLLRLLAGLDSPAGGHIEraAAVAWVAQQPtLTPETTLATLLGYASVFAALSRLEQGQGLADdFDLLDG 118
Cdd:cd03266    35 GLLGPNGAGKTTTLRMLAGLLEPDAGFAT--VDGFDVVKEP-AEARRRLGFVSDSTGLYDRLTARENLEYFAG-LYGLKG 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 119 HwDLTDRLSLAFREADLPPFsADRPAFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLD----RQGREWLYHQLEswQG 194
Cdd:cd03266   111 D-ELTARLEELADRLGMEEL-LDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDvmatRALREFIRQLRA--LG 186

                  ....*.
gi 1512845752 195 GALIAS 200
Cdd:cd03266   187 KCILFS 192
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
370-519 2.74e-10

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: 59.96  E-value: 2.74e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 370 IALKGPNGCGKTTLLKTLLGLEQAASGDVRLSV----------SAAYLDQHLT-QLdLSLSVMAHL--SLEDTPLDEGLL 436
Cdd:cd03226    29 IALTGKNGAGKTTLAKILAGLIKESSGSILLNGkpikakerrkSIGYVMQDVDyQL-FTDSVREELllGLKELDAGNEQA 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 437 RTRLAQLQLGADKVTLPLSaLSGGERLKAALACVLWRREPaqLLLLDEPTNHLDLASTQAIESA---LAAFPGAMLVVSH 513
Cdd:cd03226   108 ETVLKDLDLYALKERHPLS-LSGGQKQRLAIAAALLSGKD--LLIFDEPTSGLDYKNMERVGELireLAAQGKAVIVITH 184

                  ....*.
gi 1512845752 514 DEAFLQ 519
Cdd:cd03226   185 DYEFLA 190
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
29-202 3.58e-10

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: 59.83  E-value: 3.58e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  29 LSVSLEPSLC-GLVGRNGVGKTRLLRLLAGLDSPAGGHIeraaavawvaqqptltpettlaTLLGYaSVFAALSRLEQGQ 107
Cdd:cd03263    21 LSLNVYKGEIfGLLGHNGAGKTTTLKMLTGELRPTSGTA----------------------YINGY-SIRTDRKAARQSL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 108 GLADDFDLLDghWDLTDRLSLAF--------------------READLPPFsADRPAFSLSGGERMKALLCGAFVSGADY 167
Cdd:cd03263    78 GYCPQFDALF--DELTVREHLRFyarlkglpkseikeevelllRVLGLTDK-ANKRARTLSGGMKRKLSLAIALIGGPSV 154
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1512845752 168 LLLDEPTNHLDRQGREWLYHQLESWQGGA--LIASHD 202
Cdd:cd03263   155 LLLDEPTSGLDPASRRAIWDLILEVRKGRsiILTTHS 191
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
8-215 4.44e-10

ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213195 [Multi-domain]  Cd Length: 171  Bit Score: 58.55  E-value: 4.44e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752   8 PAFVLHQVTCQFATGQTLfgplsvslepslcGLVGRNGVGKTRLLRLLAGLDSPAGGHIeraaavawvaqqptltpettl 87
Cdd:cd03228    14 PKPVLKDVSLTIKPGEKV-------------AIVGPSGSGKSTLLKLLLRLYDPTSGEI--------------------- 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  88 atLLGyasvfaalsrleqGQGLADdfdlLDGHWdLTDRLSLAFREADLppfsadrpaFS-------LSGGERMKALLCGA 160
Cdd:cd03228    60 --LID-------------GVDLRD----LDLES-LRKNIAYVPQDPFL---------FSgtireniLSGGQRQRIAIARA 110
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1512845752 161 FVSGADYLLLDEPTNHLDRQGREWLYHQLESWQGG--ALIASHDRELLTRMPRIIEL 215
Cdd:cd03228   111 LLRDPPILILDEATSALDPETEALILEALRALAKGktVIVIAHRLSTIRDADRIIVL 167
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
25-217 4.92e-10

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 59.43  E-value: 4.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  25 LFGPLSVSLEPS-LCGLVGRNGVGKTRLLRLLAGLDSPAGGHIERAAAVAWVAqqptltPETTLATLL--GYAS-VFAAL 100
Cdd:PRK13538   16 LFSGLSFTLNAGeLVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQ------RDEYHQDLLylGHQPgIKTEL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 101 SRLE------QGQGLADDFDLldghWDLTDRLSLAFREadlppfsaDRPAFSLSGGERMKALLCGAFVSGADYLLLDEPT 174
Cdd:PRK13538   90 TALEnlrfyqRLHGPGDDEAL----WEALAQVGLAGFE--------DVPVRQLSAGQQRRVALARLWLTRAPLWILDEPF 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1512845752 175 NHLDRQGREWLYHQLESW--QGG-ALIASH-DRELLTRMPRIIELTP 217
Cdd:PRK13538  158 TAIDKQGVARLEALLAQHaeQGGmVILTTHqDLPVASDKVRKLRLGQ 204
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
8-215 5.12e-10

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: 62.09  E-value: 5.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752   8 PAFVLHQVTCQF-ATGQTLFGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIEraaavaWVAQQPTLTPET 85
Cdd:COG4987   332 PSLELEDVSFRYpGAGRPVLDGLSLTLPPgERVAIVGPSGSGKSTLLALLLRFLDPQSGSIT------LGGVDLRDLDED 405
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  86 TLATLLGYAS----VFAA-------LSRLEqgqglADDFDLLDghwdltdrlslAFREADLPPFSADRP----------A 144
Cdd:COG4987   406 DLRRRIAVVPqrphLFDTtlrenlrLARPD-----ATDEELWA-----------ALERVGLGDWLAALPdgldtwlgegG 469
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1512845752 145 FSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGREWLYHQLESWQGGA--LIASHDRELLTRMPRIIEL 215
Cdd:COG4987   470 RRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRtvLLITHRLAGLERMDRILVL 542
F420-0_ABC_ATP TIGR03873
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ...
36-205 8.09e-10

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: 59.44  E-value: 8.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  36 SLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIE------RAAAVAWVAQQPTLTPETTLATLLGYASVFAALSRLEQGQGL 109
Cdd:TIGR03873  28 SLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDlagvdlHGLSRRARARRVALVEQDSDTAVPLTVRDVVALGRIPHRSLW 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 110 ADDFDLLDGhwdLTDRLSLAFREADLppfsADRPAFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLD---RQGREWLY 186
Cdd:TIGR03873 108 AGDSPHDAA---VVDRALARTELSHL----ADRDMSTLSGGERQRVHVARALAQEPKLLLLDEPTNHLDvraQLETLALV 180
                         170
                  ....*....|....*....
gi 1512845752 187 HQLESWQGGALIASHDREL 205
Cdd:TIGR03873 181 RELAATGVTVVAALHDLNL 199
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
453-518 2.11e-09

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: 57.48  E-value: 2.11e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1512845752 453 PLSALSGGERLKAALACVLWRRepAQLLLLDEPTNHLDLASTQAIESALAAFPGA---MLVVSHDEAFL 518
Cdd:cd03225   131 SPFTLSGGQKQRVAIAGVLAMD--PDILLLDEPTAGLDPAGRRELLELLKKLKAEgktIIIVTHDLDLL 197
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
23-207 2.25e-09

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 58.66  E-value: 2.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  23 QTLFGPLSVSLEPSLC-GLVGRNGVGKTRLLRLLAGLDSPAGGHIeraaavawvaqqptltpettlaTLLGyASVFAALS 101
Cdd:PRK13537   20 KLVVDGLSFHVQRGECfGLLGPNGAGKTTTLRMLLGLTHPDAGSI----------------------SLCG-EPVPSRAR 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 102 RLEQGQGLADDFDLLDGhwDLTDR-----------LSLAFREADLPPF--------SADRPAFSLSGGERMKALLCGAFV 162
Cdd:PRK13537   77 HARQRVGVVPQFDNLDP--DFTVRenllvfgryfgLSAAAARALVPPLlefaklenKADAKVGELSGGMKRRLTLARALV 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1512845752 163 SGADYLLLDEPTNHLDRQGREWLYHQLESwqggaLIASHDRELLT 207
Cdd:PRK13537  155 NDPDVLVLDEPTTGLDPQARHLMWERLRS-----LLARGKTILLT 194
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
24-256 2.32e-09

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 59.75  E-value: 2.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  24 TLFGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIE-------------RAaavawvaqqpTLTPETTlat 89
Cdd:PRK11819  338 LLIDDLSFSLPPgGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKigetvklayvdqsRD----------ALDPNKT--- 404
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  90 llgyasVFAALSrleqgqglaDDFDLLD-GHWDLTDRLSLA---FREADlppfsADRPAFSLSGGERMKALLCGAFVSGA 165
Cdd:PRK11819  405 ------VWEEIS---------GGLDIIKvGNREIPSRAYVGrfnFKGGD-----QQKKVGVLSGGERNRLHLAKTLKQGG 464
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 166 DYLLLDEPTNHLDRQGREWLYHQLESWQGGALIASHDRELLTRMPRIIeltpTALRS------YGGNYDEYQ---RQRMA 236
Cdd:PRK11819  465 NVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRIATHI----LAFEGdsqvewFEGNFQEYEedkKRRLG 540
                         250       260
                  ....*....|....*....|
gi 1512845752 237 EQqaarAALEHAVTDRRRTR 256
Cdd:PRK11819  541 AD----AARPHRIKYKKLTR 556
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
8-218 2.75e-09

ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 59.44  E-value: 2.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752   8 PAFVLHQVTCQFATGQTLFGPLSVSLEPslcG----LVGRNGVGKTRLLRLLAGLDSPAGGHIERaaavawvaqqPTLT- 82
Cdd:COG4178   361 GALALEDLTLRTPDGRPLLEDLSLSLKP---GerllITGPSGSGKSTLLRAIAGLWPYGSGRIAR----------PAGAr 427
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  83 ----------PETTLATLLGYAsvfaalsrleqgqGLADDFDlldghwdlTDRLSLAFREADLPPFsADRPAFS------ 146
Cdd:COG4178   428 vlflpqrpylPLGTLREALLYP-------------ATAEAFS--------DAELREALEAVGLGHL-AERLDEEadwdqv 485
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1512845752 147 LSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGREWLYHQL-ESWQGGALIA-SHDRELLTRMPRIIELTPT 218
Cdd:COG4178   486 LSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLrEELPGTTVISvGHRSTLAAFHDRVLELTGD 559
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
369-519 2.82e-09

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 59.58  E-value: 2.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 369 RIALKGPNGCGKT-------------------TLLKTLLGLEQ----AASGDVRLSVS------AAYLDQ-----HLTQL 414
Cdd:PRK11147   31 RVCLVGRNGAGKStlmkilngevllddgriiyEQDLIVARLQQdpprNVEGTVYDFVAegieeqAEYLKRyhdisHLVET 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 415 DLS---LSVMAHLSLEDTPLDEGLLRTR----LAQLQLGADKvtlPLSALSGGERLKAALACVLwRREPaQLLLLDEPTN 487
Cdd:PRK11147  111 DPSeknLNELAKLQEQLDHHNLWQLENRinevLAQLGLDPDA---ALSSLSGGWLRKAALGRAL-VSNP-DVLLLDEPTN 185
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1512845752 488 HLDLASTQAIESALAAFPGAMLVVSHDEAFLQ 519
Cdd:PRK11147  186 HLDIETIEWLEGFLKTFQGSIIFISHDRSFIR 217
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
12-202 3.00e-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: 57.10  E-value: 3.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  12 LHQVTCQFATGQ---TLFGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIERAAAVAWVAQqptltPETTL 87
Cdd:cd03293     3 VRNVSKTYGGGGgavTALEDISLSVEEgEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG-----PDRGY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  88 ----ATLLGYASVF--AALSrLEQgQGLADDfdlldghwDLTDRLSLAFREADLPPFSADRPAfSLSGGERMKALLCGAF 161
Cdd:cd03293    78 vfqqDALLPWLTVLdnVALG-LEL-QGVPKA--------EARERAEELLELVGLSGFENAYPH-QLSGGMRQRVALARAL 146
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1512845752 162 VSGADYLLLDEPTNHLDRQGR----EWLYHQLESWQGGALIASHD 202
Cdd:cd03293   147 AVDPDVLLLDEPFSALDALTReqlqEELLDIWRETGKTVLLVTHD 191
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
39-209 3.72e-09

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: 56.04  E-value: 3.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  39 GLVGRNGVGKTRLLRLLAGLDSPAGGHIERAaavawvaqqptltpettlatllgyasvfaalsrleqGQGLADDFDLLDg 118
Cdd:cd03229    30 ALLGPSGSGKSTLLRCIAGLEEPDSGSILID------------------------------------GEDLTDLEDELP- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 119 hwDLTDRLSLAFREADLPP-FSA-DRPAFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGREWLYHQLESWQGGA 196
Cdd:cd03229    73 --PLRRRIGMVFQDFALFPhLTVlENIALGLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQL 150
                         170
                  ....*....|....*..
gi 1512845752 197 ----LIASHDRELLTRM 209
Cdd:cd03229   151 gitvVLVTHDLDEAARL 167
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
14-215 5.90e-09

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: 56.26  E-value: 5.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  14 QVTCQFATGQTLFGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIEraaavawvaqqptlTPETTLATLLG 92
Cdd:cd03292     5 NVTKTYPNGTAALDGINISISAgEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIR--------------VNGQDVSDLRG 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  93 yasvfAALSRLEQGQGLA-DDFDLL-----------------DGHWDLTDRLSLAFREADLPPFSADRPAfSLSGGERMK 154
Cdd:cd03292    71 -----RAIPYLRRKIGVVfQDFRLLpdrnvyenvafalevtgVPPREIRKRVPAALELVGLSHKHRALPA-ELSGGEQQR 144
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1512845752 155 ALLCGAFVSGADYLLLDEPTNHLDRQGREWLYHQLESW-QGGA--LIASHDRELLTRM-PRIIEL 215
Cdd:cd03292   145 VAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKInKAGTtvVVATHAKELVDTTrHRVIAL 209
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
12-178 6.09e-09

ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213231 [Multi-domain]  Cd Length: 211  Bit Score: 56.05  E-value: 6.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  12 LHQVTCQFATGQTLfGPLSVSLEPSLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIERAAAVAWVAQQ------------P 79
Cdd:cd03264     3 LENLTKRYGKKRAL-DGVSLTLGPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQklrrrigylpqeF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  80 TLTPETTLATLLGYAsvfAALSRLEQGQGLADDFDLLDgHWDLTDRlslafreadlppfsADRPAFSLSGGERMKALLCG 159
Cdd:cd03264    82 GVYPNFTVREFLDYI---AWLKGIPSKEVKARVDEVLE-LVNLGDR--------------AKKKIGSLSGGMRRRVGIAQ 143
                         170
                  ....*....|....*....
gi 1512845752 160 AFVSGADYLLLDEPTNHLD 178
Cdd:cd03264   144 ALVGDPSILIVDEPTAGLD 162
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
10-215 6.62e-09

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: 56.34  E-value: 6.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  10 FVLHQVTCQFATGQTLFgplsvslepslcgLVGRNGVGKTRLLRLLAGLDSPAGGHIEraaavaWVAQQPTLTPETTLAT 89
Cdd:cd03255    18 QALKGVSLSIEKGEFVA-------------IVGPSGSGKSTLLNILGGLDRPTSGEVR------VDGTDISKLSEKELAA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  90 L----LGYasVFaalsrleQGQGLADDFDLLD-----------GHWDLTDRLSLAFREADLPPFSADRPAfSLSGGERMK 154
Cdd:cd03255    79 FrrrhIGF--VF-------QSFNLLPDLTALEnvelplllagvPKKERRERAEELLERVGLGDRLNHYPS-ELSGGQQQR 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1512845752 155 ALLCGAFVSGADYLLLDEPTNHLDRQGREW---LYHQLESWQGGALI-ASHDRELLTRMPRIIEL 215
Cdd:cd03255   149 VAIARALANDPKIILADEPTGNLDSETGKEvmeLLRELNKEAGTTIVvVTHDPELAEYADRIIEL 213
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
453-516 1.57e-08

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 54.55  E-value: 1.57e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1512845752 453 PLSALSGGERLKAALACVLWRRepAQLLLLDEPTNHLDLASTQAIESALAAFPG---AMLVVSHDEA 516
Cdd:NF040873  116 QLGELSGGQRQRALLAQGLAQE--ADLLLLDEPTTGLDAESRERIIALLAEEHArgaTVVVVTHDLE 180
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
400-527 1.78e-08

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 55.32  E-value: 1.78e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 400 LSVSAAYLDQH---LTQLD----LSLSVMAHLSLEDtplDEGLLRTRLAQLQLGaDKVTLPLSALSGGERLKAALACVL- 471
Cdd:PRK03695   67 LARHRAYLSQQqtpPFAMPvfqyLTLHQPDKTRTEA---VASALNEVAEALGLD-DKLGRSVNQLSGGEWQRVRLAAVVl 142
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1512845752 472 --WRR-EP-AQLLLLDEPTNHLDLASTQAIESALAAFP---GAMLVVSHDeaflqglkLTHSL 527
Cdd:PRK03695  143 qvWPDiNPaGQLLLLDEPMNSLDVAQQAALDRLLSELCqqgIAVVMSSHD--------LNHTL 197
BtuD COG4138
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ...
358-527 1.87e-08

ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];


Pssm-ID: 443313 [Multi-domain]  Cd Length: 248  Bit Score: 55.23  E-value: 1.87e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 358 APLNWRIDGPMRIALKGPNGCGkTTLLKTLLGLEQAASGDVRL------SVSAAYLDQH---LTQLDLSLSVMA---HLS 425
Cdd:COG4138    13 GPISAQVNAGELIHLIGPNGAG-KSTLLARMAGLLPGQGEILLngrplsDWSAAELARHrayLSQQQSPPFAMPvfqYLA 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 426 L-----EDTPLDEGLLRTRLAQLQLgADKVTLPLSALSGGERLKAALACVLWRREP-----AQLLLLDEPTNHLDLASTQ 495
Cdd:COG4138    92 LhqpagASSEAVEQLLAQLAEALGL-EDKLSRPLTQLSGGEWQRVRLAAVLLQVWPtinpeGQLLLLDEPMNSLDVAQQA 170
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1512845752 496 AIESALAAFP---GAMLVVSHDeaflqglkLTHSL 527
Cdd:COG4138   171 ALDRLLRELCqqgITVVMSSHD--------LNHTL 197
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
11-182 1.91e-08

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: 56.84  E-value: 1.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  11 VLHQVTCQFATGQTLfgplsvslepslcGLVGRNGVGKTRLLRLLAGLDSPAGGHIERAAAVAWVAQQPTLTPettLATL 90
Cdd:COG1123   280 AVDDVSLTLRRGETL-------------GLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE---LRRR 343
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  91 LG------YASVFAALSRLEQ-GQGLaDDFDLLDGHwDLTDRLSLAFREADLPPFSADRPAFSLSGGERMKALLCGAFVS 163
Cdd:COG1123   344 VQmvfqdpYSSLNPRMTVGDIiAEPL-RLHGLLSRA-ERRERVAELLERVGLPPDLADRYPHELSGGQRQRVAIARALAL 421
                         170
                  ....*....|....*....
gi 1512845752 164 GADYLLLDEPTNHLDRQGR 182
Cdd:COG1123   422 EPKLLILDEPTSALDVSVQ 440
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
39-178 3.05e-08

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: 54.65  E-value: 3.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  39 GLVGRNGVGKTRLLRLLAGLDSPAGGhieraaavawvaqqptltpETTLATLLGYASVFAALSRLE----QGQGLAddfd 114
Cdd:cd03267    51 GFIGPNGAGKTTTLKILSGLLQPTSG-------------------EVRVAGLVPWKRRKKFLRRIGvvfgQKTQLW---- 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 115 lldghWDLTDRLSLAFREA--DLPPFSA-----------------DRPAFSLSGGERMKALLCGAFVSGADYLLLDEPTN 175
Cdd:cd03267   108 -----WDLPVIDSFYLLAAiyDLPPARFkkrldelselldleellDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTI 182

                  ...
gi 1512845752 176 HLD 178
Cdd:cd03267   183 GLD 185
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
8-214 3.16e-08

ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 54.71  E-value: 3.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752   8 PAFVLHQVTCQFATGQ---TLFGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIERAAAVAWVaqqptLTP 83
Cdd:COG1116     6 PALELRGVSKRFPTGGggvTALDDVSLTVAAgEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG-----PGP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  84 ETTL----ATLLGYASVFA--ALSRLEQGQGLADDFDLLDghwDLTDRLSLAFREADLPpfsadrpaFSLSGGERMKALL 157
Cdd:COG1116    81 DRGVvfqePALLPWLTVLDnvALGLELRGVPKAERRERAR---ELLELVGLAGFEDAYP--------HQLSGGMRQRVAI 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1512845752 158 CGAFVSGADYLLLDEPTNHLDRQGREWLYHQLES-WQGG---ALIASHDRE----------LLTRMP-RIIE 214
Cdd:COG1116   150 ARALANDPEVLLMDEPFGALDALTRERLQDELLRlWQETgktVLFVTHDVDeavfladrvvVLSARPgRIVE 221
PLN03073 PLN03073
ABC transporter F family; Provisional
22-207 3.20e-08

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 56.41  E-value: 3.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  22 GQTLFGPLSVSLE-PSLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIERAAAVAWVAQQPTLTPETTLAT--LLGYASVFA 98
Cdd:PLN03073  521 GPLLFKNLNFGIDlDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAVFSQHHVDGLDLSSnpLLYMMRCFP 600
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  99 ALSRLEQGQGLaddfdlldGHWDLTDRLSLafreadlppfsadRPAFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLD 178
Cdd:PLN03073  601 GVPEQKLRAHL--------GSFGVTGNLAL-------------QPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
                         170       180
                  ....*....|....*....|....*....
gi 1512845752 179 RQGREWLYHQLESWQGGALIASHDRELLT 207
Cdd:PLN03073  660 LDAVEALIQGLVLFQGGVLMVSHDEHLIS 688
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
29-206 3.26e-08

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 55.01  E-value: 3.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  29 LSVSLEPsLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIERAAAVAWVAQQPTLTPETTLATLLG-------YASVFAALS 101
Cdd:PRK13638   22 LDFSLSP-VTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLALRQQVATVFQdpeqqifYTDIDSDIA 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 102 RLEQGQGLADDfdlldghwDLTDRLSLAFREADLPPFSaDRPAFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQG 181
Cdd:PRK13638  101 FSLRNLGVPEA--------EITRRVDEALTLVDAQHFR-HQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAG 171
                         170       180
                  ....*....|....*....|....*...
gi 1512845752 182 REWLYHQLE--SWQGG-ALIASHDRELL 206
Cdd:PRK13638  172 RTQMIAIIRriVAQGNhVIISSHDIDLI 199
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
38-191 4.46e-08

molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]


Pssm-ID: 131197 [Multi-domain]  Cd Length: 354  Bit Score: 55.12  E-value: 4.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  38 CGLVGRNGVGKTRLLRLLAGLDSPAGGHIERAAAVAWVAQQPTLTPETTLAtlLGY----ASVFAALSRLEqgqgladdf 113
Cdd:TIGR02142  26 TAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPPEKRR--IGYvfqeARLFPHLSVRG--------- 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 114 DLLDGHWDLTDRLSLAFREA-----DLPPFsADRPAFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGREWLYHQ 188
Cdd:TIGR02142  95 NLRYGMKRARPSERRISFERviellGIGHL-LGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPY 173

                  ...
gi 1512845752 189 LES 191
Cdd:TIGR02142 174 LER 176
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
39-202 5.25e-08

The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.


Pssm-ID: 213204 [Multi-domain]  Cd Length: 246  Bit Score: 53.95  E-value: 5.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  39 GLVGRNGVGKTRLLRLLAGLDSPAGGHIEraaavawvAQQPTLT--PETTLATLLGyaSVFAALSRLEQGQGLADDFDLl 116
Cdd:cd03237    29 GILGPNGIGKTTFIKMLAGVLKPDEGDIE--------IELDTVSykPQYIKADYEG--TVRDLLSSITKDFYTHPYFKT- 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 117 dghwDLTDRLSLafrEADLppfsaDRPAFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGR----EWLYHQLESW 192
Cdd:cd03237    98 ----EIAKPLQI---EQIL-----DREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRlmasKVIRRFAENN 165
                         170
                  ....*....|
gi 1512845752 193 QGGALIASHD 202
Cdd:cd03237   166 EKTAFVVEHD 175
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
453-514 5.59e-08

ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 53.94  E-value: 5.59e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1512845752 453 PLSALSGGERLKAALACVLWRRepAQLLLLDEPTNHLDLASTQAIESALAAFPG---AMLVVSHD 514
Cdd:COG1121   136 PIGELSGGQQQRVLLARALAQD--PDLLLLDEPFAGVDAATEEALYELLRELRRegkTILVVTHD 198
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
10-190 6.02e-08

Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 54.02  E-value: 6.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  10 FVLHQVTCQFAtGQTLFGPLSVSLEPS-LCGLVGRNGVGKTRLLRLLAGLDSPAGGHIeraaavawvaqqptLTPETTLA 88
Cdd:PRK10575   12 FALRNVSFRVP-GRTLLHPLSLTFPAGkVTGLIGHNGSGKSTLLKMLGRHQPPSEGEI--------------LLDAQPLE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  89 TLLGYAsvFA-ALSRLEQGQGLADDFDLLD-------------GHWDLTDRLSL--AFREADLPPFsADRPAFSLSGGER 152
Cdd:PRK10575   77 SWSSKA--FArKVAYLPQQLPAAEGMTVRElvaigrypwhgalGRFGAADREKVeeAISLVGLKPL-AHRLVDSLSGGER 153
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1512845752 153 MKALLCGAFVSGADYLLLDEPTNHLDrqgrewLYHQLE 190
Cdd:PRK10575  154 QRAWIAMLVAQDSRCLLLDEPTSALD------IAHQVD 185
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
8-274 6.09e-08

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: 55.29  E-value: 6.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752   8 PAFVLHQVTCQFATGQT-LFGPLSVSLEPSLC-GLVGRNGVGKTRLLRLLAGLdSPAGGHIEraAAVAWVAQQPTLTPET 85
Cdd:COG1123     3 PLLEVRDLSVRYPGGDVpAVDGVSLTIAPGETvALVGESGSGKSTLALALMGL-LPHGGRIS--GEVLLDGRDLLELSEA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  86 TLATLLGYasVF----AALSRLEQGQGLADDFDLLD-GHWDLTDRLSLAFREADLPPFsADRPAFSLSGGERMKALLCGA 160
Cdd:COG1123    80 LRGRRIGM--VFqdpmTQLNPVTVGDQIAEALENLGlSRAEARARVLELLEAVGLERR-LDRYPHQLSGGQRQRVAIAMA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 161 FVSGADYLLLDEPTNHLDRQGREWLYHQLESWQG----GALIASHDRELLTRMP-RIIELtptalrsyggnydeyQRQRM 235
Cdd:COG1123   157 LALDPDLLIADEPTTALDVTTQAEILDLLRELQRergtTVLLITHDLGVVAEIAdRVVVM---------------DDGRI 221
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1512845752 236 AEQQAARAALEHAVTDRRRTRARMQKEHDAAQRRSAQTL 274
Cdd:COG1123   222 VEDGPPEEILAAPQALAAVPRLGAARGRAAPAAAAAEPL 260
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
41-202 6.16e-08

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 53.91  E-value: 6.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  41 VGRNGVGKTRLLRLLAGLDSPAGGHIeraaavawvaqqptLTPETTLATLLGYASVFAALSRLEQGQGLADDFDL-LDGH 119
Cdd:PRK11247   44 VGRSGCGKSTLLRLLAGLETPSAGEL--------------LAGTAPLAEAREDTRLMFQDARLLPWKKVIDNVGLgLKGQ 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 120 WdlTDRLSLAFREADLPPFSADRPAfSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGREWLYHQLES-WQG---G 195
Cdd:PRK11247  110 W--RDAALQALAAVGLADRANEWPA-ALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESlWQQhgfT 186

                  ....*..
gi 1512845752 196 ALIASHD 202
Cdd:PRK11247  187 VLLVTHD 193
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
39-235 6.47e-08

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: 55.23  E-value: 6.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  39 GLVGRNGVGKTRLLRLLAGLDSPAGGHIE------RaaavawvaqqpTLTPETtLATLLGY----ASVFA-------ALS 101
Cdd:COG2274   505 AIVGRSGSGKSTLLKLLLGLYEPTSGRILidgidlR-----------QIDPAS-LRRQIGVvlqdVFLFSgtireniTLG 572
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 102 RLEqgqglADDFDLLDghwdltdrlslAFREADLPPFSADRP----------AFSLSGGERMKALLCGAFVSGADYLLLD 171
Cdd:COG2274   573 DPD-----ATDEEIIE-----------AARLAGLHDFIEALPmgydtvvgegGSNLSGGQRQRLAIARALLRNPRILILD 636
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1512845752 172 EPTNHLDRQGREWLYHQLESWQGGA--LIASHDRELLTRMPRIIEL---------TPTALRSYGGNYDEYQRQRM 235
Cdd:COG2274   637 EATSALDAETEAIILENLRRLLKGRtvIIIAHRLSTIRLADRIIVLdkgrivedgTHEELLARKGLYAELVQQQL 711
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
39-206 6.84e-08

ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.


