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Conserved domains on  [gi|15830287|ref|NP_309060|]
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replication regulatory ABC-F family DNA-binding ATPase [Escherichia coli O157:H7 str. Sakai]

Protein Classification

ABC transporter ATP-binding protein( domain architecture ID 11485229)

ABC transporter ATP-binding protein is the ATPase catalytic subunit of an ATP transporter complex responsible for coupling the energy of ATP hydrolysis to the import of one or more from a variety of substrates; similar to Escherichia coli ABC transporter ATP-binding protein uup

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
1-635 0e+00

ABC transporter ATPase component; Reviewed


:

Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 1328.43  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287    1 MSLISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLIVARLQQDPPRNVE 80
Cdd:PRK11147   1 MSLISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQDPPRNVE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   81 GSVYDFVAEGIEEQAEYLKRYHDISRLVMNDPSEKNLNELAKVQEQLDHHNLWQLENRINEVLAQLGLDPNVALSSLSGG 160
Cdd:PRK11147  81 GTVYDFVAEGIEEQAEYLKRYHDISHLVETDPSEKNLNELAKLQEQLDHHNLWQLENRINEVLAQLGLDPDAALSSLSGG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  161 WLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKLVTYPGNYDQ 240
Cdd:PRK11147 161 WLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGNYDQ 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  241 YLLEKEEALRVEELQNAEFDRKLAQEEVWIRQGIKARRTRNEGRVRALKAMRRERGERREVMGTAKMQVEEASRSGKIVF 320
Cdd:PRK11147 241 YLLEKEEALRVEELQNAEFDRKLAQEEVWIRQGIKARRTRNEGRVRALKALRRERSERREVMGTAKMQVEEASRSGKIVF 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  321 EMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKLEVAYFDQHRAELDPDKTV 400
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFDQHRAELDPEKTV 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  401 MDNLAEGKQEVMVNGKPRHVLGYLQDFLFHPKRAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLE 480
Cdd:PRK11147 401 MDNLAEGKQEVMVNGRPRHVLGYLQDFLFHPKRAMTPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLE 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  481 ELIDSYQGTVLLVSHDRQFVDNTVTECWIFEGGGKIGRYVGGYHDARGQQEQYVALKQPAVKKNEEPAAPKAETVKRSSS 560
Cdd:PRK11147 481 ELLDSYQGTVLLVSHDRQFVDNTVTECWIFEGNGKIGRYVGGYHDARQQQAQYLALKQPAVKKKEEAAAPKAETVKRSSK 560
                        570       580       590       600       610       620       630
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15830287  561 KLSYKLQRELEQLPQLLEDLEAKLEALQTQVADASFFSQPHEQTQKVLADMAAAEQELEQAFERWEYLEALKNGG 635
Cdd:PRK11147 561 KLSYKLQRELEQLPQLLEDLEAEIEALQAQVADADFFSQPHEQTQKVLADLADAEQELEVAFERWEELEALKNGG 635
 
Name Accession Description Interval E-value
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
1-635 0e+00

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 1328.43  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287    1 MSLISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLIVARLQQDPPRNVE 80
Cdd:PRK11147   1 MSLISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQDPPRNVE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   81 GSVYDFVAEGIEEQAEYLKRYHDISRLVMNDPSEKNLNELAKVQEQLDHHNLWQLENRINEVLAQLGLDPNVALSSLSGG 160
Cdd:PRK11147  81 GTVYDFVAEGIEEQAEYLKRYHDISHLVETDPSEKNLNELAKLQEQLDHHNLWQLENRINEVLAQLGLDPDAALSSLSGG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  161 WLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKLVTYPGNYDQ 240
Cdd:PRK11147 161 WLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGNYDQ 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  241 YLLEKEEALRVEELQNAEFDRKLAQEEVWIRQGIKARRTRNEGRVRALKAMRRERGERREVMGTAKMQVEEASRSGKIVF 320
Cdd:PRK11147 241 YLLEKEEALRVEELQNAEFDRKLAQEEVWIRQGIKARRTRNEGRVRALKALRRERSERREVMGTAKMQVEEASRSGKIVF 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  321 EMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKLEVAYFDQHRAELDPDKTV 400
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFDQHRAELDPEKTV 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  401 MDNLAEGKQEVMVNGKPRHVLGYLQDFLFHPKRAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLE 480
Cdd:PRK11147 401 MDNLAEGKQEVMVNGRPRHVLGYLQDFLFHPKRAMTPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLE 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  481 ELIDSYQGTVLLVSHDRQFVDNTVTECWIFEGGGKIGRYVGGYHDARGQQEQYVALKQPAVKKNEEPAAPKAETVKRSSS 560
Cdd:PRK11147 481 ELLDSYQGTVLLVSHDRQFVDNTVTECWIFEGNGKIGRYVGGYHDARQQQAQYLALKQPAVKKKEEAAAPKAETVKRSSK 560
                        570       580       590       600       610       620       630
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15830287  561 KLSYKLQRELEQLPQLLEDLEAKLEALQTQVADASFFSQPHEQTQKVLADMAAAEQELEQAFERWEYLEALKNGG 635
Cdd:PRK11147 561 KLSYKLQRELEQLPQLLEDLEAEIEALQAQVADADFFSQPHEQTQKVLADLADAEQELEVAFERWEELEALKNGG 635
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
6-525 0e+00

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 669.08  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   6 MHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLIVARLQQDPPRNVEGSVYD 85
Cdd:COG0488   1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPLDDDLTVLD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  86 FVAEGIEEQAEYLKRYHDISRLvMNDPSEkNLNELAKVQEQLDHHNLWQLENRINEVLAQLGL---DPNVALSSLSGGWL 162
Cdd:COG0488  81 TVLDGDAELRALEAELEELEAK-LAEPDE-DLERLAELQEEFEALGGWEAEARAEEILSGLGFpeeDLDRPVSELSGGWR 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 163 RKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKLVTYPGNYDQYL 242
Cdd:COG0488 159 RRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAYL 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 243 LEKEEALRVEELQNAEFDRKLAQEEVWIRQ-GIKARR-TRNEGRVRALKAMRRERGERREvmGTAKMQVEEASRSGKIVF 320
Cdd:COG0488 239 EQRAERLEQEAAAYAKQQKKIAKEEEFIRRfRAKARKaKQAQSRIKALEKLEREEPPRRD--KTVEIRFPPPERLGKKVL 316
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 321 EMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKLEVAYFDQHRAELDPDKTV 400
Cdd:COG0488 317 ELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQEELDPDKTV 396
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 401 MDNLAEGKQevmvNGKPRHVLGYLQDFLFHPKRAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLE 480
Cdd:COG0488 397 LDELRDGAP----GGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALE 472
                       490       500       510       520
                ....*....|....*....|....*....|....*....|....*
gi 15830287 481 ELIDSYQGTVLLVSHDRQFVDNTVTECWIFEGGGkIGRYVGGYHD 525
Cdd:COG0488 473 EALDDFPGTVLLVSHDRYFLDRVATRILEFEDGG-VREYPGGYDD 516
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
34-525 1.08e-126

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: 385.06  E-value: 1.08e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287    34 LVGRNGAGKSTLMKILnreQGLD---DGRIIYEQDLIVARLQQDPPRNVEGSVYDFVAEGIEEQAEYLKRYHDISRLvMN 110
Cdd:TIGR03719  36 VLGLNGAGKSTLLRIM---AGVDkdfNGEARPQPGIKVGYLPQEPQLDPTKTVRENVEEGVAEIKDALDRFNEISAK-YA 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   111 DPS---EKNLNELAKVQEQLDHHNLWQLENRINEVLAQLGLDPNVA-LSSLSGGWLRKAALGRALVSNPRVLLLDEPTNH 186
Cdd:TIGR03719 112 EPDadfDKLAAEQAELQEIIDAADAWDLDSQLEIAMDALRCPPWDAdVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNH 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   187 LDIETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKLVTYPGNYDQYLLEKEEALRVEELQNAEFDRKLAQE 266
Cdd:TIGR03719 192 LDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWLEQKQKRLEQEEKEESARQKTLKRE 271
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   267 EVWIRQGIKARRTRNEGRVRALKAMRRERGERREvmGTAKMQVEEASRSGKIVFEMEDVCYQVDGKQLVKDFSAQVLRGD 346
Cdd:TIGR03719 272 LEWVRQSPKGRQAKSKARLARYEELLSQEFQKRN--ETAEIYIPPGPRLGDKVIEAENLTKAFGDKLLIDDLSFKLPPGG 349
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   347 KIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKLEVAYFDQHRAELDPDKTVMDNLAEGKQEVMVNGKPRHVLGYLQD 426
Cdd:TIGR03719 350 IVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQSRDALDPNKTVWEEISGGLDIIKLGKREIPSRAYVGR 429
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   427 FLFHPKRAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELIDSYQGTVLLVSHDRQFVDNTVTE 506
Cdd:TIGR03719 430 FNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIATH 509
                         490
                  ....*....|....*....
gi 15830287   507 CWIFEGGGKIGRYVGGYHD 525
Cdd:TIGR03719 510 ILAFEGDSHVEWFEGNFSE 528
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
321-514 3.48e-51

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: 173.40  E-value: 3.48e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 321 EMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKLEVAYFDQhraeldpdktv 400
Cdd:cd03221   2 ELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ----------- 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 401 mdnlaegkqevmvngkprhvlgylqdflfhpkramtpvraLSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLE 480
Cdd:cd03221  71 ----------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALE 110
                       170       180       190
                ....*....|....*....|....*....|....
gi 15830287 481 ELIDSYQGTVLLVSHDRQFVDNTVTECWIFEGGG 514
Cdd:cd03221 111 EALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
335-469 1.53e-29

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: 114.28  E-value: 1.53e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   335 VKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVG-----------TKLEVAYFDQHrAELDPDKTVMDN 403
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDgqdltdderksLRKEIGYVFQD-PQLFPRLTVREN 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15830287   404 LAEGKQEVMVNGKPR-----HVLGYLQDFLFHPKRAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTN 469
Cdd:pfam00005  80 LRLGLLLKGLSKREKdaraeEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
330-496 1.06e-19

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 87.29  E-value: 1.06e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  330 DGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKLEVAYFDQHRAelDPDK---TVMDNLAE 406
Cdd:NF040873   3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSE--VPDSlplTVRDLVAM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  407 GK-QEVMVNGKPRHV-----------LGyLQDFLfhpKRamtPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVE 474
Cdd:NF040873  81 GRwARRGLWRRLTRDdraavddalerVG-LADLA---GR---QLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAE 153
                        170       180
                 ....*....|....*....|....*
gi 15830287  475 TLELLEELIDSYQG---TVLLVSHD 496
Cdd:NF040873 154 SRERIIALLAEEHArgaTVVVVTHD 178
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
12-226 1.01e-13

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 69.96  E-value: 1.01e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   12 SFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLIVARLQQ--DPPRNVEGSVYDFVAE 89
Cdd:NF040873   1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQrsEVPDSLPLTVRDLVAM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   90 GIEEQAEYLKRYHDISRLVmndpseknlnelakVQEQLDHHNLWQLENRinevlaqlgldpnvALSSLSGGWLRKAALGR 169
Cdd:NF040873  81 GRWARRGLWRRLTRDDRAA--------------VDDALERVGLADLAGR--------------QLGELSGGQRQRALLAQ 132
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  170 ALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFNG---TIIFISHDRSFIRNmATRIVDL 226
Cdd:NF040873 133 GLAQEADLLLLDEPTTGLDAESRERIIALLAEEHArgaTVVVVTHDLELVRR-ADPCVLL 191
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
344-503 1.01e-10

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 60.08  E-value: 1.01e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287    344 RGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVgtklevayfdqhraeLDPDKTVMDNLAEGKQEVMVNGKprhvlgy 423
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY---------------IDGEDILEEVLDQLLLIIVGGKK------- 58
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287    424 lqdflfhpkramtpvRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELIDSYQGTVLLVSHDRQFVDNT 503
Cdd:smart00382  59 ---------------ASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLTVILTT 123
GguA NF040905
sugar ABC transporter ATP-binding protein;
19-63 5.53e-05

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 45.94  E-value: 5.53e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 15830287   19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILN--REQGLDDGRIIYE 63
Cdd:NF040905  17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSgvYPHGSYEGEILFD 63
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
138-261 6.90e-04

oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 42.41  E-value: 6.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  138 RINEVLAQLGLDPNV--ALSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETID--WLEGFLKTFNG-TIIFISHD 212
Cdd:NF000106 124 RADELLERFSLTEAAgrAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNevWDEVRSMVRDGaTVLLTTQY 203
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 15830287  213 RSFIRNMATRIVDLDRGKLVTyPGNYDQYLLE-KEEALRVEELQNAEFDR 261
Cdd:NF000106 204 MEEAEQLAHELTVIDRGRVIA-DGKVDELKTKvGGRTLQIRPAHAAELDR 252
 
Name Accession Description Interval E-value
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
1-635 0e+00