Pssm-ID: 213185 [Multi-domain]  Cd Length: 232  Bit Score: 53.32  E-value: 6.84e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  39 GLVGRNGVGKTRLLRLLAGLDSPAGGHIEraaavaWVAQQPTLTPETTLATL-LGY----ASVFAALSRLEQGQGLADDF 113
Cdd:cd03218    30 GLLGPNGAGKTTTFYMIVGLVKPDSGKIL------LDGQDITKLPMHKRARLgIGYlpqeASIFRKLTVEENILAVLEIR 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 114 DLLDGHWdlTDRLSLAFREADLPPfSADRPAFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDR---QGREWLYHQLE 190
Cdd:cd03218   104 GLSKKER--EEKLEELLEEFHITH-LRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPiavQDIQKIIKILK 180
                         170
                  ....*....|....*..
gi 1512845752 191 SWQGGALIASHD-RELL 206
Cdd:cd03218   181 DRGIGVLITDHNvRETL 197
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
8-215 7.68e-08

Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 443338 [Multi-domain]  Cd Length: 233  Bit Score: 53.21  E-value: 7.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752   8 PAFVLHQVTCQFATGQ---TLFGPLSVSLEPS-LCGLVGRNGVGKTRLLRLLAGLDSPAGGHIERAAAVawvaqqptLTP 83
Cdd:COG4181     7 PIIELRGLTKTVGTGAgelTILKGISLEVEAGeSVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQD--------LFA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  84 --ETTLATL----LGYasVF------AALSRLE------QGQGLADDFDLLDghwDLTDRLSLAFREADLPPfsadrpaf 145
Cdd:COG4181    79 ldEDARARLrarhVGF--VFqsfqllPTLTALEnvmlplELAGRRDARARAR---ALLERVGLGHRLDHYPA-------- 145
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1512845752 146 SLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGREW---LYHQLESWQGGALI-ASHDRELLTRMPRIIEL 215
Cdd:COG4181   146 QLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQiidLLFELNRERGTTLVlVTHDPALAARCDRVLRL 219
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
8-189 8.73e-08

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: 54.67  E-value: 8.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752   8 PAFVLHQVTCQFATGQTLFGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIeraaavAWVAQQPTLTPETT 86
Cdd:TIGR02868 333 PTLELRDLSAGYPGAPPVLDGVSLDLPPgERVAILGPSGSGKSTLLATLAGLLDPLQGEV------TLDGVPVSSLDQDE 406
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  87 LATLLGY----ASVFAALSR--LEQGQGLADDFDLLDghwdltdrlslAFREADLPPFSADRP----------AFSLSGG 150
Cdd:TIGR02868 407 VRRRVSVcaqdAHLFDTTVRenLRLARPDATDEELWA-----------ALERVGLADWLRALPdgldtvlgegGARLSGG 475
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1512845752 151 ERMKALLCGAFVSGADYLLLDEPTNHLDRQGREWLYHQL 189
Cdd:TIGR02868 476 ERQRLALARALLADAPILLLDEPTEHLDAETADELLEDL 514
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
374-518 1.48e-07

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 54.04  E-value: 1.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 374 GPNGCGKTTLLKTLLGLEQAASGDVRLSVSAAYLDQHLTQlDLSLSVMAHLSLEDTPLDEGLLRTRLAQ-LQLGA--DKv 450
Cdd:PRK13409  372 GPNGIGKTTFAKLLAGVLKPDEGEVDPELKISYKPQYIKP-DYDGTVEDLLRSITDDLGSSYYKSEIIKpLQLERllDK- 449
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1512845752 451 tlPLSALSGGERLKAALACVLWRrePAQLLLLDEPTNHLD----LASTQAIESALAAFPGAMLVVSHDEAFL 518
Cdd:PRK13409  450 --NVKDLSGGELQRVAIAACLSR--DADLYLLDEPSAHLDveqrLAVAKAIRRIAEEREATALVVDHDIYMI 517
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
29-215 1.62e-07

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 52.51  E-value: 1.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  29 LSVSLEPS-LCGLVGRNGVGKTRLLRLLAGLDSPAGGHIeraaavawvaqqptLTPETTLATLLGYASvfAALSRLEQG- 106
Cdd:PRK11629   28 VSFSIGEGeMMAIVGSSGSGKSTLLHLLGGLDTPTSGDV--------------IFNGQPMSKLSSAAK--AELRNQKLGf 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 107 ----QGLADDFD--------LLDGH---WDLTDRLSLAFREADLPPFSADRPAfSLSGGERMKALLCGAFVSGADYLLLD 171
Cdd:PRK11629   92 iyqfHHLLPDFTalenvampLLIGKkkpAEINSRALEMLAAVGLEHRANHRPS-ELSGGERQRVAIARALVNNPRLVLAD 170
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1512845752 172 EPTNHLDRQGREWLYH---QLESWQGGA-LIASHDRELLTRMPRIIEL 215
Cdd:PRK11629  171 EPTGNLDARNADSIFQllgELNRLQGTAfLVVTHDLQLAKRMSRQLEM 218
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
457-516 1.63e-07

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: 53.83  E-value: 1.63e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1512845752 457 LSGGERLKAALACVLWRrePAQLLLLDEPTNHLDLASTQAIESALAAFPG--AMLVVSHDEA 516
Cdd:TIGR02857 459 LSGGQAQRLALARAFLR--DAPLLLLDEPTAHLDAETEAEVLEALRALAQgrTVLLVTHRLA 518
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
370-514 2.22e-07

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: 52.35  E-value: 2.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 370 IALKGPNGCG----------KTtllktllgleQAASGDVRL---SVSA----------AYLDQHlTQLDLSLSV------ 420
Cdd:COG1120    30 TALLGPNGSGkstllralagLL----------KPSSGEVLLdgrDLASlsrrelarriAYVPQE-PPAPFGLTVrelval 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 421 --MAHLSL--EDTPLDEGLLRTRLAQLQLG--ADKvtlPLSALSGGERLKAALACVLwrrepAQ---LLLLDEPTNHLDL 491
Cdd:COG1120    99 grYPHLGLfgRPSAEDREAVEEALERTGLEhlADR---PVDELSGGERQRVLIARAL-----AQeppLLLLDEPTSHLDL 170
                         170       180
                  ....*....|....*....|....*..
gi 1512845752 492 ASTQAIES---ALAAFPG-AMLVVSHD 514
Cdd:COG1120   171 AHQLEVLEllrRLARERGrTVVMVLHD 197
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
29-214 2.25e-07

retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]


Pssm-ID: 130324 [Multi-domain]  Cd Length: 2272  Bit Score: 53.86  E-value: 2.25e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752   29 LSVSLEPSLC-GLVGRNGVGKTRLLRLLAGLDSPAGGHieraaavawvaqqptltpettlATLLGyASVFAALSRLEQGQ 107
Cdd:TIGR01257 1958 LCVGVRPGECfGLLGVNGAGKTTTFKMLTGDTTVTSGD----------------------ATVAG-KSILTNISDVHQNM 2014
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  108 GLADDFDLLDGHWDLTDRLSLAFREADLPP-----------------FSADRPAFSLSGGERMKALLCGAFVSGADYLLL 170
Cdd:TIGR01257 2015 GYCPQFDAIDDLLTGREHLYLYARLRGVPAeeiekvanwsiqslglsLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLL 2094
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1512845752  171 DEPTNHLDRQGREWLYHQLESW--QGGALI-ASHDRE----LLTRMPRIIE 214
Cdd:TIGR01257 2095 DEPTTGMDPQARRMLWNTIVSIirEGRAVVlTSHSMEeceaLCTRLAIMVK 2145
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
28-178 3.04e-07

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: 51.35  E-value: 3.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  28 PLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIERAAAVAWVAQQ----------------------PTLTPE 84
Cdd:cd03257    23 DVSFSIKKgETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRrlrkirrkeiqmvfqdpmsslnPRMTIG 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  85 TTLATLLgyasvfaalsrLEQGQgladdfdlLDGHWDLTDRLSLAFREADLPPFSADRPAFSLSGGERMKALLCGAFVSG 164
Cdd:cd03257   103 EQIAEPL-----------RIHGK--------LSKKEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARALALN 163
                         170
                  ....*....|....
gi 1512845752 165 ADYLLLDEPTNHLD 178
Cdd:cd03257   164 PKLLIADEPTSALD 177
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
142-219 3.06e-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: 51.07  E-value: 3.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 142 RPAFSLSGGERMKA------LLCGAFVSGADYLLLDEPTNHLDRQGREWLYHQL-ESWQGGA----LIASHDRELLTRMP 210
Cdd:cd03240   111 DMRGRCSGGEKVLAsliirlALAETFGSNCGILALDEPTTNLDEENIEESLAEIiEERKSQKnfqlIVITHDEELVDAAD 190

                  ....*....
gi 1512845752 211 RIIELTPTA 219
Cdd:cd03240   191 HIYRVEKDG 199
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
370-491 3.29e-07

Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 51.55  E-value: 3.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 370 IALKGPNGCGKTTLLKTLLGLEQAASGDV-------------RLSVSAAYLDQ-HLTQLDLS------------LSVMAH 423
Cdd:PRK11231   31 TALIGPNGCGKSTLLKCFARLLTPQSGTVflgdkpismlssrQLARRLALLPQhHLTPEGITvrelvaygrspwLSLWGR 110
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1512845752 424 LSLEDTPL-DEGLLRTRLAQLqlgADKvtlPLSALSGGERLKAALACVLWRREPaqLLLLDEPTNHLDL 491
Cdd:PRK11231  111 LSAEDNARvNQAMEQTRINHL---ADR---RLTDLSGGQRQRAFLAMVLAQDTP--VVLLDEPTTYLDI 171
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
29-191 4.00e-07

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 52.14  E-value: 4.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  29 LSVSLEPSLC-GLVGRNGVGKTRLLRLLAGLDSPAGGHIeraaavawvaqqptltpettlaTLLGyASVFAALSRLEQGQ 107
Cdd:PRK13536   60 LSFTVASGECfGLLGPNGAGKSTIARMILGMTSPDAGKI----------------------TVLG-VPVPARARLARARI 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 108 GLADDFDLLDGHWDLTDRLSLAFR---------EADLPPF--------SADRPAFSLSGGERMKALLCGAFVSGADYLLL 170
Cdd:PRK13536  117 GVVPQFDNLDLEFTVRENLLVFGRyfgmstreiEAVIPSLlefarlesKADARVSDLSGGMKRRLTLARALINDPQLLIL 196
                         170       180
                  ....*....|....*....|.
gi 1512845752 171 DEPTNHLDRQGREWLYHQLES 191
Cdd:PRK13536  197 DEPTTGLDPHARHLIWERLRS 217
F420-0_ABC_ATP TIGR03873
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ...
391-514 6.28e-07

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: 50.97  E-value: 6.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 391 EQAASGDVRLSVSAAYLdqhltqldlsLSVMAHLSL--EDTPLDEGLLRTRLAQLQLgADKVTLPLSALSGGERLKAALA 468
Cdd:TIGR03873  81 EQDSDTAVPLTVRDVVA----------LGRIPHRSLwaGDSPHDAAVVDRALARTEL-SHLADRDMSTLSGGERQRVHVA 149
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1512845752 469 CVLwRREPaQLLLLDEPTNHLDLASTQAIESALA--AFPGAMLVVS-HD 514
Cdd:TIGR03873 150 RAL-AQEP-KLLLLDEPTNHLDVRAQLETLALVRelAATGVTVVAAlHD 196
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
457-519 6.83e-07

ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.