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 1328.43  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287    1 MSLISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLIVARLQQDPPRNVE 80
Cdd:PRK11147   1 MSLISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQDPPRNVE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   81 GSVYDFVAEGIEEQAEYLKRYHDISRLVMNDPSEKNLNELAKVQEQLDHHNLWQLENRINEVLAQLGLDPNVALSSLSGG 160
Cdd:PRK11147  81 GTVYDFVAEGIEEQAEYLKRYHDISHLVETDPSEKNLNELAKLQEQLDHHNLWQLENRINEVLAQLGLDPDAALSSLSGG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  161 WLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKLVTYPGNYDQ 240
Cdd:PRK11147 161 WLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGNYDQ 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  241 YLLEKEEALRVEELQNAEFDRKLAQEEVWIRQGIKARRTRNEGRVRALKAMRRERGERREVMGTAKMQVEEASRSGKIVF 320
Cdd:PRK11147 241 YLLEKEEALRVEELQNAEFDRKLAQEEVWIRQGIKARRTRNEGRVRALKALRRERSERREVMGTAKMQVEEASRSGKIVF 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  321 EMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKLEVAYFDQHRAELDPDKTV 400
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFDQHRAELDPEKTV 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  401 MDNLAEGKQEVMVNGKPRHVLGYLQDFLFHPKRAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLE 480
Cdd:PRK11147 401 MDNLAEGKQEVMVNGRPRHVLGYLQDFLFHPKRAMTPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLE 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  481 ELIDSYQGTVLLVSHDRQFVDNTVTECWIFEGGGKIGRYVGGYHDARGQQEQYVALKQPAVKKNEEPAAPKAETVKRSSS 560
Cdd:PRK11147 481 ELLDSYQGTVLLVSHDRQFVDNTVTECWIFEGNGKIGRYVGGYHDARQQQAQYLALKQPAVKKKEEAAAPKAETVKRSSK 560
                        570       580       590       600       610       620       630
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15830287  561 KLSYKLQRELEQLPQLLEDLEAKLEALQTQVADASFFSQPHEQTQKVLADMAAAEQELEQAFERWEYLEALKNGG 635
Cdd:PRK11147 561 KLSYKLQRELEQLPQLLEDLEAEIEALQAQVADADFFSQPHEQTQKVLADLADAEQELEVAFERWEELEALKNGG 635
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
6-525 0e+00

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 669.08  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   6 MHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLIVARLQQDPPRNVEGSVYD 85
Cdd:COG0488   1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPLDDDLTVLD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  86 FVAEGIEEQAEYLKRYHDISRLvMNDPSEkNLNELAKVQEQLDHHNLWQLENRINEVLAQLGL---DPNVALSSLSGGWL 162
Cdd:COG0488  81 TVLDGDAELRALEAELEELEAK-LAEPDE-DLERLAELQEEFEALGGWEAEARAEEILSGLGFpeeDLDRPVSELSGGWR 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 163 RKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKLVTYPGNYDQYL 242
Cdd:COG0488 159 RRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAYL 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 243 LEKEEALRVEELQNAEFDRKLAQEEVWIRQ-GIKARR-TRNEGRVRALKAMRRERGERREvmGTAKMQVEEASRSGKIVF 320
Cdd:COG0488 239 EQRAERLEQEAAAYAKQQKKIAKEEEFIRRfRAKARKaKQAQSRIKALEKLEREEPPRRD--KTVEIRFPPPERLGKKVL 316
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 321 EMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKLEVAYFDQHRAELDPDKTV 400
Cdd:COG0488 317 ELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQEELDPDKTV 396
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 401 MDNLAEGKQevmvNGKPRHVLGYLQDFLFHPKRAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLE 480
Cdd:COG0488 397 LDELRDGAP----GGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALE 472
                       490       500       510       520
                ....*....|....*....|....*....|....*....|....*
gi 15830287 481 ELIDSYQGTVLLVSHDRQFVDNTVTECWIFEGGGkIGRYVGGYHD 525
Cdd:COG0488 473 EALDDFPGTVLLVSHDRYFLDRVATRILEFEDGG-VREYPGGYDD 516
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
34-525 1.08e-126

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: 385.06  E-value: 1.08e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287    34 LVGRNGAGKSTLMKILnreQGLD---DGRIIYEQDLIVARLQQDPPRNVEGSVYDFVAEGIEEQAEYLKRYHDISRLvMN 110
Cdd:TIGR03719  36 VLGLNGAGKSTLLRIM---AGVDkdfNGEARPQPGIKVGYLPQEPQLDPTKTVRENVEEGVAEIKDALDRFNEISAK-YA 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   111 DPS---EKNLNELAKVQEQLDHHNLWQLENRINEVLAQLGLDPNVA-LSSLSGGWLRKAALGRALVSNPRVLLLDEPTNH 186
Cdd:TIGR03719 112 EPDadfDKLAAEQAELQEIIDAADAWDLDSQLEIAMDALRCPPWDAdVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNH 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   187 LDIETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKLVTYPGNYDQYLLEKEEALRVEELQNAEFDRKLAQE 266
Cdd:TIGR03719 192 LDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWLEQKQKRLEQEEKEESARQKTLKRE 271
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   267 EVWIRQGIKARRTRNEGRVRALKAMRRERGERREvmGTAKMQVEEASRSGKIVFEMEDVCYQVDGKQLVKDFSAQVLRGD 346
Cdd:TIGR03719 272 LEWVRQSPKGRQAKSKARLARYEELLSQEFQKRN--ETAEIYIPPGPRLGDKVIEAENLTKAFGDKLLIDDLSFKLPPGG 349
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   347 KIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKLEVAYFDQHRAELDPDKTVMDNLAEGKQEVMVNGKPRHVLGYLQD 426
Cdd:TIGR03719 350 IVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQSRDALDPNKTVWEEISGGLDIIKLGKREIPSRAYVGR 429
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   427 FLFHPKRAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELIDSYQGTVLLVSHDRQFVDNTVTE 506
Cdd:TIGR03719 430 FNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIATH 509
                         490
                  ....*....|....*....
gi 15830287   507 CWIFEGGGKIGRYVGGYHD 525
Cdd:TIGR03719 510 ILAFEGDSHVEWFEGNFSE 528
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
34-525 4.83e-122

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 372.91  E-value: 4.83e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   34 LVGRNGAGKSTLMKILnreQGLD---DGRIIYEQDLIVARLQQDPPRNVEGSVYDFVAEGIEEQAEYLKRYHDISRLvMN 110
Cdd:PRK11819  38 VLGLNGAGKSTLLRIM---AGVDkefEGEARPAPGIKVGYLPQEPQLDPEKTVRENVEEGVAEVKAALDRFNEIYAA-YA 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  111 DP---SEKNLNELAKVQEQLDHHNLWQLENRINEVLAQLGLDPNVA-LSSLSGGWLRKAALGRALVSNPRVLLLDEPTNH 186
Cdd:PRK11819 114 EPdadFDALAAEQGELQEIIDAADAWDLDSQLEIAMDALRCPPWDAkVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNH 193
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  187 LDIETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKLVTYPGNYDQYLLEKEEALRVEELQNAEFDRKLAQE 266
Cdd:PRK11819 194 LDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWLEQKAKRLAQEEKQEAARQKALKRE 273
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  267 EVWIRQGIKARRTRNEGRVRALKAMRRERGERREvmGTAKMQVEEASRSGKIVFEMEDVCYQVDGKQLVKDFSAQVLRGD 346
Cdd:PRK11819 274 LEWVRQSPKARQAKSKARLARYEELLSEEYQKRN--ETNEIFIPPGPRLGDKVIEAENLSKSFGDRLLIDDLSFSLPPGG 351
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  347 KIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKLEVAYFDQHRAELDPDKTVMDNLAEGKQEVMVNGKPRHVLGYLQD 426
Cdd:PRK11819 352 IVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYVDQSRDALDPNKTVWEEISGGLDIIKVGNREIPSRAYVGR 431
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  427 FLFHPKRAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELIDSYQGTVLLVSHDRQFVDNTVTE 506
Cdd:PRK11819 432 FNFKGGDQQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRIATH 511
                        490
                 ....*....|....*....
gi 15830287  507 CWIFEGGGKIGRYVGGYHD 525
Cdd:PRK11819 512 ILAFEGDSQVEWFEGNFQE 530
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
13-525 2.46e-84

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 274.08  E-value: 2.46e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   13 FSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLIVARLQQDPPRNVEGSVYDFVAEGIE 92
Cdd:PRK15064  11 FGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKLRQDQFAFEEFTVLDTVIMGHT 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   93 EQAEyLKRYHDisRLVMN-DPSEKNLNELAKVQEQLDHHNLWQLENRINEVLAQLGLDP---NVALSSLSGGWLRKAALG 168
Cdd:PRK15064  91 ELWE-VKQERD--RIYALpEMSEEDGMKVADLEVKFAEMDGYTAEARAGELLLGVGIPEeqhYGLMSEVAPGWKLRVLLA 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  169 RALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKLVTYPGNYDQYLlekEEA 248
Cdd:PRK15064 168 QALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELRVYPGNYDEYM---TAA 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  249 LRVEELQNAEFDRKLAQ-EEVwirQGIKARRTRNEGRVRA----LKAMRrergerrevmgtaKMQVEE---ASR-SGKIV 319
Cdd:PRK15064 245 TQARERLLADNAKKKAQiAEL---QSFVSRFSANASKAKQatsrAKQID-------------KIKLEEvkpSSRqNPFIR 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  320 FEM-----------EDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKLEVAYFD 388
Cdd:PRK15064 309 FEQdkklhrnalevENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYA 388
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  389 Q-HRAELDPDKTVMDNLAEGKQ----EVMVngkpRHVLGYLqdfLFHPKRAMTPVRALSGGERNRLLLARLFLKPSNLLI 463
Cdd:PRK15064 389 QdHAYDFENDLTLFDWMSQWRQegddEQAV----RGTLGRL---LFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLV 461
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15830287  464 LDEPTNDLDVETLELLEELIDSYQGTVLLVSHDRQFVDNTVTEcwIFE-GGGKIGRYVGGYHD 525
Cdd:PRK15064 462 MDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATR--IIEiTPDGVVDFSGTYEE 522
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
18-631 9.81e-68

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 232.75  E-value: 9.81e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   18 LLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLIVARLQQDPPRnVEGSVYDFVAEGIEEQAEY 97
Cdd:PRK10636  16 LLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETPA-LPQPALEYVIDGDREYRQL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   98 LKRyhdisrlvMNDPSEKNL-NELAKVQEQLDHHNLWQLENRINEVLAQLGLDPNV---ALSSLSGGWLRKAALGRALVS 173
Cdd:PRK10636  95 EAQ--------LHDANERNDgHAIATIHGKLDAIDAWTIRSRAASLLHGLGFSNEQlerPVSDFSGGWRMRLNLAQALIC 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  174 NPRVLLLDEPTNHLDIETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKLVTYPGNYDQYllEKEEALRVEE 253
Cdd:PRK10636 167 RSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSSF--EVQRATRLAQ 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  254 lQNAEFD---RKLAQEEVWI-RQGIKARRTRN-EGRVRALKAMRRERGERreVMGTAKMQVEEASRSGKIVFEMEDVCYQ 328
Cdd:PRK10636 245 -QQAMYEsqqERVAHLQSYIdRFRAKATKAKQaQSRIKMLERMELIAPAH--VDNPFHFSFRAPESLPNPLLKMEKVSAG 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  329 VDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKLEVAYFDQHRAE-LDPDKTVMDNLAEG 407
Cdd:PRK10636 322 YGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQLEfLRADESPLQHLARL 401
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  408 KQEVMvngkPRHVLGYLQDFLFHPKRAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELIDSYQ 487
Cdd:PRK10636 402 APQEL----EQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFE 477
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  488 GTVLLVSHDRQFVDNTVTECWIFEgGGKIGRYVGGYHDAR----GQQEQYVALKQPAVKKNEEPAAPKAETVKRSSS--K 561
Cdd:PRK10636 478 GALVVVSHDRHLLRSTTDDLYLVH-DGKVEPFDGDLEDYQqwlsDVQKQENQTDEAPKENNANSAQARKDQKRREAElrT 556
                        570       580       590       600       610       620       630
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15830287  562 LSYKLQRELEQLPQLLEDLEAKLEALQTQVADASFFSQPHEQT-QKVLADMAAAEQELEQAFERW----EYLEAL 631
Cdd:PRK10636 557 QTQPLRKEIARLEKEMEKLNAQLAQAEEKLGDSELYDQSRKAElTACLQQQASAKSGLEECEMAWleaqEQLEQM 631
PLN03073 PLN03073
ABC transporter F family; Provisional
4-525 5.72e-55

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 199.32  E-value: 5.72e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287    4 ISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMK---------------ILNREQGLDDGRIIYEQDLIV 68
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRymamhaidgipkncqILHVEQEVVGDDTTALQCVLN 257
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   69 ARLQQDPPRNVEGSVYDFVAEgIEEQAEYLKRYHDISRLVMNDPSEKNLNELAKVQEQLDHHNLwqlENRINEVLAQLGL 148
Cdd:PLN03073 258 TDIERTQLLEEEAQLVAQQRE-LEFETETGKGKGANKDGVDKDAVSQRLEEIYKRLELIDAYTA---EARAASILAGLSF 333
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  149 DPNV---ALSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVD 225
Cdd:PLN03073 334 TPEMqvkATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILH 413
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  226 LDRGKLVTYPGNYDQYLLEKEEALRVEELQNAEFDRKLAQEEVWI---RQGIKaRRTRNEGRVRALKAMrrerGERREVM 302
Cdd:PLN03073 414 LHGQKLVTYKGDYDTFERTREEQLKNQQKAFESNERSRSHMQAFIdkfRYNAK-RASLVQSRIKALDRL----GHVDAVV 488
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  303 GTAKMQVEEAS---RSGKIVFEMEDVCYQVDGKQLV-KDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV 378
Cdd:PLN03073 489 NDPDYKFEFPTpddRPGPPIISFSDASFGYPGGPLLfKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFR 568
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  379 GTKLEVAYFDQHRAE-LDPDKTVMDNLAEgkqevMVNGKPRHVL-GYLQDFLFHPKRAMTPVRALSGGERNRLLLARLFL 456
Cdd:PLN03073 569 SAKVRMAVFSQHHVDgLDLSSNPLLYMMR-----CFPGVPEQKLrAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITF 643
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15830287  457 KPSNLLILDEPTNDLDVETLELLEELIDSYQGTVLLVSHDRQFVDNTVTECWIFEgGGKIGRYVGGYHD 525
Cdd:PLN03073 644 KKPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVS-EGKVTPFHGTFHD 711
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
321-514 3.48e-51

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: 173.40  E-value: 3.48e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 321 EMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKLEVAYFDQhraeldpdktv 400
Cdd:cd03221   2 ELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ----------- 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 401 mdnlaegkqevmvngkprhvlgylqdflfhpkramtpvraLSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLE 480
Cdd:cd03221  71 ----------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALE 110
                       170       180       190
                ....*....|....*....|....*....|....
gi 15830287 481 ELIDSYQGTVLLVSHDRQFVDNTVTECWIFEGGG 514
Cdd:cd03221 111 EALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
3-242 3.21e-46

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 171.02  E-value: 3.21e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   3 LISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLIVARLQQDpprnvegs 82
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQH-------- 386
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  83 vydfvaegieeqAEYLkryhdisrlvmnDPSEKNLNELAKVQEQLDHHNLWQLenrinevLAQLGLDPNVAL---SSLSG 159
Cdd:COG0488 387 ------------QEEL------------DPDKTVLDELRDGAPGGTEQEVRGY-------LGRFLFSGDDAFkpvGVLSG 435
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 160 GWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKLVTYPGNYD 239
Cdd:COG0488 436 GEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREYPGGYD 515

                ...
gi 15830287 240 QYL 242
Cdd:COG0488 516 DYL 518
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
4-230 1.04e-44

ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.