Pssm-ID: 213212 [Multi-domain]  Cd Length: 220  Bit Score: 50.28  E-value: 6.83e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1512845752 457 LSGGERLKAALACVLWRREPaqLLLLDEPTNHLDLASTQAIESALAAFPG--AMLVVSHDEAFLQ 519
Cdd:cd03245   141 LSGGQRQAVALARALLNDPP--ILLLDEPTSAMDMNSEERLKERLRQLLGdkTLIIITHRPSLLD 203
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
11-68 7.88e-07

ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 50.47  E-value: 7.88e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1512845752  11 VLHQVTCQFATGQTLfgplsvslepslcGLVGRNGVGKTRLLRLLAGLDSPAGGHIER 68
Cdd:COG1134    41 ALKDVSFEVERGESV-------------GIIGRNGAGKSTLLKLIAGILEPTSGRVEV 85
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
41-191 1.06e-06

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 51.17  E-value: 1.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  41 VGRNGVGKTRLLRLLAGLDSPAGGHieraaavawvaqqptltpettlatllgYASVFAALSRL--EQGQGLADD------ 112
Cdd:PRK10938   35 VGANGSGKSALARALAGELPLLSGE---------------------------RQSQFSHITRLsfEQLQKLVSDewqrnn 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 113 FDLL----------------DGHWD--LTDRLSLAFREADLppfsADRPAFSLSGGERMKALLCGAFVSGADYLLLDEPT 174
Cdd:PRK10938   88 TDMLspgeddtgrttaeiiqDEVKDpaRCEQLAQQFGITAL----LDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPF 163
                         170
                  ....*....|....*..
gi 1512845752 175 NHLDRQGREWLYHQLES 191
Cdd:PRK10938  164 DGLDVASRQQLAELLAS 180
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
40-213 1.07e-06

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 50.40  E-value: 1.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  40 LVGRNGVGKTRLLRLLAGLDSPAGGHIERAAAvawvaqqpTLTPETTLATLLGYASVFAALSRLEQGQGLADD--FDLLD 117
Cdd:PRK13635   38 IVGHNGSGKSTLAKLLNGLLLPEAGTITVGGM--------VLSEETVWDVRRQVGMVFQNPDNQFVGATVQDDvaFGLEN 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 118 G---HWDLTDRLSLAFREADLPPFSADRPAfSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGREWLY---HQLES 191
Cdd:PRK13635  110 IgvpREEMVERVDQALRQVGMEDFLNREPH-RLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLetvRQLKE 188
                         170       180
                  ....*....|....*....|...
gi 1512845752 192 WQGGALIA-SHDRELLTRMPRII 213
Cdd:PRK13635  189 QKGITVLSiTHDLDEAAQADRVI 211
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
374-518 1.13e-06

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: 51.32  E-value: 1.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 374 GPNGCGKTTLLKTLLGLEQAASGDVRLSVSAAYLDQHLTQlDLSLSVMAHLSLEDTP-LDEGLLRTRLAQ-LQLGA--DK 449
Cdd:COG1245   373 GPNGIGKTTFAKILAGVLKPDEGEVDEDLKISYKPQYISP-DYDGTVEEFLRSANTDdFGSSYYKTEIIKpLGLEKllDK 451
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1512845752 450 vtlPLSALSGGERLKAALACVLWRrePAQLLLLDEPTNHLD----LASTQAIESALAAFPGAMLVVSHDEAFL 518
Cdd:COG1245   452 ---NVKDLSGGELQRVAIAACLSR--DADLYLLDEPSAHLDveqrLAVAKAIRRFAENRGKTAMVVDHDIYLI 519
PRK13541 PRK13541
cytochrome c biogenesis protein CcmA; Provisional
12-201 1.15e-06

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184128 [Multi-domain]  Cd Length: 195  Bit Score: 49.10  E-value: 1.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  12 LHQVtcQFATGQTLFGPLSVSLEPSLCGLV-GRNGVGKTRLLRLLAGLDSPAGGHIERAAAVAWVAQQPTLtpeTTLATL 90
Cdd:PRK13541    4 LHQL--QFNIEQKNLFDLSITFLPSAITYIkGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYC---TYIGHN 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  91 LGYASVFAALSRLEQGQGLADDFDLLDG---HWDLTDRLslafreadlppfsaDRPAFSLSGGERMKALLCGAFVSGADY 167
Cdd:PRK13541   79 LGLKLEMTVFENLKFWSEIYNSAETLYAaihYFKLHDLL--------------DEKCYSLSSGMQKIVAIARLIACQSDL 144
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1512845752 168 LLLDEPTNHLDRQGREWLYH--QLESWQGG-ALIASH 201
Cdd:PRK13541  145 WLLDEVETNLSKENRDLLNNliVMKANSGGiVLLSSH 181
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
39-68 1.37e-06

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: 49.45  E-value: 1.37e-06
                          10        20        30
                  ....*....|....*....|....*....|
gi 1512845752  39 GLVGRNGVGKTRLLRLLAGLDSPAGGHIER 68
Cdd:cd03220    52 GLIGRNGAGKSTLLRLLAGIYPPDSGTVTV 81
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
40-216 1.48e-06

nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]


Pssm-ID: 130252 [Multi-domain]  Cd Length: 230  Bit Score: 49.39  E-value: 1.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  40 LVGRNGVGKTRLLRLLAGLDSPAGGHI------------ERAAAVAWVAQQPTLTPETTLAtlLGYASVFAALSRLEQGQ 107
Cdd:TIGR01184  16 LIGHSGCGKSTLLNLISGLAQPTSGGVilegkqitepgpDRMVVFQNYSLLPWLTVRENIA--LAVDRVLPDLSKSERRA 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 108 gladdfdLLDGHWDLtdrlsLAFREAdlppfsADRPAFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGREWLYH 187
Cdd:TIGR01184  94 -------IVEEHIAL-----VGLTEA------ADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQE 155
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1512845752 188 QL-ESWQGG---ALIASHD-RELLTRMPRIIELT 216
Cdd:TIGR01184 156 ELmQIWEEHrvtVLMVTHDvDEALLLSDRVVMLT 189
PRK13543 PRK13543
heme ABC exporter ATP-binding protein CcmA;
25-201 1.61e-06

heme ABC exporter ATP-binding protein CcmA;


Pssm-ID: 184129 [Multi-domain]  Cd Length: 214  Bit Score: 49.08  E-value: 1.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  25 LFGPLSVSLEPSLCGLV-GRNGVGKTRLLRLLAGLDSPAGGHIEraaavawvaqqptltPETTLATLLGYASVFAALSRL 103
Cdd:PRK13543   26 VFGPLDFHVDAGEALLVqGDNGAGKTTLLRVLAGLLHVESGQIQ---------------IDGKTATRGDRSRFMAYLGHL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 104 EqgqGLADDFDLLDghwDLTDRLSLAFREADLPPFSA----------DRPAFSLSGGERMKALLCGAFVSGADYLLLDEP 173
Cdd:PRK13543   91 P---GLKADLSTLE---NLHFLCGLHGRRAKQMPGSAlaivglagyeDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEP 164
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1512845752 174 TNHLDRQGREWLYHQLESW---QGGALIASH 201
Cdd:PRK13543  165 YANLDLEGITLVNRMISAHlrgGGAALVTTH 195
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
11-190 1.66e-06

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 49.38  E-value: 1.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  11 VLHQVTCQFATGQTLfgplsvslepslcGLVGRNGVGKTRLLRLLAGLDSPAGGHIERAAAVAWVAQQPTLTpeTTLATL 90
Cdd:PRK13548   17 LLDDVSLTLRPGEVV-------------AILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELA--RRRAVL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  91 LGYASV-FA-------ALSRLEQGQGLADDFDLLDghwdltdrlsLAFREADLPPFsADRPAFSLSGGERMKALL----- 157
Cdd:PRK13548   82 PQHSSLsFPftveevvAMGRAPHGLSRAEDDALVA----------AALAQVDLAHL-AGRDYPQLSGGEQQRVQLarvla 150
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1512845752 158 -CGAFVSGADYLLLDEPTNHLDrqgrewLYHQLE 190
Cdd:PRK13548  151 qLWEPDGPPRWLLLDEPTSALD------LAHQHH 178
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
370-514 1.90e-06

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: 48.20  E-value: 1.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 370 IALKGPNGCGKTTLLKTLLGLEQAASGDVRL---SVSA----------AYLDQHLTQLDLslsvmAHLsledtpldegll 436
Cdd:cd03214    28 VGILGPNGAGKSTLLKTLAGLLKPSSGEILLdgkDLASlspkelarkiAYVPQALELLGL-----AHL------------ 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 437 rtrlaqlqlgADKvtlPLSALSGGERLKAALACVLWRRepAQLLLLDEPTNHLDLASTQAIESALAAFPG----AMLVVS 512
Cdd:cd03214    91 ----------ADR---PFNELSGGERQRVLLARALAQE--PPILLLDEPTSHLDIAHQIELLELLRRLARergkTVVMVL 155

                  ..
gi 1512845752 513 HD 514
Cdd:cd03214   156 HD 157
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
11-178 2.76e-06

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: 48.65  E-value: 2.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  11 VLHQVTCQFATGQTLfgplsvslepslcGLVGRNGVGKTRLLRLLAGLDSPAGGHIEraaavAWVAQQPTLTPETTLATL 90
Cdd:cd03261    15 VLKGVDLDVRRGEIL-------------AIIGPSGSGKSTLLRLIVGLLRPDSGEVL-----IDGEDISGLSEAELYRLR 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  91 LGYASVFaalsrleQGQGLADDFDLLD------------GHWDLTDRLSLAFREADLPPFSADRPAfSLSGGERMKALLC 158
Cdd:cd03261    77 RRMGMLF-------QSGALFDSLTVFEnvafplrehtrlSEEEIREIVLEKLEAVGLRGAEDLYPA-ELSGGMKKRVALA 148
                         170       180
                  ....*....|....*....|
gi 1512845752 159 GAFVSGADYLLLDEPTNHLD 178
Cdd:cd03261   149 RALALDPELLLYDEPTAGLD 168
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
457-521 3.46e-06

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: 47.39  E-value: 3.46e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1512845752 457 LSGGERLKAALACVLWRRepAQLLLLDEPTNHLDLASTQAIES---ALAAFPGAMLVVSHDEAFLQGL 521
Cdd:cd03230    96 LSGGMKQRLALAQALLHD--PELLILDEPTSGLDPESRREFWEllrELKKEGKTILLSSHILEEAERL 161
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
29-190 4.01e-06

Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 48.47  E-value: 4.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  29 LSVSLEPS-LCGLVGRNGVGKTRLLRLLAGLDSPAGGHIERAAAVAWVAQQPTL------------TPE-TTLATLLGYA 94
Cdd:PRK11231   21 LSLSLPTGkITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLarrlallpqhhlTPEgITVRELVAYG 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  95 -----SVFAALSRleqgqglaDDFDLLDGHWDLTDRLSLafreadlppfsADRPAFSLSGGERMKALLCGAFVSGADYLL 169
Cdd:PRK11231  101 rspwlSLWGRLSA--------EDNARVNQAMEQTRINHL-----------ADRRLTDLSGGQRQRAFLAMVLAQDTPVVL 161
                         170       180
                  ....*....|....*....|.
gi 1512845752 170 LDEPTNHLDrqgrewLYHQLE 190
Cdd:PRK11231  162 LDEPTTYLD------INHQVE 176
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
23-174 5.53e-06

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: 47.43  E-value: 5.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  23 QTLFGpLSVSLEPSLC-GLVGRNGVGKTRLLRLLAGLDSPAGGHIERaaavaWVAQQPTLTPETTLATLLGYA----SVF 97
Cdd:cd03224    14 QILFG-VSLTVPEGEIvALLGRNGAGKTTLLKTIMGLLPPRSGSIRF-----DGRDITGLPPHERARAGIGYVpegrRIF 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  98 AALSRLE------QGQGLADDFDLLDGHWDLTDRLSlAFReadlppfsaDRPAFSLSGGER-MKAlLCGAFVSGADYLLL 170
Cdd:cd03224    88 PELTVEEnlllgaYARRRAKRKARLERVYELFPRLK-ERR---------KQLAGTLSGGEQqMLA-IARALMSRPKLLLL 156

                  ....
gi 1512845752 171 DEPT 174
Cdd:cd03224   157 DEPS 160
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
457-513 5.83e-06

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: 46.83  E-value: 5.83e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 457 LSGGERLKAALACVLWRRePAqLLLLDEPTNHLDLASTQAIESALAAFPGAM---LVVSH 513
Cdd:cd03246    97 LSGGQRQRLGLARALYGN-PR-ILVLDEPNSHLDVEGERALNQAIAALKAAGatrIVIAH 154
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
370-522 6.24e-06

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: 47.09  E-value: 6.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 370 IALKGPNGCG----------KTtllktllgleQAASGDVRL------SVSAAYLDQ-----HLTQLDLSLSVMAHL---- 424
Cdd:COG4133    31 LALTGPNGSGkttllrilagLL----------PPSAGEVLWngepirDAREDYRRRlaylgHADGLKPELTVRENLrfwa 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 425 SLEDTPLDEGLLRTRLAQLQLG--ADkvtLPLSALSGGERLKAALACVLWRrePAQLLLLDEPTNHLDLASTQAIESALA 502
Cdd:COG4133   101 ALYGLRADREAIDEALEAVGLAglAD---LPVRQLSAGQKRRVALARLLLS--PAPLWLLDEPFTALDAAGVALLAELIA 175
                         170       180
                  ....*....|....*....|...
gi 1512845752 503 AFP---GAMLVVSHDEAFLQGLK 522
Cdd:COG4133   176 AHLargGAVLLTTHQPLELAAAR 198
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
455-518 7.51e-06

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: 48.60  E-value: 7.51e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1512845752 455 SALSGGERLKAALACVLWRrePAQLLLLDEPTNHLDLASTQAIESALAAFPG--AMLVVSHDEAFL 518
Cdd:COG4988   472 RGLSGGQAQRLALARALLR--DAPLLLLDEPTAHLDAETEAEILQALRRLAKgrTVILITHRLALL 535
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
448-521 8.49e-06

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: 46.41  E-value: 8.49e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1512845752 448 DKVTLPLSalsGGERLKAALACVLwRREPaQLLLLDEPTNHLDLASTQAIESAL----AAFPGAMLVVSHDEAFLQGL 521
Cdd:cd03229    95 ENIALGLS---GGQQQRVALARAL-AMDP-DVLLLDEPTSALDPITRREVRALLkslqAQLGITVVLVTHDLDEAARL 167
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
10-219 9.46e-06

Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];


Pssm-ID: 443809 [Multi-domain]  Cd Length: 229  Bit Score: 47.04  E-value: 9.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  10 FVLHQVTcqfatGQTL--FGPLSVSLEPSLC-GLVGRNGVGKTRLLRLLAGLDSPAGGHIeRAAAVAWVAQQPTLTPETT 86
Cdd:COG4778    14 FTLHLQG-----GKRLpvLDGVSFSVAAGECvALTGPSGAGKSTLLKCIYGNYLPDSGSI-LVRHDGGWVDLAQASPREI 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  87 LA---TLLGYASVF-------AAL-----SRLEQGQGLADDFD----LLDghwdltdRLSLAFREADLPP--FSadrpaf 145
Cdd:COG4778    88 LAlrrRTIGYVSQFlrviprvSALdvvaePLLERGVDREEARArareLLA-------RLNLPERLWDLPPatFS------ 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1512845752 146 slsGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGREW---LYHQLESwQGGALIA-SHDRELLTRMP-RIIELTPTA 219
Cdd:COG4778   155 ---GGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVvveLIEEAKA-RGTAIIGiFHDEEVREAVAdRVVDVTPFS 229
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
458-521 1.08e-05

Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];


Pssm-ID: 443809 [Multi-domain]  Cd Length: 229  Bit Score: 46.66  E-value: 1.08e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1512845752 458 SGGERLKAALACVLWRREPaqLLLLDEPTNHLDLASTQA----IESALAAfpG-AMLVVSHDEAFLQGL 521
Cdd:COG4778   154 SGGEQQRVNIARGFIADPP--LLLLDEPTASLDAANRAVvvelIEEAKAR--GtAIIGIFHDEEVREAV 218
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
12-178 1.11e-05

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: 46.50  E-value: 1.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  12 LHQVTCQFATGQTLFGpLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIERAAAVAWVAQQPT---------L 81
Cdd:cd03269     3 VENVTKRFGRVTALDD-ISFSVEKgEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRigylpeergL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  82 TPETTLATLLGYasvFAALSRLEQGQGLADDFDLLDgHWDLTDRlslafreadlppfsADRPAFSLSGGERMKALLCGAF 161
Cdd:cd03269    82 YPKMKVIDQLVY---LAQLKGLKKEEARRRIDEWLE-RLELSEY--------------ANKRVEELSKGNQQKVQFIAAV 143
                         170
                  ....*....|....*..
gi 1512845752 162 VSGADYLLLDEPTNHLD 178
Cdd:cd03269   144 IHDPELLILDEPFSGLD 160
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
455-519 1.17e-05

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: 48.29  E-value: 1.17e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1512845752 455 SALSGGERLKAALACVLWRRepAQLLLLDEPTNHLDLASTQAIESALAAFPG--AMLVVSHDEAFLQ 519
Cdd:COG2274   610 SNLSGGQRQRLAIARALLRN--PRILILDEATSALDAETEAIILENLRRLLKgrTVIIIAHRLSTIR 674
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
39-173 1.20e-05

ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440752 [Multi-domain]  Cd Length: 240  Bit Score: 46.95  E-value: 1.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  39 GLVGRNGVGKTRLLRLLAGLDSPAGGHIeraaavawvaqqpTLTPE--TTL-----ATL-LGY----ASVFAALS----- 101
Cdd:COG1137    33 GLLGPNGAGKTTTFYMIVGLVKPDSGRI-------------FLDGEdiTHLpmhkrARLgIGYlpqeASIFRKLTvedni 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 102 ----------------RLEQgqgLADDFDLldghwdltDRLslafreadlppfsADRPAFSLSGGERMKALLCGAFVSGA 165
Cdd:COG1137   100 lavlelrklskkereeRLEE---LLEEFGI--------THL-------------RKSKAYSLSGGERRRVEIARALATNP 155

                  ....*...
gi 1512845752 166 DYLLLDEP 173
Cdd:COG1137   156 KFILLDEP 163
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
12-206 1.34e-05

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 46.65  E-value: 1.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  12 LHQVTCQFATGQTLfGPLSVSLEPS-LCGLVGRNGVGKTRLLRLLAGLDSPAGGHIERAAAVAWVAQQPTLTPETTLATL 90
Cdd:PRK09544    7 LENVSVSFGQRRVL-SDVSLELKPGkILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYLDTTLPLT 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  91 LGY----------ASVFAALSRLEQGQGLaddfdlldghwdltdrlslafreadlppfsaDRPAFSLSGGERMKALLCGA 160
Cdd:PRK09544   86 VNRflrlrpgtkkEDILPALKRVQAGHLI-------------------------------DAPMQKLSGGETQRVLLARA 134
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1512845752 161 FVSGADYLLLDEPTNHLDRQGREWLY---HQLESWQG-GALIASHDRELL 206
Cdd:PRK09544  135 LLNRPQLLVLDEPTQGVDVNGQVALYdliDQLRRELDcAVLMVSHDLHLV 184
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
8-66 1.47e-05

ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 47.40  E-value: 1.47e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752   8 PAFVLHQVTCQFAtGQTLFGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPAGGHI 66
Cdd:COG3842     4 PALELENVSKRYG-DVTALDDVSLSIEPgEFVALLGPSGCGKTTLLRMIAGFETPDSGRI 62
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
369-487 1.64e-05

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: 44.95  E-value: 1.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 369 RIALKGPNGCGKTTLLKTLLGLEQAASGDVRLSVSA-------------AYLDQHlTQLDLSLSV-------MAHLSLED 428
Cdd:pfam00005  13 ILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDltdderkslrkeiGYVFQD-PQLFPRLTVrenlrlgLLLKGLSK 91
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1512845752 429 TPLDEGL--LRTRLAQLQLGADKVTLPLSALSGGERLKAALACVLWRRepAQLLLLDEPTN 487
Cdd:pfam00005  92 REKDARAeeALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTK--PKLLLLDEPTA 150
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
410-492 1.75e-05

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: 45.95  E-value: 1.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 410 HLT---QLDLSLSVMAHLsledTPLDEGLLRTRLAQLQLGADKVTLPlSALSGGERLKAALACVLWRREPaqLLLLDEPT 486
Cdd:cd03298    84 HLTveqNVGLGLSPGLKL----TAEDRQAIEVALARVGLAGLEKRLP-GELSGGERQRVALARVLVRDKP--VLLLDEPF 156

                  ....*.
gi 1512845752 487 NHLDLA 492
Cdd:cd03298   157 AALDPA 162
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
129-219 1.76e-05

ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 45.94  E-value: 1.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 129 AFREADLPPFSADRPAfSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDR----QGREWLYHQLESWQGGALIASHDRE 204
Cdd:COG4136   117 ALEEAGLAGFADRDPA-TLSGGQRARVALLRALLAEPRALLLDEPFSKLDAalraQFREFVFEQIRQRGIPALLVTHDEE 195
                          90
                  ....*....|....*
gi 1512845752 205 LLTRMPRIIELTPTA 219
Cdd:COG4136   196 DAPAAGRVLDLGNWQ 210
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
11-178 2.23e-05

ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).


Pssm-ID: 213227 [Multi-domain]  Cd Length: 227  Bit Score: 45.63  E-value: 2.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  11 VLHQVTCQFATGQTLfgplsvslepslcGLVGRNGVGKTRLLRLLAGL-----DSPAGGHIERAAAVAWVAQQPTLTPET 85
Cdd:cd03260    15 ALKDISLDIPKGEIT-------------ALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLDVDVLELRR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  86 TLATLLGYASVFAAlsrleqgqGLADDFDL---LDGHWD---LTDRLSLAFREADLPPFSADRP-AFSLSGGERMKALLC 158
Cdd:cd03260    82 RVGMVFQKPNPFPG--------SIYDNVAYglrLHGIKLkeeLDERVEEALRKAALWDEVKDRLhALGLSGGQQQRLCLA 153
                         170       180
                  ....*....|....*....|
gi 1512845752 159 GAFVSGADYLLLDEPTNHLD 178
Cdd:cd03260   154 RALANEPEVLLLDEPTSALD 173
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
39-178 2.24e-05

Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 47.09  E-value: 2.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  39 GLVGRNGVGKTRLLRLLAGLDSPAGGHIEraaavawvaqqPTLTpettlatlLGYasvfaalsrleQGQGLADDFD---- 114
Cdd:COG1245   370 GIVGPNGIGKTTFAKILAGVLKPDEGEVD-----------EDLK--------ISY-----------KPQYISPDYDgtve 419
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 115 -LLDGHwdLTDRLSLAFREADL-PPFSA----DRPAFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLD 178
Cdd:COG1245   420 eFLRSA--NTDDFGSSYYKTEIiKPLGLekllDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 487
LPS_export_lptB TIGR04406
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ...
39-173 2.53e-05

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: 45.73  E-value: 2.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  39 GLVGRNGVGKTRLLRLLAGLDSPAGGHIEraaavaWVAQQPTLTPETTLATL-LGY----ASVFAALSrleqgqgLADDF 113
Cdd:TIGR04406  31 GLLGPNGAGKTTSFYMIVGLVRPDAGKIL------IDGQDITHLPMHERARLgIGYlpqeASIFRKLT-------VEENI 97
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1512845752 114 D-LLDGHWDLTDRLSLAFREADLPPFS----ADRPAFSLSGGERMKALLCGAFVSGADYLLLDEP 173
Cdd:TIGR04406  98 MaVLEIRKDLDRAEREERLEALLEEFQishlRDNKAMSLSGGERRRVEIARALATNPKFILLDEP 162
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
29-178 2.54e-05

ABC-type uncharacterized transport system, ATPase component [General function prediction only];


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 46.23  E-value: 2.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  29 LSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIEraaavawvaqqptltpettlatLLGY-------------A 94
Cdd:COG4586    41 ISFTIEPgEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR----------------------VLGYvpfkrrkefarriG 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  95 SVFaalsrleqGQ--------GLADDFDLLDGHWDLTDRlslAFREA--------DLPPFsADRPAFSLSGGERMKALLC 158
Cdd:COG4586    99 VVF--------GQrsqlwwdlPAIDSFRLLKAIYRIPDA---EYKKRldelvellDLGEL-LDTPVRQLSLGQRMRCELA 166
                         170       180
                  ....*....|....*....|
gi 1512845752 159 GAFVSGADYLLLDEPTNHLD 178
Cdd:COG4586   167 AALLHRPKILFLDEPTIGLD 186
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
455-518 2.59e-05

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: 47.07  E-value: 2.59e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1512845752 455 SALSGGERLKAALACVLWRrePAQLLLLDEPTNHLDLASTQAI-ESALAAFPG-AMLVVSHDEAFL 518
Cdd:COG4987   470 RRLSGGERRRLALARALLR--DAPILLLDEPTEGLDAATEQALlADLLEALAGrTVLLITHRLAGL 533
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
140-185 4.79e-05

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: 45.08  E-value: 4.79e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1512845752 140 ADRPAFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGREWL 185
Cdd:COG1119   136 ADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELL 181
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
370-514 5.76e-05

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: 44.71  E-value: 5.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 370 IALKGPNGCGKTTLLKTLLGLEQAASGDVRLSV-SAAYLDQHLtQLDLSLSVMAHL-SLEDTPLDEGLLRTRLAQ-LQLg 446
Cdd:cd03237    28 IGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELdTVSYKPQYI-KADYEGTVRDLLsSITKDFYTHPYFKTEIAKpLQI- 105
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1512845752 447 ADKVTLPLSALSGGERLKAALACVLWRrePAQLLLLDEPTNHLD----LASTQAIES-ALAAFPGAMlVVSHD 514
Cdd:cd03237   106 EQILDREVPELSGGELQRVAIAACLSK--DADIYLLDEPSAYLDveqrLMASKVIRRfAENNEKTAF-VVEHD 175
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
14-229 6.23e-05

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 44.48  E-value: 6.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  14 QVTCQFATGQTLFGPLSVSLEPS-LCGLVGRNGVGKTRLLRLLAGLDSPAGGHI---ERAAAVAWVAQQPTLTPETTLA- 88
Cdd:PRK10908    6 HVSKAYLGGRQALQGVTFHMRPGeMAFLTGHSGAGKSTLLKLICGIERPSAGKIwfsGHDITRLKNREVPFLRRQIGMIf 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  89 ---TLLGYASVFAALSRLEQGQGLADDfdlldghwDLTDRLSLAFREADLPPFSADRPaFSLSGGERMKALLCGAFVSGA 165
Cdd:PRK10908   86 qdhHLLMDRTVYDNVAIPLIIAGASGD--------DIRRRVSAALDKVGLLDKAKNFP-IQLSGGEQQRVGIARAVVNKP 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1512845752 166 DYLLLDEPTNHLDRQGREWLYHQLESWQG---GALIASHDRELLTRMPRIIeLTPTALRSYGGNYDE 229
Cdd:PRK10908  157 AVLLADEPTGNLDDALSEGILRLFEEFNRvgvTVLMATHDIGLISRRSYRM-LTLSDGHLHGGVGGE 222
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
448-514 6.93e-05

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 44.65  E-value: 6.93e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1512845752 448 DKVTLPLSALSGGERLKAALACVLWRRepAQLLLLDEPTNHLDLASTQAIESALAAFPG--AMLVVSHD 514
Cdd:PRK14246  145 DRLNSPASQLSGGQQQRLTIARALALK--PKVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHN 211
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
23-174 7.53e-05

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: 44.20  E-value: 7.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  23 QTLFGpLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIE-------RaaavawvaqqptLTPETTLATLLGYA 94
Cdd:COG0410    17 HVLHG-VSLEVEEgEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRfdgeditG------------LPPHRIARLGIGYV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  95 ----SVFAALS---RLEQGQGLADDFDllDGHWDLTDRLSLaF-READLppfsADRPAFSLSGGER-MKALlcG-AFVSG 164
Cdd:COG0410    84 pegrRIFPSLTveeNLLLGAYARRDRA--EVRADLERVYEL-FpRLKER----RRQRAGTLSGGEQqMLAI--GrALMSR 154
                         170
                  ....*....|
gi 1512845752 165 ADYLLLDEPT 174
Cdd:COG0410   155 PKLLLLDEPS 164
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
36-202 8.35e-05

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 44.45  E-value: 8.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  36 SLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIERAAAVAWVAQQPTLTPETTLATL-------LGYASVFAALSRLEQGQG 108
Cdd:PRK13636   33 EVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMKLRESVGMVfqdpdnqLFSASVYQDVSFGAVNLK 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 109 LADDfdlldghwDLTDRLSLAFREADLPPFSaDRPAFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGREWLYHQ 188
Cdd:PRK13636  113 LPED--------EVRKRVDNALKRTGIEHLK-DKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKL 183
                         170
                  ....*....|....*...
gi 1512845752 189 LESWQGGA----LIASHD 202
Cdd:PRK13636  184 LVEMQKELgltiIIATHD 201
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
417-521 8.36e-05

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: 45.20  E-value: 8.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 417 SLSVMAHLSLEDTPLDEGLLRTRLAQLQLGADKVTLPLSALSGGERLKAALA-CVLWRrepAQLLLLDEPTNHLDLASTQ 495
Cdd:TIGR02633 364 VLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLPIGRLSGGNQQKAVLAkMLLTN---PRVLILDEPTRGVDVGAKY 440
                          90       100
                  ....*....|....*....|....*....
gi 1512845752 496 AIE---SALAAFPGAMLVVSHDEAFLQGL 521
Cdd:TIGR02633 441 EIYkliNQLAQEGVAIIVVSSELAEVLGL 469
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
360-513 9.09e-05