Pssm-ID: 213188 [Multi-domain]  Cd Length: 144  Bit Score: 156.07  E-value: 1.04e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   4 ISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLIVARLQQdpprnvegsv 83
Cdd:cd03221   1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ---------- 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  84 ydfvaegieeqaeylkryhdisrlvmndpseknlnelakvqeqldhhnlwqlenrinevlaqlgldpnvalssLSGGWLR 163
Cdd:cd03221  71 -------------------------------------------------------------------------LSGGEKM 77
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15830287 164 KAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGK 230
Cdd:cd03221  78 RLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
11-496 4.39e-44

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: 165.08  E-value: 4.39e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  11 LSFS----DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNR---EQGLDDGRIIYE-QDL----------IVARLQ 72
Cdd:COG1123  10 LSVRypggDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGllpHGGRISGEVLLDgRDLlelsealrgrRIGMVF 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  73 QDPPRNVEG-SVYDFVAEGIEEQaeylkryhDISRLVMndpseknlnelakvqeqldhhnlwqlENRINEVLAQLGLDP- 150
Cdd:COG1123  90 QDPMTQLNPvTVGDQIAEALENL--------GLSRAEA--------------------------RARVLELLEAVGLERr 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 151 -NVALSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLD----IETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVD 225
Cdd:COG1123 136 lDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDvttqAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVV 215
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 226 LDRGKLVtypgnydqyllekeEALRVEELQnaefdrklaqeevwirqgikarrtrneGRVRALKAMRRergerrevMGTA 305
Cdd:COG1123 216 MDDGRIV--------------EDGPPEEIL---------------------------AAPQALAAVPR--------LGAA 246
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 306 KMQVEEASRSGKIVFEMEDVC--YQVDGK---QLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVG- 379
Cdd:COG1123 247 RGRAAPAAAAAEPLLEVRNLSkrYPVRGKggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDg 326
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 380 ---TKLEVAYFDQHRAE-----------LDPDKTVMDNLAEG--------KQEVMvngkpRHVLGYLQDFLFHPKRAMTP 437
Cdd:COG1123 327 kdlTKLSRRSLRELRRRvqmvfqdpyssLNPRMTVGDIIAEPlrlhgllsRAERR-----ERVAELLERVGLPPDLADRY 401
                       490       500       510       520       530       540
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15830287 438 VRALSGGERNRLLLAR-LFLKPSnLLILDEPTNDLDVETLELLEELIDSYQ----GTVLLVSHD 496
Cdd:COG1123 402 PHELSGGQRQRVAIARaLALEPK-LLILDEPTSALDVSVQAQILNLLRDLQrelgLTYLFISHD 464
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
320-513 4.11e-33

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 126.08  E-value: 4.11e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 320 FEMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKL-----------EVAYFD 388
Cdd:COG4619   1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPlsampppewrrQVAYVP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 389 QhRAELdPDKTVMDNLAEGKQEVMVNGKPRHVLGYLQDFLFHPKRAMTPVRALSGGERNRLLLAR-LFLKPSNLLiLDEP 467
Cdd:COG4619  81 Q-EPAL-WGGTVRDNLPFPFQLRERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRaLLLQPDVLL-LDEP 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 15830287 468 TNDLDVETLELLEELIDSY----QGTVLLVSHDRQFVDNTVTECWIFEGG 513
Cdd:COG4619 158 TSALDPENTRRVEELLREYlaeeGRAVLWVSHDPEQIERVADRVLTLEAG 207
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
12-258 7.78e-33

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: 126.51  E-value: 7.78e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  12 SFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEqdlivarlqqdpprnvegsvydfvAEGI 91
Cdd:COG4555  10 KYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILID------------------------GEDV 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  92 EEQAEYLKRyhDISRLVMNDPSEKNLnelaKVQEQLDH----HNLW--QLENRINEVLAQLGLDP--NVALSSLSGGWLR 163
Cdd:COG4555  66 RKEPREARR--QIGVLPDERGLYDRL----TVRENIRYfaelYGLFdeELKKRIEELIELLGLEEflDRRVGELSTGMKK 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 164 KAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTF---NGTIIFISHDRSFIRNMATRIVDLDRGKLV---TYPGN 237
Cdd:COG4555 140 KVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALkkeGKTVLFSSHIMQEVEALCDRVVILHKGKVVaqgSLDEL 219
                       250       260
                ....*....|....*....|.
gi 15830287 238 YDQYLLEKEEALRVEELQNAE 258
Cdd:COG4555 220 REEIGEENLEDAFVALIGSEE 240
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
1-231 7.79e-33

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 126.36  E-value: 7.79e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   1 MSLISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRI-IYEQDLIVARL------QQ 73
Cdd:COG1121   4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVrLFGKPPRRARRrigyvpQR 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  74 dppRNVEG----SVYDFVAEGieeqaeylkRYHDISRLVMNDPSEKnlnelAKVQEQLDHHNLWQLENRinevlaqlgld 149
Cdd:COG1121  84 ---AEVDWdfpiTVRDVVLMG---------RYGRRGLFRRPSRADR-----EAVDEALERVGLEDLADR----------- 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 150 pnvALSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFNG---TIIFISHDRSFIRNMATRIVDL 226
Cdd:COG1121 136 ---PIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRegkTILVVTHDLGAVREYFDRVLLL 212

                ....*
gi 15830287 227 DRGKL 231
Cdd:COG1121 213 NRGLV 217
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
3-232 1.46e-32

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: 125.93  E-value: 1.46e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   3 LISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYE-QDL----------IVARL 71
Cdd:COG1120   1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDgRDLaslsrrelarRIAYV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  72 QQDPPRNVEGSVYDFVAEGieeqaeylkRYhdisrlvmndPseknlnelakvqeqldHHNLWQLENR-----INEVLAQL 146
Cdd:COG1120  81 PQEPPAPFGLTVRELVALG---------RY----------P----------------HLGLFGRPSAedreaVEEALERT 125
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 147 GLDP--NVALSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDI----ETIDWLEGFLKTFNGTIIFISHDRSFIRNMA 220
Cdd:COG1120 126 GLEHlaDRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLahqlEVLELLRRLARERGRTVVMVLHDLNLAARYA 205
                       250
                ....*....|..
gi 15830287 221 TRIVDLDRGKLV 232
Cdd:COG1120 206 DRLVLLKDGRIV 217
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
12-232 1.39e-31

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 122.86  E-value: 1.39e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  12 SFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNreqGL---DDGRI-IYEQDliVARLQQDPPRNV-----EGS 82
Cdd:COG1131   9 RYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLL---GLlrpTSGEVrVLGED--VARDPAEVRRRIgyvpqEPA 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  83 VYDFVAegIEEQAEYLKRYHDISRlvmndpseknlnelakvqeqldhhnlWQLENRINEVLAQLGLDP--NVALSSLSGG 160
Cdd:COG1131  84 LYPDLT--VRENLRFFARLYGLPR--------------------------KEARERIDELLELFGLTDaaDRKVGTLSGG 135
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15830287 161 WLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFNG---TIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:COG1131 136 MKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAAegkTVLLSTHYLEEAERLCDRVAIIDKGRIV 210
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
11-230 1.88e-31

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: 121.42  E-value: 1.88e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  11 LSFS----DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLIVARLQQDPPRNVeGSVYDF 86
Cdd:cd03225   5 LSFSypdgARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKV-GLVFQN 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  87 VaegiEEQaeylkryhdisrLVMNDPSEknlnELA--KVQEQLDHHnlwQLENRINEVLAQLGLDP--NVALSSLSGGWL 162
Cdd:cd03225  84 P----DDQ------------FFGPTVEE----EVAfgLENLGLPEE---EIEERVEEALELVGLEGlrDRSPFTLSGGQK 140
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15830287 163 RKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFNG---TIIFISHDRSFIRNMATRIVDLDRGK 230
Cdd:cd03225 141 QRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAegkTIIIVTHDLDLLLELADRVIVLEDGK 211
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
11-232 2.09e-30

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: 119.36  E-value: 2.09e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  11 LSFS---DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNreqGL---DDGRIIYE-QDLIVARLQ----------Q 73
Cdd:COG1122   6 LSFSypgGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLN---GLlkpTSGEVLVDgKDITKKNLRelrrkvglvfQ 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  74 DpPRN--VEGSVYDFVAEGIEEQAeylkryhdISRlvmndpseknlnelAKVQEqldhhnlwqlenRINEVLAQLGLDP- 150
Cdd:COG1122  83 N-PDDqlFAPTVEEDVAFGPENLG--------LPR--------------EEIRE------------RVEEALELVGLEHl 127
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 151 -NVALSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFNG---TIIFISHDRSFIRNMATRIVDL 226
Cdd:COG1122 128 aDRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKegkTVIIVTHDLDLVAELADRVIVL 207

                ....*.
gi 15830287 227 DRGKLV 232
Cdd:COG1122 208 DDGRIV 213
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
319-504 4.46e-30

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 118.65  E-value: 4.46e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 319 VFEMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV-GTKLE-----VAYFDQhRA 392
Cdd:COG1121   6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLfGKPPRrarrrIGYVPQ-RA 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 393 ELDPDK--TVMDnlaegkqeVMVNGKPRHvLGylqdFLFHPKRA-------------MT-----PVRALSGGERNRLLLA 452
Cdd:COG1121  85 EVDWDFpiTVRD--------VVLMGRYGR-RG----LFRRPSRAdreavdealervgLEdladrPIGELSGGQQQRVLLA 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15830287 453 RLFLKPSNLLILDEPTNDLDVETLELLEELIDSYQG---TVLLVSHD----RQFVDNTV 504
Cdd:COG1121 152 RALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRegkTILVVTHDlgavREYFDRVL 210
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
323-503 9.21e-30

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: 116.42  E-value: 9.21e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 323 EDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVG----TKLEVAYFDQ-----HRAE 393
Cdd:COG4133   6 ENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNgepiRDAREDYRRRlaylgHADG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 394 LDPDKTVMDNL---AEGKQEVMVNGKPRHVLGYLQdfLfhPKRAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTND 470
Cdd:COG4133  86 LKPELTVRENLrfwAALYGLRADREAIDEALEAVG--L--AGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTA 161
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 15830287 471 LDVETLELLEELIDSY---QGTVLLVSHDRQFVDNT 503
Cdd:COG4133 162 LDAAGVALLAELIAAHlarGGAVLLTTHQPLELAAA 197
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
4-231 9.39e-30

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 116.84  E-value: 9.39e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   4 ISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLI-----------VARLQ 72
Cdd:COG4619   1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLsampppewrrqVAYVP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  73 QDPPRnVEGSVYDfvaegieeqaeYLKRYHDISRLVMNDPseknlnelakvqeqldhhnlwqlenRINEVLAQLGLDPNV 152
Cdd:COG4619  81 QEPAL-WGGTVRD-----------NLPFPFQLRERKFDRE-------------------------RALELLERLGLPPDI 123
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 153 A---LSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIET----IDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVD 225
Cdd:COG4619 124 LdkpVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENtrrvEELLREYLAEEGRAVLWVSHDPEQIERVADRVLT 203

                ....*.
gi 15830287 226 LDRGKL 231
Cdd:COG4619 204 LEAGRL 209
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
17-232 1.00e-29

ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];


Pssm-ID: 440741 [Multi-domain]  Cd Length: 248  Bit Score: 117.98  E-value: 1.00e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  17 PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLIVARLQQDPPRNVegsvydfvaegieeqae 96
Cdd:COG1124  19 PVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV----------------- 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  97 ylkryhdisRLVMNDPsEKNLNELAKVQEQLD----HHNLWQLENRINEVLAQLGLDPNVAL---SSLSGGWLRKAALGR 169
Cdd:COG1124  82 ---------QMVFQDP-YASLHPRHTVDRILAeplrIHGLPDREERIAELLEQVGLPPSFLDrypHQLSGGQRQRVAIAR 151
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15830287 170 ALVSNPRVLLLDEPTNHLDI----ETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:COG1124 152 ALILEPELLLLDEPTSALDVsvqaEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIV 218
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
335-469 1.53e-29

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: 114.28  E-value: 1.53e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   335 VKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVG-----------TKLEVAYFDQHrAELDPDKTVMDN 403
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDgqdltdderksLRKEIGYVFQD-PQLFPRLTVREN 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15830287   404 LAEGKQEVMVNGKPR-----HVLGYLQDFLFHPKRAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTN 469
Cdd:pfam00005  80 LRLGLLLKGLSKREKdaraeEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
4-232 1.83e-29

Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 116.31  E-value: 1.83e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   4 ISMHGAWLSFS-DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIY-EQDLivARLQQD--PP--R 77
Cdd:COG2884   2 IRFENVSKRYPgGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVnGQDL--SRLKRReiPYlrR 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  78 NVeGSVY-DFvaegieeqaeylkryhdisRLVMNDPSEKNLnELA-KVQEQLDHhnlwQLENRINEVLAQLGLD------ 149
Cdd:COG2884  80 RI-GVVFqDF-------------------RLLPDRTVYENV-ALPlRVTGKSRK----EIRRRVREVLDLVGLSdkakal 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 150 PNValssLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFN--G-TIIFISHDRSFIRNMATRIVDL 226
Cdd:COG2884 135 PHE----LSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINrrGtTVLIATHDLELVDRMPKRVLEL 210

                ....*.
gi 15830287 227 DRGKLV 232
Cdd:COG2884 211 EDGRLV 216
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
321-500 4.68e-29

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: 114.94  E-value: 4.68e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 321 EMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV-GTKLE-----VAYFDQHRaEL 394
Cdd:cd03235   1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVfGKPLEkerkrIGYVPQRR-SI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 395 DPDK--TVMDnlaegkqeVMVNGKPRHVlgylqDFLFHPKRA-------------MT-----PVRALSGGERNRLLLARL 454
Cdd:cd03235  80 DRDFpiSVRD--------VVLMGLYGHK-----GLFRRLSKAdkakvdealervgLSeladrQIGELSGGQQQRVLLARA 146
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 15830287 455 FLKPSNLLILDEPTNDLDVETLELLEELIDSYQG---TVLLVSHDRQFV 500
Cdd:cd03235 147 LVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRRegmTILVVTHDLGLV 195
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
12-242 9.56e-29

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 120.77  E-value: 9.56e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   12 SFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLIVARLQQDpprnvegSVYDFvAEGI 91
Cdd:PRK15064 328 GFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQD-------HAYDF-ENDL 399
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   92 ---EEQAEYLKRYHDisrlvmndpseknlnelakvqEQLdhhnlwqlenrINEVLAQL---GLDPNVALSSLSGGWLRKA 165
Cdd:PRK15064 400 tlfDWMSQWRQEGDD---------------------EQA-----------VRGTLGRLlfsQDDIKKSVKVLSGGEKGRM 447
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15830287  166 ALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKLVTYPGNYDQYL 242
Cdd:PRK15064 448 LFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFSGTYEEYL 524
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
317-511 1.37e-28

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: 120.43  E-value: 1.37e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   317 KIVFEMEDVCYQVD-GKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKLEVAYFDQhRAELD 395
Cdd:TIGR03719   2 QYIYTMNRVSKVVPpKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQ-EPQLD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   396 PDKTVMDNLAEGKQEVmvngkpRHVL------------------------GYLQDFLFHPK---------RAM------- 435
Cdd:TIGR03719  81 PTKTVRENVEEGVAEI------KDALdrfneisakyaepdadfdklaaeqAELQEIIDAADawdldsqleIAMdalrcpp 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15830287   436 --TPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELIDSYQGTVLLVSHDRQFVDNtVTEcWIFE 511
Cdd:TIGR03719 155 wdADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDN-VAG-WILE 230
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
12-231 4.67e-28

ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213197 [Multi-domain]  Cd Length: 173  Bit Score: 110.57  E-value: 4.67e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  12 SFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNreqGLddgriiyeqdlivarLQQDpprnvEGSVYDFVAEGI 91
Cdd:cd03230   9 RYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIIL---GL---------------LKPD-----SGEIKVLGKDIK 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  92 EEQAEYLKRyhdISRLVMNDPSEKNLNelakVQEQLDhhnlwqlenrinevlaqlgldpnvalssLSGGWLRKAALGRAL 171
Cdd:cd03230  66 KEPEEVKRR---IGYLPEEPSLYENLT----VRENLK----------------------------LSGGMKQRLALAQAL 110
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15830287 172 VSNPRVLLLDEPTNHLDIETIDWLEGFLKTFN---GTIIFISHDRSFIRNMATRIVDLDRGKL 231
Cdd:cd03230 111 LHDPELLILDEPTSGLDPESRREFWELLRELKkegKTILLSSHILEEAERLCDRVAILNNGRI 173
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
321-495 5.02e-28

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: 110.55  E-value: 5.02e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 321 EMEDVC--YQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIhvgtklevaYFDQHraeldpdk 398
Cdd:cd03228   2 EFKNVSfsYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEI---------LIDGV-------- 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 399 tvmdNLAEGKQEVMvngkpRHVLGYL-QD-FLFHpkraMTpVRA--LSGGERNRLLLARLFLKPSNLLILDEPTNDLDVE 474
Cdd:cd03228  65 ----DLRDLDLESL-----RKNIAYVpQDpFLFS----GT-IREniLSGGQRQRIAIARALLRDPPILILDEATSALDPE 130
                       170       180
                ....*....|....*....|...
gi 15830287 475 TLELLEELIDSYQG--TVLLVSH 495
Cdd:cd03228 131 TEALILEALRALAKgkTVIVIAH 153
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
310-538 7.10e-28

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: 118.33  E-value: 7.10e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 310 EEASRSGKIVFEMEDVC--YQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV-GTKLE--- 383
Cdd:COG4987 324 EPAPAPGGPSLELEDVSfrYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLgGVDLRdld 403
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 384 -------VAYFDQhraelDP---DKTVMDNLAEGKQEV----MvngkpRHVLG--YLQDFLFH-PKRAMTPV----RALS 442
Cdd:COG4987 404 eddlrrrIAVVPQ-----RPhlfDTTLRENLRLARPDAtdeeL-----WAALErvGLGDWLAAlPDGLDTWLgeggRRLS 473
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 443 GGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELIDSYQG--TVLLVSHDRQFVDNtVTECWIFEGGGKIGRyv 520
Cdd:COG4987 474 GGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAgrTVLLITHRLAGLER-MDRILVLEDGRIVEQ-- 550
                       250
                ....*....|....*...
gi 15830287 521 GGYHDARGQQEQYVALKQ 538
Cdd:COG4987 551 GTHEELLAQNGRYRQLYQ 568
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
310-513 1.03e-27

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: 117.94  E-value: 1.03e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 310 EEASRSGKIVFEMEDVCYQ-VDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV-GTKLE---- 383
Cdd:COG4988 327 APLPAAGPPSIELEDVSFSyPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILInGVDLSdldp 406
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 384 ------VAYFDQHrAELdPDKTVMDNLAEGK-----QEVmvngkpRHVLG--YLQDFLfhpkRAM-----TPV----RAL 441
Cdd:COG4988 407 aswrrqIAWVPQN-PYL-FAGTIRENLRLGRpdasdEEL------EAALEaaGLDEFV----AALpdgldTPLgeggRGL 474
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15830287 442 SGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELIDSY-QG-TVLLVSHDRQFVDNtVTECWIFEGG 513
Cdd:COG4988 475 SGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLaKGrTVILITHRLALLAQ-ADRILVLDDG 547
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
17-232 1.26e-27

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: 111.06  E-value: 1.26e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  17 PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEqdlivarlqqdpPRNVEGSVydfvaegieeQAE 96
Cdd:cd03257  19 KALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFD------------GKDLLKLS----------RRL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  97 YLKRYHDISrLVMNDPSEkNLNELAKVQEQL--------DHHNLWQLENRINEVLAQLGLDPNVALS---SLSGGWLRKA 165
Cdd:cd03257  77 RKIRRKEIQ-MVFQDPMS-SLNPRMTIGEQIaeplrihgKLSKKEARKEAVLLLLVGVGLPEEVLNRyphELSGGQRQRV 154
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15830287 166 ALGRALVSNPRVLLLDEPTNHLD----IETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:cd03257 155 AIARALALNPKLLIADEPTSALDvsvqAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIV 225
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
19-232 1.91e-27

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: 116.54  E-value: 1.91e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYE-QDL----------IVARLQ---QDP-----PRNv 79
Cdd:COG1123 281 VDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDgKDLtklsrrslreLRRRVQmvfQDPysslnPRM- 359
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  80 egSVYDFVAEGieeqaeyLKRYHDISRlvmndpseknlnelakvqeqldhhnlWQLENRINEVLAQLGLDPNVAL---SS 156
Cdd:COG1123 360 --TVGDIIAEP-------LRLHGLLSR--------------------------AERRERVAELLERVGLPPDLADrypHE 404
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 157 LSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIET----IDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:COG1123 405 LSGGQRQRVAIARALALEPKLLILDEPTSALDVSVqaqiLNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIV 484
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
317-511 2.06e-27

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 116.76  E-value: 2.06e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  317 KIVFEMEDVCYQVDG-KQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKLEVAYFDQhRAELD 395
Cdd:PRK11819   4 QYIYTMNRVSKVVPPkKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYLPQ-EPQLD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  396 PDKTVMDNLAEGKQEVM--------VN---GKPRHVL-------GYLQDFLFHP---------KRAM---------TPVR 439
Cdd:PRK11819  83 PEKTVRENVEEGVAEVKaaldrfneIYaayAEPDADFdalaaeqGELQEIIDAAdawdldsqlEIAMdalrcppwdAKVT 162
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15830287  440 ALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELIDSYQGTVLLVSHDRQFVDNtVTEcWIFE 511
Cdd:PRK11819 163 KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDN-VAG-WILE 232
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
3-230 2.89e-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: 2.89e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   3 LISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILnreQGL---DDGRIiyeqdlivaRLQQDPPRNV 79
Cdd:COG4133   2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRIL---AGLlppSAGEV---------LWNGEPIRDA 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  80 EGSVYDFVAegieeqaeYLkrYHDISrlvmndpseknLNELAKVQEQLDH----HNLWQLENRINEVLAQLGLDP--NVA 153
Cdd:COG4133  70 REDYRRRLA--------YL--GHADG-----------LKPELTVRENLRFwaalYGLRADREAIDEALEAVGLAGlaDLP 128
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 154 LSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFN---GTIIFISHDRSFIRnmATRIVDLDRGK 230
Cdd:COG4133 129 VRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLargGAVLLTTHQPLELA--AARVLDLGDFK 206
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
5-230 9.11e-27

ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213179 [Multi-domain]  Cd Length: 157  Bit Score: 106.56  E-value: 9.11e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   5 SMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIiyeqdlivarlqqdpprnvegsvy 84
Cdd:cd00267   1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEI------------------------ 56
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  85 dfvaegieeqaeylkryhdisrlvmndpseknlnelakvqeQLDHHNLWQLENRinEVLAQLGLdpnvaLSSLSGGWLRK 164
Cdd:cd00267  57 -----------------------------------------LIDGKDIAKLPLE--ELRRRIGY-----VPQLSGGQRQR 88
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15830287 165 AALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFNG---TIIFISHDRSFIRNMATRIVDLDRGK 230
Cdd:cd00267  89 VALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEegrTVIIVTHDPELAELAADRVIVLKDGK 157
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
321-496 4.78e-26

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: 105.21  E-value: 4.78e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 321 EMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV-GTKLE----------VAYFDQ 389
Cdd:cd03214   1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLdGKDLAslspkelarkIAYVPQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 390 HRAELDpdktvMDNLAEgkqevmvngkpRhvlgylqdflfhpkramtPVRALSGGERNRLLLARLFLKPSNLLILDEPTN 469
Cdd:cd03214  81 ALELLG-----LAHLAD-----------R------------------PFNELSGGERQRVLLARALAQEPPILLLDEPTS 126
                       170       180       190
                ....*....|....*....|....*....|.
gi 15830287 470 DLDVETLELLEELI----DSYQGTVLLVSHD 496
Cdd:cd03214 127 HLDIAHQIELLELLrrlaRERGKTVVMVLHD 157
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
3-473 1.32e-25