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: 43.14  E-value: 9.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 360 LNWRIDGPMRIALKGPNGCGKTTLLKTLLGLEQAASGDVRLSvsaaylDQHLTQLDLSlSVMAHLSL--EDTPLDEGLLR 437
Cdd:cd03228    21 VSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILID------GVDLRDLDLE-SLRKNIAYvpQDPFLFSGTIR 93
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1512845752 438 TRLaqlqlgadkvtlplsaLSGGERLKAALACVLWRRepAQLLLLDEPTNHLDLASTQAIESALAAFPG--AMLVVSH 513
Cdd:cd03228    94 ENI----------------LSGGQRQRIAIARALLRD--PPILILDEATSALDPETEALILEALRALAKgkTVIVIAH 153
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
27-202 9.43e-05

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 44.15  E-value: 9.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  27 GPLSVSLEPS-LCGLVGRNGVGKTRLLRLLAGLdSPAGGHIeraaavaWVAQQPTLT-PETTLATLLGYAS--------- 95
Cdd:PRK03695   13 GPLSAEVRAGeILHLVGPNGAGKSTLLARMAGL-LPGSGSI-------QFAGQPLEAwSAAELARHRAYLSqqqtppfam 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  96 -VFAALSR-LEQGQGLADDFDLLDghwDLTDRLSLafreADLPPfsadRPAFSLSGGERMKALLCGAFV-------SGAD 166
Cdd:PRK03695   85 pVFQYLTLhQPDKTRTEAVASALN---EVAEALGL----DDKLG----RSVNQLSGGEWQRVRLAAVVLqvwpdinPAGQ 153
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1512845752 167 YLLLDEPTNHLDRQGREWLY---HQLESWQGGALIASHD 202
Cdd:PRK03695  154 LLLLDEPMNSLDVAQQAALDrllSELCQQGIAVVMSSHD 192
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
360-514 1.02e-04

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: 43.68  E-value: 1.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 360 LNWRIDGPMRIALKGPNGCGKTTLLKTLLGLEQAASGDVRL--------SVSAAYLDQH--------LTQLDL-SLSVMA 422
Cdd:cd03235    18 VSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVfgkplekeRKRIGYVPQRrsidrdfpISVRDVvLMGLYG 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 423 HLSLEDTP-------LDEGLLRTRLAQLqlgADKvtlPLSALSGGERLKAALACVLWRRepAQLLLLDEPTNHLDLASTQ 495
Cdd:cd03235    98 HKGLFRRLskadkakVDEALERVGLSEL---ADR---QIGELSGGQQQRVLLARALVQD--PDLLLLDEPFAGVDPKTQE 169
                         170       180
                  ....*....|....*....|..
gi 1512845752 496 AIESALAAFPG---AMLVVSHD 514
Cdd:cd03235   170 DIYELLRELRRegmTILVVTHD 191
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
457-501 1.17e-04

lipid A ABC transporter ATP-binding protein/permease MsbA;


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 45.01  E-value: 1.17e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1512845752 457 LSGGERLKAALACVLWRREPaqLLLLDEPTNHLDLASTQAIESAL 501
Cdd:PRK11176  481 LSGGQRQRIAIARALLRDSP--ILILDEATSALDTESERAIQAAL 523
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
422-514 1.21e-04

ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 43.59  E-value: 1.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 422 AHLSLED------------TPLDEGLLRTRLAQLQLGADKVTLPlSALSGGERLKAALACVLWRREPaqLLLLDEP---- 485
Cdd:COG3840    84 PHLTVAQniglglrpglklTAEQRAQVEQALERVGLAGLLDRLP-GQLSGGQRQRVALARCLVRKRP--ILLLDEPfsal 160
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1512845752 486 -----TNHLDLASTQAIESALaafpgAMLVVSHD 514
Cdd:COG3840   161 dpalrQEMLDLVDELCRERGL-----TVLMVTHD 189
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
453-518 1.24e-04

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: 44.78  E-value: 1.24e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 453 PLSALSGGERLKAALACVLWRRepAQLLLLDEPTNHLD----LASTQAIESaLAAFPGAMLVVSHDEAFL 518
Cdd:COG1245   209 DISELSGGELQRVAIAAALLRD--ADFYFFDEPSSYLDiyqrLNVARLIRE-LAEEGKYVLVVEHDLAIL 275
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
40-180 1.25e-04

ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 43.41  E-value: 1.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  40 LVGRNGVGKTRLLRLLAG--LDSPAGGHIEraaavawvAQQPTLTPETTLATLLGYASVFAALSRLEQGQGLADDFDLLd 117
Cdd:COG2401    61 IVGASGSGKSTLLRLLAGalKGTPVAGCVD--------VPDNQFGREASLIDAIGRKGDFKDAVELLNAVGLSDAVLWL- 131
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1512845752 118 ghwdltdrlslafreadlppfsadRPAFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQ 180
Cdd:COG2401   132 ------------------------RRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQ 170
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
39-215 1.36e-04

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: 42.42  E-value: 1.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  39 GLVGRNGVGKTRLLRLLAGLDSPAGGHIeraaavawvaqqptltpettlatllgyasvfaalsrleqgqgladdfdLLDG 118
Cdd:cd03216    30 ALLGENGAGKSTLMKILSGLYKPDSGEI------------------------------------------------LVDG 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 119 HwdltdrlSLAFREadlpPFSADR----PAFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGREWLYHQLESW-- 192
Cdd:cd03216    62 K-------EVSFAS----PRDARRagiaMVYQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLra 130
                         170       180
                  ....*....|....*....|....
gi 1512845752 193 QGGALI-ASHdrelltRMPRIIEL 215
Cdd:cd03216   131 QGVAVIfISH------RLDEVFEI 148
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
11-183 1.37e-04

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 44.33  E-value: 1.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  11 VLHQVTCQFATgQTLFGPLSVSL-EPSLCGLVGRNGVGKTRLLRLLAGLDSPAGGHI--------ERAAAVA---WVAQQ 78
Cdd:PRK11432    8 VLKNITKRFGS-NTVIDNLNLTIkQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIfidgedvtHRSIQQRdicMVFQS 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  79 PTLTPETTLATLLGYASVFAALSRLEQGQgladdfdlldghwdltdRLSLAFREADLPPFsADRPAFSLSGGERMKALLC 158
Cdd:PRK11432   87 YALFPHMSLGENVGYGLKMLGVPKEERKQ-----------------RVKEALELVDLAGF-EDRYVDQISGGQQQRVALA 148
                         170       180
                  ....*....|....*....|....*....
gi 1512845752 159 GAFVSGADYLLLDEPTNHLD----RQGRE 183
Cdd:PRK11432  149 RALILKPKVLLFDEPLSNLDanlrRSMRE 177
cbiO PRK13645
energy-coupling factor transporter ATPase;
135-209 1.43e-04

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 43.84  E-value: 1.43e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1512845752 135 LPPFSADRPAFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGRE---WLYHQLESWQGGALI-ASHDRELLTRM 209
Cdd:PRK13645  139 LPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEdfiNLFERLNKEYKKRIImVTHNMDQVLRI 217
PLN03073 PLN03073
ABC transporter F family; Provisional
369-518 1.44e-04

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 44.47  E-value: 1.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 369 RIALKGPNGCGKTTLLKTLLG--------------LEQAASGD---------------VRLSVSAAYLDQHLTQLDLSLS 419
Cdd:PLN03073  205 HYGLVGRNGTGKTTFLRYMAMhaidgipkncqilhVEQEVVGDdttalqcvlntdierTQLLEEEAQLVAQQRELEFETE 284
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 420 VMAHLSLEDTPLDEGLLRTRLAQ-----------------------LQLGADKVTLPLSALSGGERLKAALACVLWrREP 476
Cdd:PLN03073  285 TGKGKGANKDGVDKDAVSQRLEEiykrlelidaytaearaasilagLSFTPEMQVKATKTFSGGWRMRIALARALF-IEP 363
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1512845752 477 aQLLLLDEPTNHLDLASTQAIESALAAFPGAMLVVSHDEAFL 518
Cdd:PLN03073  364 -DLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFL 404
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
455-518 1.45e-04

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: 44.41  E-value: 1.45e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1512845752 455 SALSGGERLKAALACVLWrREPaQLLLLDEPTNHLD----LASTQAIESALAAFPGAMLVVSHDEAFL 518
Cdd:TIGR03269 426 DELSEGERHRVALAQVLI-KEP-RIVILDEPTGTMDpitkVDVTHSILKAREEMEQTFIIVSHDMDFV 491
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
40-178 1.83e-04

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: 42.87  E-value: 1.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  40 LVGRNGVGKTRLLRLLAGLDSPAGGHIErAAAVAWVAQQPTLTPettLATLLGYASVFAALSrLEQGQGLADDFDLldgH 119
Cdd:cd03298    29 IVGPSGSGKSTLLNLIAGFETPQSGRVL-INGVDVTAAPPADRP---VSMLFQENNLFAHLT-VEQNVGLGLSPGL---K 100
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1512845752 120 WDLTDR--LSLAFREADLPPFSADRPAfSLSGGERMKALLCGAFVSGADYLLLDEPTNHLD 178
Cdd:cd03298   101 LTAEDRqaIEVALARVGLAGLEKRLPG-ELSGGERQRVALARVLVRDKPVLLLDEPFAALD 160
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
370-514 1.84e-04

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 43.22  E-value: 1.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 370 IALKGPNGCGKTTLLKTLLGLEQAASGDVRL------SVSAAYLDQHL------TQLDLSLSV----------MAHLSLE 427
Cdd:PRK13548   31 VAILGPNGAGKSTLLRALSGELSPDSGEVRLngrplaDWSPAELARRRavlpqhSSLSFPFTVeevvamgrapHGLSRAE 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 428 DTPL-DEGLLRTRLAQLqlgADKvtlPLSALSGGERLKAALACVL---WRREPAQ-LLLLDEPTNHLDLASTQAIESALA 502
Cdd:PRK13548  111 DDALvAAALAQVDLAHL---AGR---DYPQLSGGEQQRVQLARVLaqlWEPDGPPrWLLLDEPTSALDLAHQHHVLRLAR 184
                         170
                  ....*....|....*.
gi 1512845752 503 AF----PGAMLVVSHD 514
Cdd:PRK13548  185 QLaherGLAVIVVLHD 200
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
31-174 1.93e-04

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 44.35  E-value: 1.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  31 VSLE-PS--LCGLVGRNGVGKTRLLRLLAGLDSPAGGHIE------RAAAVAWVAQQ--------------PTLTPETTL 87
Cdd:NF033858   20 VSLDiPAgcMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEvlggdmADARHRRAVCPriaympqglgknlyPTLSVFENL 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  88 ---ATLLGyasvfaaLSRLEQGQGLADdfdlldghwdLTDRLSLAfreadlpPFsADRPAFSLSGGERMKALLCGAFVSG 164
Cdd:NF033858  100 dffGRLFG-------QDAAERRRRIDE----------LLRATGLA-------PF-ADRPAGKLSGGMKQKLGLCCALIHD 154
                         170
                  ....*....|
gi 1512845752 165 ADYLLLDEPT 174
Cdd:NF033858  155 PDLLILDEPT 164
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
29-174 1.95e-04

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: 43.19  E-value: 1.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  29 LSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIeRAAAVAWVAQQPTLTPETTLA------TLLGYASVF---- 97
Cdd:cd03219    19 VSFSVRPgEIHGLIGPNGAGKTTLFNLISGFLRPTSGSV-LFDGEDITGLPPHEIARLGIGrtfqipRLFPELTVLenvm 97
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1512845752  98 -AALSRLEQGQGLADDFDLLDGHWDLTDRLsLAFreADLPPFsADRPAFSLSGGERMKALLCGAFVSGADYLLLDEPT 174
Cdd:cd03219    98 vAAQARTGSGLLLARARREEREARERAEEL-LER--VGLADL-ADRPAGELSYGQQRRLEIARALATDPKLLLLDEPA 171
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
11-178 2.22e-04

ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213223 [Multi-domain]  Cd Length: 241  Bit Score: 42.94  E-value: 2.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  11 VLHQVTCQFATGQtlfgplsvslepsLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIERAAAVAWVAQQ------------ 78
Cdd:cd03256    16 ALKDVSLSINPGE-------------FVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGkalrqlrrqigm 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  79 ----PTLTPETT-----LATLLGYASVFAALSRLEQGQGLADDFDLLdghwDLTDRLSLAFREADlppfsadrpafSLSG 149
Cdd:cd03256    83 ifqqFNLIERLSvlenvLSGRLGRRSTWRSLFGLFPKEEKQRALAAL----ERVGLLDKAYQRAD-----------QLSG 147
                         170       180
                  ....*....|....*....|....*....
gi 1512845752 150 GERMKALLCGAFVSGADYLLLDEPTNHLD 178
Cdd:cd03256   148 GQQQRVAIARALMQQPKLILADEPVASLD 176
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
391-518 2.23e-04

The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.