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 110.88  E-value: 1.32e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   3 LISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIyeqdlivarlqqdpprnVEGS 82
Cdd:COG1129   4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEIL-----------------LDGE 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  83 VYDF-------------------------VAEGIeeqaeYLKRYHDISRLVmndpSEKNLNELAKvqeqldhhnlwqlen 137
Cdd:COG1129  67 PVRFrsprdaqaagiaiihqelnlvpnlsVAENI-----FLGREPRRGGLI----DWRAMRRRAR--------------- 122
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 138 rinEVLAQLGL--DPNVALSSLSGGwlRKA--ALGRALVSNPRVLLLDEPTNHLDIETIDWLegF-----LKTFNGTIIF 208
Cdd:COG1129 123 ---ELLARLGLdiDPDTPVGDLSVA--QQQlvEIARALSRDARVLILDEPTASLTEREVERL--FriirrLKAQGVAIIY 195
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 209 ISHDRSFIRNMATRIVDLDRGKLvtypgnydqyllekeealrVEELQNAEFDRklaqEEVwIRQ--GikarrtrnegrvR 286
Cdd:COG1129 196 ISHRLDEVFEIADRVTVLRDGRL-------------------VGTGPVAELTE----DEL-VRLmvG------------R 239
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 287 ALKAMRRergerrevmgtakmqvEEASRSGKIVFEMEDVCyqvdGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLML 366
Cdd:COG1129 240 ELEDLFP----------------KRAAAPGEVVLEVEGLS----VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALF 299
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 367 GQLQADSGRIHV-GTKLE-----------VAYF--DQHRAELDPDKTVMDNLAEGKQEVMVNGKP-------RHVLGYLQ 425
Cdd:COG1129 300 GADPADSGEIRLdGKPVRirsprdairagIAYVpeDRKGEGLVLDLSIRENITLASLDRLSRGGLldrrrerALAEEYIK 379
                       490       500       510       520
                ....*....|....*....|....*....|....*....|....*....
gi 15830287 426 DFLFHPKRAMTPVRALSGGERNRLLLAR-LFLKPSnLLILDEPTNDLDV 473
Cdd:COG1129 380 RLRIKTPSPEQPVGNLSGGNQQKVVLAKwLATDPK-VLILDEPTRGIDV 427
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
320-513 1.64e-25

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: 105.11  E-value: 1.64e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 320 FEMEDVCYQV-DGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV-GTKLEVAYFDQHRAEL--- 394
Cdd:COG1122   1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVdGKDITKKNLRELRRKVglv 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 395 --DPD-----KTVMD-------NLAEGKQEV---------MVNgkprhvlgyLQDFLFHpkramtPVRALSGGERNRLLL 451
Cdd:COG1122  81 fqNPDdqlfaPTVEEdvafgpeNLGLPREEIrerveealeLVG---------LEHLADR------PPHELSGGQKQRVAI 145
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15830287 452 AR-LFLKPSnLLILDEPTNDLDVETLELLEELIDSYQG---TVLLVSHDRQFVDNTVTECWIFEGG 513
Cdd:COG1122 146 AGvLAMEPE-VLVLDEPTAGLDPRGRRELLELLKRLNKegkTVIIVTHDLDLVAELADRVIVLDDG 210
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
321-513 2.28e-25

ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213179 [Multi-domain]  Cd Length: 157  Bit Score: 102.32  E-value: 2.28e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 321 EMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIhvgtklevaYFDQHRAELDPDKTV 400
Cdd:cd00267   1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEI---------LIDGKDIAKLPLEEL 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 401 MDNLAegkqevmvngkprhvlgylqdFLFHpkramtpvraLSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLE 480
Cdd:cd00267  72 RRRIG---------------------YVPQ----------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLL 120
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 15830287 481 ELIDSYQG---TVLLVSHDRQFVDNTVTECWIFEGG 513
Cdd:cd00267 121 ELLRELAEegrTVIIVTHDPELAELAADRVIVLKDG 156
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
321-496 3.50e-25

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: 102.48  E-value: 3.50e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 321 EMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV----------GTKLEVAYFDQH 390
Cdd:cd03230   2 EVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVlgkdikkepeEVKRRIGYLPEE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 391 rAELDPDKTVMDNLaegkqevmvngkprhvlgylqdflfhpkramtpvrALSGGERNRLLLARLFLKPSNLLILDEPTND 470
Cdd:cd03230  82 -PSLYENLTVRENL-----------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSG 125
                       170       180
                ....*....|....*....|....*....
gi 15830287 471 LDVETLELLEELIDSY---QGTVLLVSHD 496
Cdd:cd03230 126 LDPESRREFWELLRELkkeGKTILLSSHI 154
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
5-231 4.88e-25

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: 103.38  E-value: 4.88e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   5 SMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILnreQGL---DDGRI------IYEQDLIVARLQQ-- 73
Cdd:cd03235   1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAI---LGLlkpTSGSIrvfgkpLEKERKRIGYVPQrr 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  74 DPPRNVEGSVYDFVAEGIEEQAEYLKRYHDISRlvmndpseknlnelAKVQEQLDHHNLWQLENRinevlaqlgldpnvA 153
Cdd:cd03235  78 SIDRDFPISVRDVVLMGLYGHKGLFRRLSKADK--------------AKVDEALERVGLSELADR--------------Q 129
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 154 LSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFNG---TIIFISHDRSFIRNMATRIVDLDRGK 230
Cdd:cd03235 130 IGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRRegmTILVVTHDLGLVLEYFDRVLLLNRTV 209

                .
gi 15830287 231 L 231
Cdd:cd03235 210 V 210
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
321-496 4.94e-25

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 103.99  E-value: 4.94e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 321 EMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVG----------TKLEVAYFDQH 390
Cdd:COG1131   2 EVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLgedvardpaeVRRRIGYVPQE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 391 rAELDPDKTVMDNLaegkqEVM--VNGKPRHVLG-----YLQDF-LfhPKRAMTPVRALSGGERNRLLLARLFLKPSNLL 462
Cdd:COG1131  82 -PALYPDLTVRENL-----RFFarLYGLPRKEARerideLLELFgL--TDAADRKVGTLSGGMKQRLGLALALLHDPELL 153
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 15830287 463 ILDEPTNDLDVETLELLEELIDSY--QG-TVLLVSHD 496
Cdd:COG1131 154 ILDEPTSGLDPEARRELWELLRELaaEGkTVLLSTHY 190
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
12-232 5.99e-25

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: 103.07  E-value: 5.99e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  12 SFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILnreQGL---DDGRIiyeQDLIVARLQQDPPRNVEGSVydfva 88
Cdd:cd03268   9 TYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKII---LGLikpDSGEI---TFDGKSYQKNIEALRRIGAL----- 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  89 egIEEQAeylkryhdisrLVMNDPSEKNLNELAKVqeqldhhnLWQLENRINEVLAQLGLD--PNVALSSLSGGWLRKAA 166
Cdd:cd03268  78 --IEAPG-----------FYPNLTARENLRLLARL--------LGIRKKRIDEVLDVVGLKdsAKKKVKGFSLGMKQRLG 136
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15830287 167 LGRALVSNPRVLLLDEPTNHLDIETIDWLEGF---LKTFNGTIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:cd03268 137 IALALLGNPDLLILDEPTNGLDPDGIKELRELilsLRDQGITVLISSHLLSEIQKVADRIGIINKGKLI 205
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
11-234 6.80e-25

ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.


Pssm-ID: 213181 [Multi-domain]  Cd Length: 180  Bit Score: 101.74  E-value: 6.80e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  11 LSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQdlivarlqqdpprnvegsvydfvaeg 90
Cdd:cd03214   7 VGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDG-------------------------- 60
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  91 ieeqaeylkryHDISRLvmndpSEKnlnELAK----VQEQLDHHNLWQLENRInevlaqlgldpnvaLSSLSGGWLRKAA 166
Cdd:cd03214  61 -----------KDLASL-----SPK---ELARkiayVPQALELLGLAHLADRP--------------FNELSGGERQRVL 107
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15830287 167 LGRALVSNPRVLLLDEPTNHLDI----ETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKLVTY 234
Cdd:cd03214 108 LARALAQEPPILLLDEPTSHLDIahqiELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQ 179
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
11-246 8.59e-25

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: 109.54  E-value: 8.59e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  11 LSFS----DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILnreQGL---DDGRIIY-EQDLivarlQQDPPRNV--- 79
Cdd:COG2274 479 VSFRypgdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLL---LGLyepTSGRILIdGIDL-----RQIDPASLrrq 550
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  80 -----------EGSVYD---FVAEGIEEQaeylkRYHDISRLVmndpsekNLNELAKvqeqldhhnlwQLENRINEVLAQ 145
Cdd:COG2274 551 igvvlqdvflfSGTIREnitLGDPDATDE-----EIIEAARLA-------GLHDFIE-----------ALPMGYDTVVGE 607
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 146 LGldpnvalSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIET----IDWLEGFLKtfNGTIIFISHDRSFIRNmAT 221
Cdd:COG2274 608 GG-------SNLSGGQRQRLAIARALLRNPRILILDEATSALDAETeaiiLENLRRLLK--GRTVIIIAHRLSTIRL-AD 677
                       250       260
                ....*....|....*....|....*
gi 15830287 222 RIVDLDRGKLVTYpGNYDQyLLEKE 246
Cdd:COG2274 678 RIIVLDKGRIVED-GTHEE-LLARK 700
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
315-502 1.29e-24

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: 109.15  E-value: 1.29e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 315 SGKIvfEMEDVC--YQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGtklevayfDQHRA 392
Cdd:COG2274 471 KGDI--ELENVSfrYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILID--------GIDLR 540
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 393 ELDPDK-----------------TVMDNLAEGKQEV----------MVNgkprhvlgyLQDFL-FHPKRAMTPV----RA 440
Cdd:COG2274 541 QIDPASlrrqigvvlqdvflfsgTIRENITLGDPDAtdeeiieaarLAG---------LHDFIeALPMGYDTVVgeggSN 611
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15830287 441 LSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELIDSYQG--TVLLVSHDRQFVDN 502
Cdd:COG2274 612 LSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKgrTVIIIAHRLSTIRL 675
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
4-230 1.95e-24

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: 100.34  E-value: 1.95e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   4 ISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNreqGLDdgriiyeqdlivarlqqdppRNVEGSV 83
Cdd:cd03229   1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIA---GLE--------------------EPDSGSI 57
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  84 YdfvAEGIeeqaeylkryhDISRLVMNDPseknlnelakvqeqldhhnlwQLENRINEVLAQLGLDP------NVALSsL 157
Cdd:cd03229  58 L---IDGE-----------DLTDLEDELP---------------------PLRRRIGMVFQDFALFPhltvleNIALG-L 101
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15830287 158 SGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKT----FNGTIIFISHDRSFIRNMATRIVDLDRGK 230
Cdd:cd03229 102 SGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSlqaqLGITVVLVTHDLDEAARLADRVVVLRDGK 178
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
321-513 4.21e-24

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: 100.62  E-value: 4.21e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 321 EMEDVCYQVDG--KQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKLEVAYFDQHRAEL---- 394
Cdd:cd03225   1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKvglv 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 395 --DPD-----KTVMDNLAEGkqevMVN-GKPRH-----VLGYLQDFLFHPKRAmTPVRALSGGERNRLLLAR-LFLKPsN 460
Cdd:cd03225  81 fqNPDdqffgPTVEEEVAFG----LENlGLPEEeieerVEEALELVGLEGLRD-RSPFTLSGGQKQRVAIAGvLAMDP-D 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15830287 461 LLILDEPTNDLDVETLELLEELIDSYQG---TVLLVSHDRQFVDNTVTECWIFEGG 513
Cdd:cd03225 155 ILLLDEPTAGLDPAGRRELLELLKKLKAegkTIIIVTHDLDLLLELADRVIVLEDG 210
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
13-517 4.84e-24

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: 106.43  E-value: 4.84e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287    13 FSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILnreQGLDD-----GRIIYEQDLIVARLQQDPPRNV-------- 79
Cdd:TIGR03269  10 FDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVL---RGMDQyeptsGRIIYHVALCEKCGYVERPSKVgepcpvcg 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287    80 ---EGSVYDFVAEGIEEQAEYLKR-----------YHDISRL--VMNDPSEKNLNELAKVQEQLDHHNLWQLENRINEVL 143
Cdd:TIGR03269  87 gtlEPEEVDFWNLSDKLRRRIRKRiaimlqrtfalYGDDTVLdnVLEALEEIGYEGKEAVGRAVDLIEMVQLSHRITHIA 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   144 aqlgldpnvalSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDW----LEGFLKTFNGTIIFISHDRSFIRNM 219
Cdd:TIGR03269 167 -----------RDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLvhnaLEEAVKASGISMVLTSHWPEVIEDL 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   220 ATRIVDLDRGKLVTyPGNYDQYLlekeeALRVEELQNAEFDRKLAQEEVWIR-QGIKARRTRNE-GRVRAlkamrrerge 297
Cdd:TIGR03269 236 SDKAIWLENGEIKE-EGTPDEVV-----AVFMEGVSEVEKECEVEVGEPIIKvRNVSKRYISVDrGVVKA---------- 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   298 rrevmgtakmqveeasrsgkivfemedvcyqVDGKQLvkdfsaQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIH 377
Cdd:TIGR03269 300 -------------------------------VDNVSL------EVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVN 342
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   378 VG--------TKLEVayFDQHRAE-----------LDPDKTVMDNLAEG-KQEVMVNGKPRHVLGYLQDFLFHPKRAMTP 437
Cdd:TIGR03269 343 VRvgdewvdmTKPGP--DGRGRAKryigilhqeydLYPHRTVLDNLTEAiGLELPDELARMKAVITLKMVGFDEEKAEEI 420
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   438 VR----ALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELI----DSYQGTVLLVSHDRQFVDNTVTECWI 509
Cdd:TIGR03269 421 LDkypdELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSIlkarEEMEQTFIIVSHDMDFVLDVCDRAAL 500
                         570
                  ....*....|
gi 15830287   510 FEGGG--KIG 517
Cdd:TIGR03269 501 MRDGKivKIG 510
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
4-232 8.36e-24

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: 99.90  E-value: 8.36e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   4 ISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRI-IYEQDliVARLqqdPPRnvegs 82
Cdd:cd03259   1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEIlIDGRD--VTGV---PPE----- 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  83 vydfvaegieeqaeylKRyhDISrLVMNDPS-------EKNLN---ELAKVQEQldhhnlwQLENRINEVLAQLGLDP-- 150
Cdd:cd03259  71 ----------------RR--NIG-MVFQDYAlfphltvAENIAfglKLRGVPKA-------EIRARVRELLELVGLEGll 124
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 151 NVALSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKT----FNGTIIFISHDRSFIRNMATRIVDL 226
Cdd:cd03259 125 NRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELREELKElqreLGITTIYVTHDQEEALALADRIAVM 204

                ....*.
gi 15830287 227 DRGKLV 232
Cdd:cd03259 205 NEGRIV 210
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
319-496 9.37e-24

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: 100.89  E-value: 9.37e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 319 VFEMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV-GTKLE----------VAYF 387
Cdd:COG1120   1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLdGRDLAslsrrelarrIAYV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 388 DQHRaELDPDKTVMDNLAEGK------------------QEVMvngkprHVLGyLQDFlfhpkrAMTPVRALSGGERNRL 449
Cdd:COG1120  81 PQEP-PAPFGLTVRELVALGRyphlglfgrpsaedreavEEAL------ERTG-LEHL------ADRPVDELSGGERQRV 146
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15830287 450 LLARLFLKPSNLLILDEPTNDLDVetlelleelidSYQ---------------GTVLLVSHD 496
Cdd:COG1120 147 LIARALAQEPPLLLLDEPTSHLDL-----------AHQlevlellrrlarergRTVVMVLHD 197
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
11-246 1.15e-22

ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444012 [Multi-domain]  Cd Length: 563  Bit Score: 102.14  E-value: 1.15e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  11 LSFS---DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRI-IYEQDLivARLQQDPPRN-------- 78
Cdd:COG4988 342 VSFSypgGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSIlINGVDL--SDLDPASWRRqiawvpqn 419
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  79 ---VEGSVYDFVaegieeqaeylkryhdisRLVMNDPSEknlnelAKVQEQLDHHNLWqlenrinEVLAQL--GLDPNVA 153
Cdd:COG4988 420 pylFAGTIRENL------------------RLGRPDASD------EELEAALEAAGLD-------EFVAALpdGLDTPLG 468
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 154 L--SSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIET---IdwLEGFLKTFNG-TIIFISHDRSFIRNmATRIVDLD 227
Cdd:COG4988 469 EggRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETeaeI--LQALRRLAKGrTVILITHRLALLAQ-ADRILVLD 545
                       250
                ....*....|....*....
gi 15830287 228 RGKLVTYpGNYDQyLLEKE 246
Cdd:COG4988 546 DGRIVEQ-GTHEE-LLAKN 562
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
11-250 1.46e-22

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: 102.15  E-value: 1.46e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  11 LSFS----DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRI---------IYEQDL--IVARLQQDP 75
Cdd:COG4987 339 VSFRypgaGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSItlggvdlrdLDEDDLrrRIAVVPQRP 418
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  76 prnvegsvYDF---VAEGIeeqaeylkryhdisRLVMNDPSEKNLNE-LAKVQeqLDhhnlwqlenrinEVLAQL--GLD 149
Cdd:COG4987 419 --------HLFdttLRENL--------------RLARPDATDEELWAaLERVG--LG------------DWLAALpdGLD 462
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 150 PNV--ALSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETID-WLEGFLKTFNG-TIIFISHDRSFIRNMaTRIVD 225
Cdd:COG4987 463 TWLgeGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQaLLADLLEALAGrTVLLITHRLAGLERM-DRILV 541
                       250       260
                ....*....|....*....|....*
gi 15830287 226 LDRGKLVTyPGNYDQyLLEKEEALR 250
Cdd:COG4987 542 LEDGRIVE-QGTHEE-LLAQNGRYR 564
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...
19-232 2.31e-22

ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];


Pssm-ID: 440180 [Multi-domain]  Cd Length: 257  Bit Score: 96.65  E-value: 2.31e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYE-QDLI------VARL------QQdpPRNVEG-SVY 84
Cdd:COG0411  20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDgRDITglpphrIARLgiartfQN--PRLFPElTVL 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  85 DFVAEGIEEQAEYlKRYHDISRLVMNDPSEKNLNElakvqeqldhhnlwqlenRINEVLAQLGLDP--NVALSSLSGGWL 162
Cdd:COG0411  98 ENVLVAAHARLGR-GLLAALLRLPRARREEREARE------------------RAEELLERVGLADraDEPAGNLSYGQQ 158
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15830287 163 RKAALGRALVSNPRVLLLDEPT---NHLDI-ETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:COG0411 159 RRLEIARALATEPKLLLLDEPAaglNPEETeELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVI 232
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
19-232 3.45e-22

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: 95.58  E-value: 3.45e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYE-QDliVARLqqdpprnvegSVYDFVAEGIeeqaey 97
Cdd:cd03219  16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDgED--ITGL----------PPHEIARLGI------ 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  98 lKRYHDISRLVMNDPSEKNLneLAKVQEQLDHHNLW--------QLENRINEVLAQLGLDP--NVALSSLSGGWLRKAAL 167
Cdd:cd03219  78 -GRTFQIPRLFPELTVLENV--MVAAQARTGSGLLLararreerEARERAEELLERVGLADlaDRPAGELSYGQQRRLEI 154
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15830287 168 GRALVSNPRVLLLDEPT---NHLDIE-TIDWLEGfLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:cd03219 155 ARALATDPKLLLLDEPAaglNPEETEeLAELIRE-LRERGITVLLVEHDMDVVMSLADRVTVLDQGRVI 222
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
1-232 3.81e-22

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: 95.92  E-value: 3.81e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   1 MSLISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNRE--QGLDDGRIIYEQDL------------ 66
Cdd:COG1119   1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDlpPTYGNDVRLFGERRggedvwelrkri 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  67 -IV-ARLQQDPPRNVegSVYDFVAEGieeqaeylkrYHDISRLvMNDPSEknlnelakvqEQldhhnlwqlENRINEVLA 144
Cdd:COG1119  81 gLVsPALQLRFPRDE--TVLDVVLSG----------FFDSIGL-YREPTD----------EQ---------RERARELLE 128
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 145 QLGLDP--NVALSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIET----IDWLEGFLKTFNGTIIFISHDRSFIRN 218
Cdd:COG1119 129 LLGLAHlaDRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGArellLALLDKLAAEGAPTLVLVTHHVEEIPP 208
                       250
                ....*....|....
gi 15830287 219 MATRIVDLDRGKLV 232
Cdd:COG1119 209 GITHVLLLKDGRVV 222
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
17-231 3.95e-22

ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.


Pssm-ID: 213222 [Multi-domain]  Cd Length: 218  Bit Score: 95.25  E-value: 3.95e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  17 PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNreqGLDD---GRIIyeqdlivarlqqdpprnVEGSvyDFVAEGIEE 93
Cdd:cd03255  18 QALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILG---GLDRptsGEVR-----------------VDGT--DISKLSEKE 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  94 QAEYLKR--------YHDISRLvmndPSEKNLnELAKVqeqLDHHNLWQLENRINEVLAQLGLD------PnvalSSLSG 159
Cdd:cd03255  76 LAAFRRRhigfvfqsFNLLPDL----TALENV-ELPLL---LAGVPKKERRERAEELLERVGLGdrlnhyP----SELSG 143
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15830287 160 GWLRKAALGRALVSNPRVLLLDEPTNHLDIET----IDWLEGFLKTFNGTIIFISHDRSFIRnMATRIVDLDRGKL 231
Cdd:cd03255 144 GQQQRVAIARALANDPKIILADEPTGNLDSETgkevMELLRELNKEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
3-232 5.89e-22

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: 95.05  E-value: 5.89e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   3 LISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNreqGL---DDGRIIY---------EQDLIVAR 70
Cdd:COG1127   5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLII---GLlrpDSGEILVdgqditglsEKELYELR 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  71 LQ-----QDpprnveGSVYDF--VAEGIeeqAEYLKRYHDISRlvmndpseknlnelakvqeqldhhnlWQLENRINEVL 143
Cdd:COG1127  82 RRigmlfQG------GALFDSltVFENV---AFPLREHTDLSE--------------------------AEIRELVLEKL 126
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 144 AQLGLDPNVAL--SSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIET---IDWLEGFL-KTFNGTIIFISHDRSFIR 217
Cdd:COG1127 127 ELVGLPGAADKmpSELSGGMRKRVALARALALDPEILLYDEPTAGLDPITsavIDELIRELrDELGLTSVVVTHDLDSAF 206
                       250
                ....*....|....*
gi 15830287 218 NMATRIVDLDRGKLV 232
Cdd:COG1127 207 AIADRVAVLADGKII 221
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
312-497 8.35e-22

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: 99.28  E-value: 8.35e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   312 ASRSGKIVFEMEDVCYQvDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGtklevayfDQHR 391
Cdd:TIGR02857 316 AAPASSLEFSGVSVAYP-GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVN--------GVPL 386
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   392 AELDPD-----------------KTVMDNLAEGKQEV---MVNGKPRHVlgYLQDFLFH-PKRAMTPV----RALSGGER 446
Cdd:TIGR02857 387 ADADADswrdqiawvpqhpflfaGTIAENIRLARPDAsdaEIREALERA--GLDEFVAAlPQGLDTPIgeggAGLSGGQA 464
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 15830287   447 NRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELIDSY-QG-TVLLVSHDR 497
Cdd:TIGR02857 465 QRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALaQGrTVLLVTHRL 517
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
321-517 1.52e-21

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: 93.09  E-value: 1.52e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 321 EMEDVCYQV-DGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKlevayfDQHRAEL----- 394
Cdd:cd03226   1 RIENISFSYkKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGK------PIKAKERrksig 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 395 ----DPD-----KTVMDNLAEGKQEV-MVNGKPRHVLGYLQDFLF---HPkramtpvRALSGGERNRLLLARLFLKPSNL 461
Cdd:cd03226  75 yvmqDVDyqlftDSVREELLLGLKELdAGNEQAETVLKDLDLYALkerHP-------LSLSGGQKQRLAIAAALLSGKDL 147
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15830287 462 LILDEPTNDLDVETLELLEELIDSYQG---TVLLVSHDRQFVDNTVTECwIFEGGGKIG 517
Cdd:cd03226 148 LIFDEPTSGLDYKNMERVGELIRELAAqgkAVIVITHDYEFLAKVCDRV-LLLANGAIV 205
ABC_tran_CTD pfam16326
ABC transporter C-terminal domain; This domain is found at the C-terminus of ABC transporters. ...
561-630 1.97e-21

ABC transporter C-terminal domain; This domain is found at the C-terminus of ABC transporters. It has a coiled coil structure with an atypical 3(10)-helix in the alpha-hairpin region. It is involved in DNA_binding.


Pssm-ID: 465095 [Multi-domain]  Cd Length: 69  Bit Score: 88.29  E-value: 1.97e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   561 KLSYKLQRELEQLPQLLEDLEAKLEALQTQVADASFFSQpHEQTQKVLADMAAAEQELEQAFERWEYLEA 630
Cdd:pfam16326   1 KLSYKEQRELEELEAEIEKLEEEIAELEAQLADPELYSD-YEKLQELSAELEELEAELEELYERWEELEE 69
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
321-502 2.69e-21

Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 92.81  E-value: 2.69e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 321 EMEDVCY-QVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVG----TKL---EVAY------ 386
Cdd:COG2884   3 RFENVSKrYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNgqdlSRLkrrEIPYlrrrig 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 387 --FDQHRaeLDPDKTVMDNLA-----EGKQEVMVNGKPRHVLGYLQdfLFHPKRAMtpVRALSGGERNRLLLARLFL-KP 458
Cdd:COG2884  83 vvFQDFR--LLPDRTVYENVAlplrvTGKSRKEIRRRVREVLDLVG--LSDKAKAL--PHELSGGEQQRVAIARALVnRP 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 15830287 459 SnLLILDEPTNDLDVETLELLEELIDSY--QG-TVLLVSHDRQFVDN 502
Cdd:COG2884 157 E-LLLADEPTGNLDPETSWEIMELLEEInrRGtTVLIATHDLELVDR 202
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
333-496 2.74e-21

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: 92.95  E-value: 2.74e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 333 QLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI----HVGTKLEVAYFDQHRAE-----------LDPD 397
Cdd:cd03257  19 KALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIifdgKDLLKLSRRLRKIRRKEiqmvfqdpmssLNPR 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 398 KTVMDNLAEG--KQEVMVNGKPRHVLGYLQDFLFH-PKRAMT--PvRALSGGERNRLLLAR-LFLKPSnLLILDEPTNDL 471
Cdd:cd03257  99 MTIGEQIAEPlrIHGKLSKKEARKEAVLLLLVGVGlPEEVLNryP-HELSGGQRQRVAIARaLALNPK-LLIADEPTSAL 176
                       170       180
                ....*....|....*....|....*....
gi 15830287 472 DVETLELLEELI----DSYQGTVLLVSHD 496
Cdd:cd03257 177 DVSVQAQILDLLkklqEELGLTLLFITHD 205
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
11-230 3.48e-21