Pssm-ID: 213203 [Multi-domain]  Cd Length: 255  Bit Score: 43.12  E-value: 2.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 391 EQAASGDVRLSVSAAYLDQHLTQLDLSLSVMAHLSLEDTPLDEGLLRTRLAQLqlgadkVTLPLSALSGGERLKAALACV 470
Cdd:cd03236    80 TKLLEGDVKVIVKPQYVDLIPKAVKGKVGELLKKKDERGKLDELVDQLELRHV------LDRNIDQLSGGELQRVAIAAA 153
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1512845752 471 LWRRepAQLLLLDEPTNHLD----LASTQAIESaLAAFPGAMLVVSHDEAFL 518
Cdd:cd03236   154 LARD--ADFYFFDEPSSYLDikqrLNAARLIRE-LAEDDNYVLVVEHDLAVL 202
cbiO PRK13637
energy-coupling factor transporter ATPase;
140-213 2.53e-04

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 43.11  E-value: 2.53e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1512845752 140 ADRPAFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGREWLYHQL----ESWQGGALIASHDRELLTRMP-RII 213
Cdd:PRK13637  138 KDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIkelhKEYNMTIILVSHSMEDVAKLAdRII 216
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
315-515 2.55e-04

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: 43.89  E-value: 2.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 315 AVQQARERVEEETPVMFTLPGSEVAA------GKQVLVVESLQLDHAPAAPLNWRIDGPM----RIALKGPNGCGKTTLL 384
Cdd:TIGR02868 299 RVRAAAERIVEVLDAAGPVAEGSAPAagavglGKPTLELRDLSAGYPGAPPVLDGVSLDLppgeRVAILGPSGSGKSTLL 378
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 385 KTLLGLEQAASGDVRLS-VSAAYLDQHLTQLDLSLSVM-AHLSleDTPLDEGLLRTR-----------LAQLQLGADKVT 451
Cdd:TIGR02868 379 ATLAGLLDPLQGEVTLDgVPVSSLDQDEVRRRVSVCAQdAHLF--DTTVRENLRLARpdatdeelwaaLERVGLADWLRA 456
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1512845752 452 LPL----------SALSGGERLKAALACVLWrrEPAQLLLLDEPTNHLDL-ASTQAIESALAAFPG-AMLVVSHDE 515
Cdd:TIGR02868 457 LPDgldtvlgeggARLSGGERQRLALARALL--ADAPILLLDEPTEHLDAeTADELLEDLLAALSGrTVVLITHHL 530
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
141-193 2.73e-04

ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213266 [Multi-domain]  Cd Length: 235  Bit Score: 42.71  E-value: 2.73e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1512845752 141 DRPAFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGREWLYHQLESWQ 193
Cdd:cd03299   124 NRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIR 176
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
440-515 2.81e-04

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: 42.48  E-value: 2.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 440 LAQLQLGADKVTLPlSALSGGERLKAALAcvlwrR----EPaQLLLLDEPTNHLDLASTQAIESALAAFPG----AMLVV 511
Cdd:cd03255   125 LERVGLGDRLNHYP-SELSGGQQQRVAIA-----RalanDP-KIILADEPTGNLDSETGKEVMELLRELNKeagtTIVVV 197

                  ....
gi 1512845752 512 SHDE 515
Cdd:cd03255   198 THDP 201
PRK10522 PRK10522
multidrug transporter membrane component/ATP-binding component; Provisional
12-216 2.98e-04

multidrug transporter membrane component/ATP-binding component; Provisional


Pssm-ID: 236707 [Multi-domain]  Cd Length: 547  Bit Score: 43.42  E-value: 2.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  12 LHQVTCQFATGQTLFGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIERAAAvawvaqqptltpETTLATL 90
Cdd:PRK10522  325 LRNVTFAYQDNGFSVGPINLTIKRgELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGK------------PVTAEQP 392
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  91 LGYASVFAAL-------SRLEQGQGLADDFDLLDG---HWDLTDRLSLA-FREADLppfsadrpafSLSGGERMKALLCG 159
Cdd:PRK10522  393 EDYRKLFSAVftdfhlfDQLLGPEGKPANPALVEKwleRLKMAHKLELEdGRISNL----------KLSKGQKKRLALLL 462
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1512845752 160 AFVSGADYLLLDEPTNHLDRQGREWLYHQLESW---QGGALIA-SH--------DRELLTRMPRIIELT 216
Cdd:PRK10522  463 ALAEERDILLLDEWAADQDPHFRREFYQVLLPLlqeMGKTIFAiSHddhyfihaDRLLEMRNGQLSELT 531
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
454-501 3.05e-04

Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.


Pssm-ID: 213180 [Multi-domain]  Cd Length: 194  Bit Score: 42.15  E-value: 3.05e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1512845752 454 LSALSGGERLKAALACVLWRREPaqLLLLDEPTNHLDLASTQAIESAL 501
Cdd:cd03213   109 LRGLSGGERKRVSIALELVSNPS--LLFLDEPTSGLDSSSALQVMSLL 154
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
455-513 3.29e-04

ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.


Pssm-ID: 213215 [Multi-domain]  Cd Length: 226  Bit Score: 42.46  E-value: 3.29e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1512845752 455 SALSGGERLKAALACVLWRrEPaQLLLLDEPTNHLDLASTQAIESALAAFPG--AMLVVSH 513
Cdd:cd03248   149 SQLSGGQKQRVAIARALIR-NP-QVLILDEATSALDAESEQQVQQALYDWPErrTVLVIAH 207
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
34-198 3.66e-04

retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]


Pssm-ID: 130324 [Multi-domain]  Cd Length: 2272  Bit Score: 43.46  E-value: 3.66e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752   34 EPSLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIeraaavawvaqqptltpettlatLLGYASVFAALSRLEQGQGLADDF 113
Cdd:TIGR01257  955 ENQITAFLGHNGAGKTTTLSILTGLLPPTSGTV-----------------------LVGGKDIETNLDAVRQSLGMCPQH 1011
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  114 DLLDGHWDLTDRLSL-------AFREADLP----------PFSADRPAFSLSGGERMKALLCGAFVSGADYLLLDEPTNH 176
Cdd:TIGR01257 1012 NILFHHLTVAEHILFyaqlkgrSWEEAQLEmeamledtglHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSG 1091
                          170       180
                   ....*....|....*....|..
gi 1512845752  177 LDRQGREWLYHQLESWQGGALI 198
Cdd:TIGR01257 1092 VDPYSRRSIWDLLLKYRSGRTI 1113
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
40-221 3.86e-04

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 42.07  E-value: 3.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  40 LVGRNGVGKTRLLRLLAGLDSPAGGHIERAAAVAwvaqqpTLTPETTLATL----LGYasVFAA------LSRLEQGQGL 109
Cdd:PRK10584   41 LIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPL------HQMDEEARAKLrakhVGF--VFQSfmliptLNALENVELP 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 110 AddfdLLDGHWD---------LTDRLSLAFREADLPPfsadrpafSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQ 180
Cdd:PRK10584  113 A----LLRGESSrqsrngakaLLEQLGLGKRLDHLPA--------QLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQ 180
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1512845752 181 GREW---LYHQLESWQGGALI-ASHDRELLTRMPRIIELTPTALR 221
Cdd:PRK10584  181 TGDKiadLLFSLNREHGTTLIlVTHDLQLAARCDRRLRLVNGQLQ 225
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
29-67 3.88e-04

ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 443319 [Multi-domain]  Cd Length: 358  Bit Score: 42.78  E-value: 3.88e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1512845752  29 LSVSLE---PSLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIE 67
Cdd:COG4148    16 LDVDFTlpgRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIR 57
ABC_sbcCD cd03279
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ...
142-222 4.13e-04

ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.


Pssm-ID: 213246 [Multi-domain]  Cd Length: 213  Bit Score: 41.87  E-value: 4.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 142 RPAFSLSGGERMKALLCGAF-----VSGA-----DYLLLDEPTNHLDRQGREWLYHQLESWQGG---ALIASHDRELLTR 208
Cdd:cd03279   119 RPVSTLSGGETFLASLSLALalsevLQNRggarlEALFIDEGFGTLDPEALEAVATALELIRTEnrmVGVISHVEELKER 198
                          90
                  ....*....|....
gi 1512845752 209 MPRIIELTPTALRS 222
Cdd:cd03279   199 IPQRLEVIKTPGGS 212
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
10-219 4.28e-04

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: 40.99  E-value: 4.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  10 FVLHQVTCQFATGQTLFGPLSVSLEPslcG----LVGRNGVGKTRLLRLLAGLDSPAGGHIERAAAVAWV--AQQPTLtP 83
Cdd:cd03223     1 IELENLSLATPDGRVLLKDLSFEIKP---GdrllITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLflPQRPYL-P 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  84 ETTLATLLGYAsvfaalsrleqgqgladdfdlldghWDLTdrlslafreadlppfsadrpafsLSGGERMKALLCGAFVS 163
Cdd:cd03223    77 LGTLREQLIYP-------------------------WDDV-----------------------LSGGEQQRLAFARLLLH 108
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1512845752 164 GADYLLLDEPTNHLDRQGREWLYHQLESwQGGALIA-SHDRELLTRMPRIIELTPTA 219
Cdd:cd03223   109 KPKFVFLDEATSALDEESEDRLYQLLKE-LGITVISvGHRPSLWKFHDRVLDLDGEG 164
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
369-492 5.66e-04

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 41.49  E-value: 5.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 369 RIALKGPNGCGKTTLLKTLLGLEQAASGDVRLSVSaaylDQHLT---QLDLSL-----SVMAHLSLEDT---PLDEGLlr 437
Cdd:PRK10771   27 RVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQ----DHTTTppsRRPVSMlfqenNLFSHLTVAQNiglGLNPGL-- 100
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1512845752 438 tRL-----AQLQLGADKVT-------LPlSALSGGERLKAALACVLWRREPaqLLLLDEPTNHLDLA 492
Cdd:PRK10771  101 -KLnaaqrEKLHAIARQMGiedllarLP-GQLSGGQRQRVALARCLVREQP--ILLLDEPFSALDPA 163
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
370-497 5.69e-04

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: 41.55  E-value: 5.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 370 IALKGPNGCGKTTLLKTLLGLEQAASGDVRLS--VSAAYLDQHL----------TQLDLSLSVMAHLSL--EDTPLDEGL 435
Cdd:cd03267    50 VGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAglVPWKRRKKFLrrigvvfgqkTQLWWDLPVIDSFYLlaAIYDLPPAR 129
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1512845752 436 LRTRLAQ----LQLGaDKVTLPLSALSGGERLKAALACVLWrREPaQLLLLDEPTNHLDLASTQAI 497
Cdd:cd03267   130 FKKRLDElselLDLE-ELLDTPVRQLSLGQRMRAEIAAALL-HEP-EILFLDEPTIGLDVVAQENI 192
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
11-67 6.61e-04

ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440744 [Multi-domain]  Cd Length: 241  Bit Score: 41.50  E-value: 6.61e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1512845752  11 VLHQVTCQFATGQTLfgplsvslepslcGLVGRNGVGKTRLLRLLAGLDSPAGGHIE 67
Cdd:COG1127    20 VLDGVSLDVPRGEIL-------------AIIGGSGSGKSVLLKLIIGLLRPDSGEIL 63
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
453-518 7.09e-04

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 42.49  E-value: 7.09e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 453 PLSALSGGERLKAALACVLWRRepAQLLLLDEPTNHLDLasTQAIESALA----AFPGAMLVVSHDEAFL 518
Cdd:PRK13409  209 DISELSGGELQRVAIAAALLRD--ADFYFFDEPTSYLDI--RQRLNVARLirelAEGKYVLVVEHDLAVL 274
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
28-66 7.81e-04

ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 41.98  E-value: 7.81e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1512845752  28 PLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPAGGHI 66
Cdd:COG3839    21 DIDLDIEDgEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEI 60
ABC_SMC2_euk cd03273
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ...
454-515 8.59e-04

ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).


Pssm-ID: 213240 [Multi-domain]  Cd Length: 251  Bit Score: 41.13  E-value: 8.59e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1512845752 454 LSALSGGERLKAALACVL--WRREPAQLLLLDEPTNHLDLASTQAIESAL-AAFPGA-MLVVSHDE 515
Cdd:cd03273   164 LTELSGGQRSLVALSLILalLLFKPAPMYILDEVDAALDLSHTQNIGRMIkTHFKGSqFIVVSLKE 229
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
371-514 9.20e-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: 41.01  E-value: 9.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 371 ALKGPNGCG-----KTTLLKTLLGLEQAASGDVRLSVSAAYLD---------------QHLTQLDLS------LSVMAHL 424
Cdd:cd03260    30 ALIGPSGCGkstllRLLNRLNDLIPGAPDEGEVLLDGKDIYDLdvdvlelrrrvgmvfQKPNPFPGSiydnvaYGLRLHG 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 425 SLEDTPLDEgLLRTRLAQLQLGaDKVTLPLSA--LSGGERLKAALACVlWRREPAqLLLLDEPTNHLDLASTQAIESALA 502
Cdd:cd03260   110 IKLKEELDE-RVEEALRKAALW-DEVKDRLHAlgLSGGQQQRLCLARA-LANEPE-VLLLDEPTSALDPISTAKIEELIA 185
                         170
                  ....*....|....
gi 1512845752 503 AF--PGAMLVVSHD 514
Cdd:cd03260   186 ELkkEYTIVIVTHN 199
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
20-234 9.56e-04

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 40.85  E-value: 9.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  20 ATGQTLFGPLSVSLEPSLCGLV-GRNGVGKTRLLRLLAGLDSPAGGHIeraaaVAWVAQQPTLTPET---------TLAT 89
Cdd:PRK10247   17 AGDAKILNNISFSLRAGEFKLItGPSGCGKSTLLKIVASLISPTSGTL-----LFEGEDISTLKPEIyrqqvsycaQTPT 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  90 LLGyASVFAALSRLEQGQGLADDFDLLdghwdltdRLSLAFREadLPPFSADRPAFSLSGGERMKALLCGAFVSGADYLL 169
Cdd:PRK10247   92 LFG-DTVYDNLIFPWQIRNQQPDPAIF--------LDDLERFA--LPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLL 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1512845752 170 LDEPTNHLDRQGR----EWLYHQLESWQGGALIASHDRELLTRMPRIIELTPtalrsYGGNYDEYQRQR 234
Cdd:PRK10247  161 LDEITSALDESNKhnvnEIIHRYVREQNIAVLWVTHDKDEINHADKVITLQP-----HAGEMQEARYEL 224
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
457-515 9.73e-04

ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.