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: 90.91  E-value: 3.48e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  11 LSFS----DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRI-IYEQDL----------IVARLQQDP 75
Cdd:cd03228   6 VSFSypgrPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEIlIDGVDLrdldleslrkNIAYVPQDP 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  76 PRnVEGSVYDfvaegieeqaeylkryhdisrlvmndpseknlnelakvqeqldhhNLwqlenrinevlaqlgldpnvals 155
Cdd:cd03228  86 FL-FSGTIRE---------------------------------------------NI----------------------- 96
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15830287 156 sLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIET-IDWLEGFLKTFNG-TIIFISHDRSFIRnMATRIVDLDRGK 230
Cdd:cd03228  97 -LSGGQRQRIAIARALLRDPPILILDEATSALDPETeALILEALRALAKGkTVIVIAHRLSTIR-DADRIIVLDDGR 171
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
2-232 7.18e-21

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 91.64  E-value: 7.18e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   2 SLISMHGAWLSFSDA----PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNreqGLD---DGRIIYE-QDliVARLQQ 73
Cdd:COG1136   3 PLLELRNLTKSYGTGegevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILG---GLDrptSGEVLIDgQD--ISSLSE 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  74 DpprnvegsvydfvaegieEQAEYlkRYHDISrLVMNDPsekNL-NELaKVQE------QLDHHNLWQLENRINEVLAQL 146
Cdd:COG1136  78 R------------------ELARL--RRRHIG-FVFQFF---NLlPEL-TALEnvalplLLAGVSRKERRERARELLERV 132
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 147 GLD------PNvalsSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIET----IDWLEGFLKTFNGTIIFISHDRsFI 216
Cdd:COG1136 133 GLGdrldhrPS----QLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTgeevLELLRELNRELGTTIVMVTHDP-EL 207
                       250
                ....*....|....*.
gi 15830287 217 RNMATRIVDLDRGKLV 232
Cdd:COG1136 208 AARADRVIRLRDGRIV 223
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
1-232 8.43e-21

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 94.39  E-value: 8.43e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   1 MSLISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNreqGL---DDGRI-IYEQDliVARLqqdPP 76
Cdd:COG3842   3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIA---GFetpDSGRIlLDGRD--VTGL---PP 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  77 --RNVeG------------SVYDFVAEGIeeqaeylkRYHDISRlvmndpseknlnelAKVQEqldhhnlwqlenRINEV 142
Cdd:COG3842  75 ekRNV-GmvfqdyalfphlTVAENVAFGL--------RMRGVPK--------------AEIRA------------RVAEL 119
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 143 LAQLGLD------PnvalSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLD----IETIDWLEGFLKTFNGTIIFISHD 212
Cdd:COG3842 120 LELVGLEgladryP----HQLSGGQQQRVALARALAPEPRVLLLDEPLSALDaklrEEMREELRRLQRELGITFIYVTHD 195
                       250       260
                ....*....|....*....|..
gi 15830287 213 RS--FIrnMATRIVDLDRGKLV 232
Cdd:COG3842 196 QEeaLA--LADRIAVMNDGRIE 215
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
327-496 9.10e-21

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: 91.03  E-value: 9.10e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 327 YQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVG----------TKLEVAYFDQHRAeLDP 396
Cdd:cd03263  10 YKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINgysirtdrkaARQSLGYCPQFDA-LFD 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 397 DKTVMDNL---AegkqevMVNGKPRH-----VLGYLQDFLFHPKRAmTPVRALSGGERNRLLLARLFLKPSNLLILDEPT 468
Cdd:cd03263  89 ELTVREHLrfyA------RLKGLPKSeikeeVELLLRVLGLTDKAN-KRARTLSGGMKRKLSLAIALIGGPSVLLLDEPT 161
                       170       180       190
                ....*....|....*....|....*....|
gi 15830287 469 NDLDVETLELLEELIDSYQG--TVLLVSHD 496
Cdd:cd03263 162 SGLDPASRRAIWDLILEVRKgrSIILTTHS 191
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
319-495 9.42e-21

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: 92.07  E-value: 9.42e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 319 VFEMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQL-QADSGRIHV-GTKLE------------- 383
Cdd:COG1119   3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLpPTYGNDVRLfGERRGgedvwelrkrigl 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 384 VAYFDQHRaeLDPDKTVMDNLAEGK----------QEVMVNgKPRHVLGYLQdfLFHpkRAMTPVRALSGGERNRLLLAR 453
Cdd:COG1119  83 VSPALQLR--FPRDETVLDVVLSGFfdsiglyrepTDEQRE-RARELLELLG--LAH--LADRPFGTLSQGEQRRVLIAR 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 15830287 454 LFLKPSNLLILDEPTNDLDVETLELLEELIDSY--QG--TVLLVSH 495
Cdd:COG1119 156 ALVKDPELLILDEPTAGLDLGARELLLALLDKLaaEGapTLVLVTH 201
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
19-185 1.20e-20

ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.


Pssm-ID: 394964 [Multi-domain]  Cd Length: 150  Bit Score: 88.86  E-value: 1.20e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287    19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLIVARLQQDPPRNVeGSVYDFVaegieeqaeyl 98
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEI-GYVFQDP----------- 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287    99 kryHDISRLVMndpsEKNLNELAKVQEQLDHHnlwqLENRINEVLAQLGLD------PNVALSSLSGGWLRKAALGRALV 172
Cdd:pfam00005  69 ---QLFPRLTV----RENLRLGLLLKGLSKRE----KDARAEEALEKLGLGdladrpVGERPGTLSGGQRQRVAIARALL 137
                         170
                  ....*....|...
gi 15830287   173 SNPRVLLLDEPTN 185
Cdd:pfam00005 138 TKPKLLLLDEPTA 150
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
321-516 1.72e-20

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 92.56  E-value: 1.72e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  321 EMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSG----------------RIHVGTkleV 384
Cdd:PRK13537   9 DFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGsislcgepvpsrarhaRQRVGV---V 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  385 AYFDQhraeLDPDKTVMDNL-AEGKQEVMVNGKPRHVLGYLQDFLFHPKRAMTPVRALSGGERNRLLLARLFLKPSNLLI 463
Cdd:PRK13537  86 PQFDN----LDPDFTVRENLlVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLV 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15830287  464 LDEPTNDLDVETLELLEELIDSYQG---TVLLVSHDRQFVDNTVTECWIFEGGGKI 516
Cdd:PRK13537 162 LDEPTTGLDPQARHLMWERLRSLLArgkTILLTTHFMEEAERLCDRLCVIEEGRKI 217
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
4-232 1.83e-20

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: 90.64  E-value: 1.83e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   4 ISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKilnreqglddgriiyeqdLIVARLQQDpprnvEGSV 83
Cdd:cd03261   1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLR------------------LIVGLLRPD-----SGEV 57
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  84 YdfvAEGieeqaeylkryHDISRLvmndpSEKNLNELAK---VQEQ------------------LDHHNL--WQLENRIN 140
Cdd:cd03261  58 L---IDG-----------EDISGL-----SEAELYRLRRrmgMLFQsgalfdsltvfenvafplREHTRLseEEIREIVL 118
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 141 EVLAQLGLDPNVAL--SSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLD-------IETIDWLEgflKTFNGTIIFISH 211
Cdd:cd03261 119 EKLEAVGLRGAEDLypAELSGGMKKRVALARALALDPELLLYDEPTAGLDpiasgviDDLIRSLK---KELGLTSIMVTH 195
                       250       260
                ....*....|....*....|.
gi 15830287 212 DRSFIRNMATRIVDLDRGKLV 232
Cdd:cd03261 196 DLDTAFAIADRIAVLYDGKIV 216
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
4-232 2.01e-20

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: 88.64  E-value: 2.01e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   4 ISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIyeqdlivarlqqdpprnVEGSV 83
Cdd:cd03216   1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEIL-----------------VDGKE 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  84 YDFvaegieeqaeylkryhdisrlvmNDPSEKnlnelakvqeqldhhnlwqLENRINEVlaqlgldpnvalSSLSGGWLR 163
Cdd:cd03216  64 VSF-----------------------ASPRDA-------------------RRAGIAMV------------YQLSVGERQ 89
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15830287 164 KAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTF--NG-TIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:cd03216  90 MVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLraQGvAVIFISHRLDEVFEIADRVTVLRDGRVV 161
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
320-500 2.15e-20

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: 88.78  E-value: 2.15e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 320 FEMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKLEVAYFDQHRAE------ 393
Cdd:cd03229   1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLrrrigm 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 394 ------LDPDKTVMDNLAEGkqevmvngkprhvlgylqdflfhpkramtpvraLSGGERNRLLLAR-LFLKPsNLLILDE 466
Cdd:cd03229  81 vfqdfaLFPHLTVLENIALG---------------------------------LSGGQQQRVALARaLAMDP-DVLLLDE 126
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 15830287 467 PTNDLDVETLELLEELI----DSYQGTVLLVSHDRQFV 500
Cdd:cd03229 127 PTSALDPITRREVRALLkslqAQLGITVVLVTHDLDEA 164
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
321-497 2.17e-20

ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213226 [Multi-domain]  Cd Length: 213  Bit Score: 89.89  E-value: 2.17e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 321 EMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKL---------EVAYFDQHR 391
Cdd:cd03259   2 ELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDvtgvpperrNIGMVFQDY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 392 AeLDPDKTVMDNLAEG--KQEVMVNGKPRHVLGYLQ--DFLFHPKRamtPVRALSGGERNRLLLAR-LFLKPSnLLILDE 466
Cdd:cd03259  82 A-LFPHLTVAENIAFGlkLRGVPKAEIRARVRELLElvGLEGLLNR---YPHELSGGQQQRVALARaLAREPS-LLLLDE 156
                       170       180       190
                ....*....|....*....|....*....|....*
gi 15830287 467 PTNDLDVETLELLEELIDSYQG----TVLLVSHDR 497
Cdd:cd03259 157 PLSALDAKLREELREELKELQRelgiTTIYVTHDQ 191
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
15-231 2.69e-20

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: 89.77  E-value: 2.69e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  15 DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEqDLIVARLqqdpPRNvegsvydfvaegieeQ 94
Cdd:cd03292  13 GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVN-GQDVSDL----RGR---------------A 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  95 AEYLKR-----YHDiSRLVMNDPSEKNLnelAKVQEQLDH-HNLWQleNRINEVLAQLGLD--PNVALSSLSGGWLRKAA 166
Cdd:cd03292  73 IPYLRRkigvvFQD-FRLLPDRNVYENV---AFALEVTGVpPREIR--KRVPAALELVGLShkHRALPAELSGGEQQRVA 146
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15830287 167 LGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFN---GTIIFISHDRSFIRNMATRIVDLDRGKL 231
Cdd:cd03292 147 IARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINkagTTVVVATHAKELVDTTRHRVIALERGKL 214
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
330-503 4.51e-20

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: 89.92  E-value: 4.51e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 330 DGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV----------GTKLEVAYFDQHRaELDPDKT 399
Cdd:COG4555  12 GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIdgedvrkeprEARRQIGVLPDER-GLYDRLT 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 400 VMDNL---AEGKQEVMVNGKPR-----HVLGyLQDFLfhpKRamtPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDL 471
Cdd:COG4555  91 VRENIryfAELYGLFDEELKKRieeliELLG-LEEFL---DR---RVGELSTGMKKKVALARALVHDPKVLLLDEPTNGL 163
                       170       180       190
                ....*....|....*....|....*....|....*
gi 15830287 472 DVETLELLEELIDSY--QG-TVLLVSHDRQFVDNT 503
Cdd:COG4555 164 DVMARRLLREILRALkkEGkTVLFSSHIMQEVEAL 198
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
12-232 4.57e-20

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


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 92.13  E-value: 4.57e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  12 SFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILnreQGL---DDGRIIY-EQDLIVARLQQDppRNVeG------ 81
Cdd:COG1118  11 RFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRII---AGLetpDSGRIVLnGRDLFTNLPPRE--RRV-Gfvfqhy 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  82 ------SVYDFVAEGIEeqaeylkryhdisrlvMNDPSEKNLNelAKVQEQLDHHNLWQLENRInevlaqlgldPnvalS 155
Cdd:COG1118  85 alfphmTVAENIAFGLR----------------VRPPSKAEIR--ARVEELLELVQLEGLADRY----------P----S 132
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 156 SLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDI----ETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKL 231
Cdd:COG1118 133 QLSGGQRQRVALARALAVEPEVLLLDEPFGALDAkvrkELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRI 212

                .
gi 15830287 232 V 232
Cdd:COG1118 213 E 213
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
321-496 6.14e-20

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: 89.10  E-value: 6.14e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 321 EMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTK--------------LEVAY 386
Cdd:cd03261   2 ELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEdisglseaelyrlrRRMGM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 387 FDQHRAELDpDKTVMDNLA------EGKQEVMVNGKprhVLGYLQDFLFHPKRAMTPvRALSGGERNRLLLAR-LFLKPS 459
Cdd:cd03261  82 LFQSGALFD-SLTVFENVAfplrehTRLSEEEIREI---VLEKLEAVGLRGAEDLYP-AELSGGMKKRVALARaLALDPE 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 15830287 460 nLLILDEPTNDLDVETLELLEELI----DSYQGTVLLVSHD 496
Cdd:cd03261 157 -LLLYDEPTAGLDPIASGVIDDLIrslkKELGLTSIMVTHD 196
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
4-232 7.26e-20

The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.