Pssm-ID: 213194 [Multi-domain]  Cd Length: 162  Bit Score: 40.04  E-value: 9.73e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1512845752 457 LSGGERLKAALACVL--WRREPAQLLLLDEPTNHLDLASTQAIESALAAF--PGA-MLVVSHDE 515
Cdd:cd03227    78 LSGGEKELSALALILalASLKPRPLYILDEIDRGLDPRDGQALAEAILEHlvKGAqVIVITHLP 141
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
417-512 1.03e-03

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 41.84  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 417 SLSVMAHLSLEDTPLDEGLLRTRLAQLQLGADKVTLPLSALSGGERLKAALA-CVLwrREPaQLLLLDEPTNHLDLASTQ 495
Cdd:PRK13549  366 ALDRFTGGSRIDDAAELKTILESIQRLKVKTASPELAIARLSGGNQQKAVLAkCLL--LNP-KILILDEPTRGIDVGAKY 442
                          90       100
                  ....*....|....*....|
gi 1512845752 496 AIE---SALAAFPGAMLVVS 512
Cdd:PRK13549  443 EIYkliNQLVQQGVAIIVIS 462
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
39-186 1.08e-03

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: 40.82  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  39 GLVGRNGVGKTRLLRLLAGLDSPAGGH------------IERAAAVAWVAQQPTLTPETT-------LATLLGYASVFAA 99
Cdd:cd03265    30 GLLGPNGAGKTTTIKMLTTLLKPTSGRatvaghdvvrepREVRRRIGIVFQDLSVDDELTgwenlyiHARLYGVPGAERR 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 100 lSRLEQgqgLADDFDLLDghwdltdrlslafreadlppfSADRPAFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDR 179
Cdd:cd03265   110 -ERIDE---LLDFVGLLE---------------------AADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDP 164

                  ....*....
gi 1512845752 180 QGRE--WLY 186
Cdd:cd03265   165 QTRAhvWEY 173
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
429-513 1.11e-03

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: 40.84  E-value: 1.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 429 TPLDEGLLRTRLAQLQLG--ADKvtlPLSALSGGERLKAALAcvlwR---REPaQLLLLDEPTNHLDLAST----QAIEs 499
Cdd:COG1119   116 TDEQRERARELLELLGLAhlADR---PFGTLSQGEQRRVLIA----RalvKDP-ELLILDEPTAGLDLGARelllALLD- 186
                          90
                  ....*....|....*
gi 1512845752 500 ALAAFPG-AMLVVSH 513
Cdd:COG1119   187 KLAAEGApTLVLVTH 201
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
31-66 1.16e-03

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: 40.79  E-value: 1.16e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1512845752  31 VSLE---PSLCGLVGRNGVGKTRLLRLLAGLDSPAGGHI 66
Cdd:cd03296    21 VSLDipsGELVALLGPSGSGKTTLLRLIAGLERPDSGTI 59
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
11-66 1.28e-03

ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 41.29  E-value: 1.28e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1512845752  11 VLHQVTCQFATGQTLfgplsvslepslcGLVGRNGVGKTRLLRLLAGLDSPAGGHI 66
Cdd:COG1118    17 LLDDVSLEIASGELV-------------ALLGPSGSGKTTLLRIIAGLETPDSGRI 59
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
29-205 2.16e-03

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 40.10  E-value: 2.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  29 LSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIERAAAVawvaqqptLTPETT--LATLLGY-----------A 94
Cdd:PRK13647   24 LSLSIPEgSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGRE--------VNAENEkwVRSKVGLvfqdpddqvfsS 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  95 SVFAALSRLEQGQGLADDfdlldghwDLTDRLSLAFREADLPPFsADRPAFSLSGGERMKALLCGAFVSGADYLLLDEPT 174
Cdd:PRK13647   96 TVWDDVAFGPVNMGLDKD--------EVERRVEEALKAVRMWDF-RDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPM 166
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1512845752 175 NHLDRQGREWLYHQLE--SWQGGALI-ASHDREL 205
Cdd:PRK13647  167 AYLDPRGQETLMEILDrlHNQGKTVIvATHDVDL 200
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
5-254 2.17e-03

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 40.08  E-value: 2.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752   5 AHIPAFVLHQVTCQFAtGQTLFGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPAGGH------------------ 65
Cdd:PRK14271   17 AAAPAMAAVNLTLGFA-GKTVLDQVSMGFPArAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYrysgdvllggrsifnyrd 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  66 -IERAAAVAWVAQQPTLTPETTLATLLGYASVFAALSRlEQGQGLADDFDLLDGHWD-LTDRLSlafreadlppfsaDRP 143
Cdd:PRK14271   96 vLEFRRRVGMLFQRPNPFPMSIMDNVLAGVRAHKLVPR-KEFRGVAQARLTEVGLWDaVKDRLS-------------DSP 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 144 aFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGREWLYHQLESWQG--GALIASH---------DRELLTRMPRI 212
Cdd:PRK14271  162 -FRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADrlTVIIVTHnlaqaarisDRAALFFDGRL 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1512845752 213 IELTPTAlrsyggnyDEYQRQRMAEQQAARAALEHAVTDRRR 254
Cdd:PRK14271  241 VEEGPTE--------QLFSSPKHAETARYVAGLSGDVKDAKR 274
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
457-513 2.30e-03

ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 40.53  E-value: 2.30e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1512845752 457 LSGGERLKAALACVLWRRepAQLLLLDEPTNHLDLASTQAIESALAAFPG--AMLVVSH 513
Cdd:COG1132   477 LSGGQRQRIAIARALLKD--PPILILDEATSALDTETEALIQEALERLMKgrTTIVIAH 533
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
455-519 2.41e-03

cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 40.60  E-value: 2.41e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1512845752 455 SALSGGERLKAALACVLWRrePAQLLLLDEPTNHLDLASTQAIESAL--AAFPGAMLVVSHDEAFLQ 519
Cdd:PRK11174  484 AGLSVGQAQRLALARALLQ--PCQLLLLDEPTASLDAHSEQLVMQALnaASRRQTTLMVTHQLEDLA 548
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
11-208 2.45e-03

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 40.06  E-value: 2.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  11 VLHQVTCQFATGQTLfgplsvslepslcGLVGRNGVGKTRLLRLLAGLDSPAGGHIERAAavawvaqqptlTPETTLAT- 89
Cdd:PRK10419   27 VLNNVSLSLKSGETV-------------ALLGRSGCGKSTLARLLVGLESPSQGNVSWRG-----------EPLAKLNRa 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  90 ----------LLGYASVFAALSRLEQGQGLADDFDLLDGhWDLTDRLSLA---FREADLPPFSADRPAFSLSGGERMKAL 156
Cdd:PRK10419   83 qrkafrrdiqMVFQDSISAVNPRKTVREIIREPLRHLLS-LDKAERLARAsemLRAVDLDDSVLDKRPPQLSGGQLQRVC 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1512845752 157 LCGAFVSGADYLLLDEPTNHLDRQGREWLYHQLESWQ---GGA-LIASHDRELLTR 208
Cdd:PRK10419  162 LARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQqqfGTAcLFITHDLRLVER 217
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
134-202 2.54e-03

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 40.07  E-value: 2.54e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1512845752 134 DLPPFSADRPAFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQG-REWL--YHQLESWQGGALIASHD 202
Cdd:PRK13651  153 GLDESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGvKEILeiFDNLNKQGKTIILVTHD 224
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
39-213 2.55e-03

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: 39.09  E-value: 2.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  39 GLVGRNGVGKTRLLRLLAGLDSPAGGHIEraaavawvaqqptltpettlatllgyasvfaalsrleqgqgladdfdlldg 118
Cdd:cd03222    29 GIVGPNGTGKTTAVKILAGQLIPNGDNDE--------------------------------------------------- 57
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 119 hWDltdRLSLAFReadlPPFsadrpaFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGR----EWLYHQLESWQG 194
Cdd:cd03222    58 -WD---GITPVYK----PQY------IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRlnaaRAIRRLSEEGKK 123
                         170
                  ....*....|....*....
gi 1512845752 195 GALIASHDRELLTRMPRII 213
Cdd:cd03222   124 TALVVEHDLAVLDYLSDRI 142
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
455-514 2.71e-03

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 39.41  E-value: 2.71e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1512845752 455 SALSGGERLKAALACVLwRREPAqLLLLDEPTNHLDLASTQAIESALAAFP----GAMLVVSHD 514
Cdd:PRK11629  144 SELSGGERQRVAIARAL-VNNPR-LVLADEPTGNLDARNADSIFQLLGELNrlqgTAFLVVTHD 205
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
440-495 2.86e-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: 40.19  E-value: 2.86e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1512845752 440 LAQLQLGADKVTLPLSALSGGERLKAALACVLWRRepAQLLLLDEPTNHLDLASTQ 495
Cdd:TIGR02633 125 LRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQ--ARLLILDEPSSSLTEKETE 178
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
114-219 3.06e-03

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 40.58  E-value: 3.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752  114 DLLDGhwdLTDRLSLAFrEADLPPFSADRPAFSLSGGERMKALLC---GAFVSGADYlLLDEPTNHLDRQGREWLYHQLE 190
Cdd:PRK00635   448 EVLQG---LKSRLSILI-DLGLPYLTPERALATLSGGEQERTALAkhlGAELIGITY-ILDEPSIGLHPQDTHKLINVIK 522
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1512845752  191 SW--QGGA-LIASHDRELLTRMPRIIELTPTA 219
Cdd:PRK00635   523 KLrdQGNTvLLVEHDEQMISLADRIIDIGPGA 554
ABC_tran_Xtn pfam12848
ABC transporter; This domain is an extension of some members of pfam00005 and other ...
220-269 3.54e-03

ABC transporter; This domain is an extension of some members of pfam00005 and other ABC-transporter families.


Pssm-ID: 463731 [Multi-domain]  Cd Length: 85  Bit Score: 36.78  E-value: 3.54e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 220 LRSYGGNYDEYQRQRMAE----------QQAARAALEHAVtDRRRTRARMQKehdAAQRR 269
Cdd:pfam12848   8 LTTYKGNYSTFLEQKEERleqqekayekQQKEIKKLEEFI-DRFRAKASKAK---QAQSR 63
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
374-516 4.11e-03

ABC-type multidrug transport system, ATPase component [Defense mechanisms];


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 38.89  E-value: 4.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 374 GPNGCG-----------KttllktllgleQAASGDVRL--------SVSA----AYLDQHLTqLDLSLSVMAHLSL--ED 428
Cdd:COG1131    33 GPNGAGktttirmllglL-----------RPTSGEVRVlgedvardPAEVrrriGYVPQEPA-LYPDLTVRENLRFfaRL 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 429 TPLDEGLLRTRLAQL--QLG-ADKVTLPLSALSGGERLKAALACVLWRRepAQLLLLDEPTNHLDLASTQAIES---ALA 502
Cdd:COG1131   101 YGLPRKEARERIDELleLFGlTDAADRKVGTLSGGMKQRLGLALALLHD--PELLILDEPTSGLDPEARRELWEllrELA 178
                         170
                  ....*....|....*.
gi 1512845752 503 AFPGAMLVVSH--DEA 516
Cdd:COG1131   179 AEGKTVLLSTHylEEA 194
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
453-515 4.27e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.05  E-value: 4.27e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1512845752 453 PLSALSGGER----LKAALACVLWRREPAQLLLLDEPTNHLD------LasTQAIESALAAFPgAMLVVSHDE 515
Cdd:PRK03918  785 PLTFLSGGERialgLAFRLALSLYLAGNIPLLILDEPTPFLDeerrrkL--VDIMERYLRKIP-QVIIVSHDE 854
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
453-497 4.52e-03

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: 38.89  E-value: 4.52e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1512845752 453 PLSALSGGERLKAALACVLWRREPaqLLLLDEPTNHLDLASTQAI 497
Cdd:cd03266   133 RVGGFSTGMRQKVAIARALVHDPP--VLLLDEPTTGLDVMATRAL 175
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
457-529 5.88e-03

ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213266 [Multi-domain]  Cd Length: 235  Bit Score: 38.47  E-value: 5.88e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1512845752 457 LSGGERLKAALACVLwRREPaQLLLLDEPTNHLDLASTQAIESalaafpgaMLVVSHDEAFLQGLKLTHSL--AW 529
Cdd:cd03299   130 LSGGEQQRVAIARAL-VVNP-KILLLDEPFSALDVRTKEKLRE--------ELKKIRKEFGVTVLHVTHDFeeAW 194
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
142-215 6.23e-03

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 39.32  E-value: 6.23e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1512845752 142 RPAfSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGRE---WLYHQLESWQGGALIASHDRELLTRMPRIIEL 215
Cdd:PRK10535  141 QPS-QLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEevmAILHQLRDRGHTVIIVTHDPQVAAQAERVIEI 216
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
360-514 7.05e-03

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: 38.16  E-value: 7.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 360 LNWRIDGPMRIALKGPNGCGKTTLLKTLLGLEQAASGDVRLSVSA---------AYLDQHL------TQLDLSLSVMAH- 423
Cdd:cd03292    20 INISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDvsdlrgraiPYLRRKIgvvfqdFRLLPDRNVYENv 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 424 -LSLEDTPLDEGLLRTR----LAQLQLGADKVTLPlSALSGGERLKAALACVLWRREPaqLLLLDEPTNHLDLASTQAIE 498
Cdd:cd03292   100 aFALEVTGVPPREIRKRvpaaLELVGLSHKHRALP-AELSGGEQQRVAIARAIVNSPT--ILIADEPTGNLDPDTTWEIM 176
                         170
                  ....*....|....*....
gi 1512845752 499 SALAAF--PGAMLVVS-HD 514
Cdd:cd03292   177 NLLKKInkAGTTVVVAtHA 195
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
12-67 8.55e-03

ABC-type uncharacterized transport system, ATPase component [General function prediction only];


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 38.17  E-value: 8.55e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1512845752  12 LHQVTCQFATGQTLFGpLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIE 67
Cdd:COG4152     4 LKGLTKRFGDKTAVDD-VSFTVPKgEIFGLLGPNGAGKTTTIRIILGILAPDSGEVL 59
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
371-490 8.73e-03

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 38.66  E-value: 8.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 371 ALKGPNGCGKTTLLKTLLGLEQAASGDVRLS-VSAAYLDQHLTQLDL---SLSVMAHLSLEDTpLDEGLLRTRLAQLQLg 446
Cdd:PRK11607   49 ALLGASGCGKSTLLRMLAGFEQPTAGQIMLDgVDLSHVPPYQRPINMmfqSYALFPHMTVEQN-IAFGLKQDKLPKAEI- 126
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1512845752 447 ADKVTLPLS-------------ALSGGERLKAALACVLWRRepAQLLLLDEPTNHLD 490
Cdd:PRK11607  127 ASRVNEMLGlvhmqefakrkphQLSGGQRQRVALARSLAKR--PKLLLLDEPMGALD 181
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
371-514 9.62e-03

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: 37.91  E-value: 9.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 371 ALKGPNGCGKTTLLKTLLGLEQAASGDVRLS--VSAAYLDQHLTQ---------LDLSLSVMAHL----SLEDTPLDEGL 435
Cdd:COG4555    31 GLLGPNGAGKTTLLRMLAGLLKPDSGSILIDgeDVRKEPREARRQigvlpdergLYDRLTVRENIryfaELYGLFDEELK 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 436 LRT----RLAQLQLGADKvtlPLSALSGGERLKAALACVLWRRepAQLLLLDEPTNHLDLASTQAIESALAAF---PGAM 508
Cdd:COG4555   111 KRIeeliELLGLEEFLDR---RVGELSTGMKKKVALARALVHD--PKVLLLDEPTNGLDVMARRLLREILRALkkeGKTV 185

                  ....*.
gi 1512845752 509 LVVSHD 514
Cdd:COG4555   186 LFSSHI 191
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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