Pssm-ID: 213268 [Multi-domain]  Cd Length: 213  Bit Score: 88.47  E-value: 7.26e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   4 ISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEqDLIVARLqqdPP--RNV-- 79
Cdd:cd03301   1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIG-GRDVTDL---PPkdRDIam 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  80 ---------EGSVYDFVAEGIE----EQAEYLKRYHDISRLVmndpseknlnelaKVQEQLDHHnlwqlenrinevlaql 146
Cdd:cd03301  77 vfqnyalypHMTVYDNIAFGLKlrkvPKDEIDERVREVAELL-------------QIEHLLDRK---------------- 127
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 147 gldPnvalSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLD----IETIDWLEGFLKTFNGTIIFISHDRSFIRNMATR 222
Cdd:cd03301 128 ---P----KQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDaklrVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADR 200
                       250
                ....*....|
gi 15830287 223 IVDLDRGKLV 232
Cdd:cd03301 201 IAVMNDGQIQ 210
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
4-234 8.80e-20

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: 88.39  E-value: 8.80e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   4 ISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLD-----------DGRIIYEQDLIVARL- 71
Cdd:cd03260   1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIpgapdegevllDGKDIYDLDVDVLELr 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  72 -------QQDPPrnVEGSVYDFVAegieeqaeYLKRYHDISRlvmndpsEKNLNELakVQEQLDHHNLWqlenriNEVLA 144
Cdd:cd03260  81 rrvgmvfQKPNP--FPGSIYDNVA--------YGLRLHGIKL-------KEELDER--VEEALRKAALW------DEVKD 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 145 QLgldpnvALSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFNG--TIIFISHDRSFIRNMATR 222
Cdd:cd03260 136 RL------HALGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKeyTIVIVTHNMQQAARVADR 209
                       250
                ....*....|..
gi 15830287 223 IVDLDRGKLVTY 234
Cdd:cd03260 210 TAFLLNGRLVEF 221
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
320-495 9.48e-20

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: 86.89  E-value: 9.48e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 320 FEMEDVCYQVDGKQ--LVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV-GTKLEVAYFDQHRaeldp 396
Cdd:cd03246   1 LEVENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLdGADISQWDPNELG----- 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 397 dktvmdnlaegkqevmvngkpRHVlGYL-QDFLFHPKRAMTPVraLSGGERNRLLLARLFLKPSNLLILDEPTNDLDVET 475
Cdd:cd03246  76 ---------------------DHV-GYLpQDDELFSGSIAENI--LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEG 131
                       170       180
                ....*....|....*....|...
gi 15830287 476 LELLEELIDSYQ---GTVLLVSH 495
Cdd:cd03246 132 ERALNQAIAALKaagATRIVIAH 154
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
1-224 9.55e-20

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


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 89.38  E-value: 9.55e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   1 MSLISMHGAWLSFSDA----PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNreqGLDD---GRIIYE--------QD 65
Cdd:COG1116   5 APALELRGVSKRFPTGgggvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIA---GLEKptsGEVLVDgkpvtgpgPD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  66 LIVArLQQD---PPRNVEGSVydfvaegieeqaeylkryhdisRLVMndpseknlnELAKVQEQldhhnlwQLENRINEV 142
Cdd:COG1116  82 RGVV-FQEPallPWLTVLDNV----------------------ALGL---------ELRGVPKA-------ERRERAREL 122
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 143 LAQLGLD------PnvalSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETI----DWLEGFLKTFNGTIIFISHD 212
Cdd:COG1116 123 LELVGLAgfedayP----HQLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRerlqDELLRLWQETGKTVLFVTHD 198
                       250
                ....*....|....*
gi 15830287 213 rsfIRN---MATRIV 224
Cdd:COG1116 199 ---VDEavfLADRVV 210
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
330-496 1.06e-19

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 87.29  E-value: 1.06e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  330 DGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKLEVAYFDQHRAelDPDK---TVMDNLAE 406
Cdd:NF040873   3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSE--VPDSlplTVRDLVAM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  407 GK-QEVMVNGKPRHV-----------LGyLQDFLfhpKRamtPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVE 474
Cdd:NF040873  81 GRwARRGLWRRLTRDdraavddalerVG-LADLA---GR---QLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAE 153
                        170       180
                 ....*....|....*....|....*
gi 15830287  475 TLELLEELIDSYQG---TVLLVSHD 496
Cdd:NF040873 154 SRERIIALLAEEHArgaTVVVVTHD 178
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
310-496 1.22e-19

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: 92.81  E-value: 1.22e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   310 EEASRSGKIVFEMEDVCYQVDGKQLV-KDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV-GTKLEVAYF 387
Cdd:TIGR02868 325 AGAVGLGKPTLELRDLSAGYPGAPPVlDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLdGVPVSSLDQ 404
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   388 DQHRAEL-----DP---DKTVMDNLAEGKQEV----MVNGKPRHVLGYLQDFLfhPKRAMTPV----RALSGGERNRLLL 451
Cdd:TIGR02868 405 DEVRRRVsvcaqDAhlfDTTVRENLRLARPDAtdeeLWAALERVGLADWLRAL--PDGLDTVLgeggARLSGGERQRLAL 482
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 15830287   452 ARLFLKPSNLLILDEPTNDLDVETLELLEELI-DSYQG-TVLLVSHD 496
Cdd:TIGR02868 483 ARALLADAPILLLDEPTEHLDAETADELLEDLlAALSGrTVVLITHH 529
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
327-472 1.39e-19

ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.


Pssm-ID: 213214 [Multi-domain]  Cd Length: 178  Bit Score: 86.60  E-value: 1.39e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 327 YQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKLEVAYFDQHRAELdpdkTVMDnlae 406
Cdd:cd03247  10 YPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLI----SVLN---- 81
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15830287 407 gkQEVMV-NGKPRHVLGylqdflfhpkramtpvRALSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:cd03247  82 --QRPYLfDTTLRNNLG----------------RRFSGGERQRLALARILLQDAPIVLLDEPTVGLD 130
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
320-513 1.45e-19

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: 87.65  E-value: 1.45e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 320 FEMEDVCYQVDGKQL--VKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIhvgtklevaYFDQHRA-ELDP 396
Cdd:cd03245   3 IEFRNVSFSYPNQEIpaLDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSV---------LLDGTDIrQLDP 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 397 DK-----------------TVMDNLAEGK-----QEVMVNGKprhvLGYLQDFL-FHPKRAMTPV----RALSGGERNRL 449
Cdd:cd03245  74 ADlrrnigyvpqdvtlfygTLRDNITLGApladdERILRAAE----LAGVTDFVnKHPNGLDLQIgergRGLSGGQRQAV 149
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15830287 450 LLARLFLKPSNLLILDEPTNDLDVETLELLEELIDSYQG--TVLLVSHdRQFVDNTVTECWIFEGG 513
Cdd:cd03245 150 ALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGdkTLIIITH-RPSLLDLVDRIIVMDSG 214
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
1-232 1.52e-19

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


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 90.52  E-value: 1.52e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   1 MSLISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILnreQGLDD---GRIIYEqDLIVARLqqdPP- 76
Cdd:COG3839   1 MASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMI---AGLEDptsGEILIG-GRDVTDL---PPk 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  77 -RNVeGSV------YDF--VAEGIeeqAEYLKryhdisrlvmndpseknlneLAKVQEQldhhnlwQLENRINEVLAQLG 147
Cdd:COG3839  74 dRNI-AMVfqsyalYPHmtVYENI---AFPLK--------------------LRKVPKA-------EIDRRVREAAELLG 122
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 148 LDPnvaL-----SSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLD----IETIDWLEGFLKTFNGTIIFISHDRSFIRN 218
Cdd:COG3839 123 LED---LldrkpKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDaklrVEMRAEIKRLHRRLGTTTIYVTHDQVEAMT 199
                       250
                ....*....|....
gi 15830287 219 MATRIVDLDRGKLV 232
Cdd:COG3839 200 LADRIAVMNDGRIQ 213
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
19-232 2.34e-19

ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];


Pssm-ID: 440213 [Multi-domain]  Cd Length: 320  Bit Score: 89.34  E-value: 2.34e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  19 LDNAELHIEDNERVCLVGRNGAGKSTLMKI---LNREQGLDDGRIIYE-QDLivARLQQDPPRNVegsvydfvaegieeq 94
Cdd:COG0444  21 VDGVSFDVRRGETLGLVGESGSGKSTLARAilgLLPPPGITSGEILFDgEDL--LKLSEKELRKI--------------- 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  95 aeylkRYHDISrLVMNDP--SeknLNELAKVQEQ----LDHHNLW---QLENRINEVLAQLGL-DPNVALSS----LSGG 160
Cdd:COG0444  84 -----RGREIQ-MIFQDPmtS---LNPVMTVGDQiaepLRIHGGLskaEARERAIELLERVGLpDPERRLDRypheLSGG 154
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15830287 161 WLRKAALGRALVSNPRVLLLDEPTNHLDI----ETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:COG0444 155 MRQRVMIARALALEPKLLIADEPTTALDVtiqaQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIV 230
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
14-232 2.39e-19

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: 87.26  E-value: 2.39e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  14 SDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQ------DLIVAR-----LQQDPpRNVEGS 82
Cdd:cd03245  15 QEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdirqlDPADLRrnigyVPQDV-TLFYGT 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  83 VYDFVAEGieeqaeylKRYHDISRLVmndpsekNLNELAKVQEQLDHHnlwqlenrinevlaQLGLDPNVAL--SSLSGG 160
Cdd:cd03245  94 LRDNITLG--------APLADDERIL-------RAAELAGVTDFVNKH--------------PNGLDLQIGErgRGLSGG 144
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15830287 161 WLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFNG--TIIFISHDRSFIrNMATRIVDLDRGKLV 232
Cdd:cd03245 145 QRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGdkTLIIITHRPSLL-DLVDRIIVMDSGRIV 217
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
4-224 4.34e-19

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: 86.37  E-value: 4.34e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   4 ISMHGAWLSFSDA----PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLIVAR-------LQ 72
Cdd:cd03293   1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPgpdrgyvFQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  73 QD---PPRnvegSVYDFVAEGIEeqaeylkryhdisrlvmndpseknlneLAKVQEQldhhnlwQLENRINEVLAQLGLD 149
Cdd:cd03293  81 QDallPWL----TVLDNVALGLE---------------------------LQGVPKA-------EARERAEELLELVGLS 122
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 150 ------PnvalSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIET----IDWLEGFLKTFNGTIIFISHDrsfIRN- 218
Cdd:cd03293 123 gfenayP----HQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTreqlQEELLDIWRETGKTVLLVTHD---IDEa 195

                ....*...
gi 15830287 219 --MATRIV 224
Cdd:cd03293 196 vfLADRVV 203
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
321-496 5.84e-19

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: 85.99  E-value: 5.84e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 321 EMEDVCYQVDGKQL----VKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV-GTKL-----EVAY-FDQ 389
Cdd:cd03293   2 EVRNVSKTYGGGGGavtaLEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVdGEPVtgpgpDRGYvFQQ 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 390 HRaeLDPDKTVMDNLAEGkqeVMVNGKPR-----HVLGY-----LQDFLFH-PKramtpvrALSGGERNRLLLAR-LFLK 457
Cdd:cd03293  82 DA--LLPWLTVLDNVALG---LELQGVPKaeareRAEELlelvgLSGFENAyPH-------QLSGGMRQRVALARaLAVD 149
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 15830287 458 PsNLLILDEPTNDLDVETLELLEELI----DSYQGTVLLVSHD 496
Cdd:cd03293 150 P-DVLLLDEPFSALDALTREQLQEELldiwRETGKTVLLVTHD 191
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
1-473 9.98e-19

ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 443332 [Multi-domain]  Cd Length: 533  Bit Score: 89.74  E-value: 9.98e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   1 MSLISMHGAWLSFSDA----PLLDNAELHIEDNERVCLVGRNGAGKS----TLMKILNREQGLDDGRIIYE-QDLivarL 71
Cdd:COG4172   4 MPLLSVEDLSVAFGQGggtvEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDgQDL----L 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  72 QQDPP--RNVEGSvydfvaegieeqaeylkryhDISrLVMNDP--SeknLNELAKVQEQLD-----HHNLW--QLENRIN 140
Cdd:COG4172  80 GLSERelRRIRGN--------------------RIA-MIFQEPmtS---LNPLHTIGKQIAevlrlHRGLSgaAARARAL 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 141 EVLAQLGL-DPNVALSS----LSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIeTI-----DWLEGFLKTFNGTIIFIS 210
Cdd:COG4172 136 ELLERVGIpDPERRLDAyphqLSGGQRQRVMIAMALANEPDLLIADEPTTALDV-TVqaqilDLLKDLQRELGMALLLIT 214
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 211 HDRSFIRNMATRIVDLDRGKLV---------TYPGN-YDQYLLEKE-------------EALRVEELQnaefdrklaqee 267
Cdd:COG4172 215 HDLGVVRRFADRVAVMRQGEIVeqgptaelfAAPQHpYTRKLLAAEprgdprpvppdapPLLEARDLK------------ 282
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 268 VW--IRQGIKARRTrneGRVRAlkamrrergerrevmgtakmqveeasrsgkivfemedvcyqvdgkqlVKDFSAQVLRG 345
Cdd:COG4172 283 VWfpIKRGLFRRTV---GHVKA-----------------------------------------------VDGVSLTLRRG 312
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 346 DKIALIGPNGCGKTTLLKLMLGqLQADSGRIHV-GTKLEVAYFDQHR--------------AELDPDKTVMDNLAEG--K 408
Cdd:COG4172 313 ETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFdGQDLDGLSRRALRplrrrmqvvfqdpfGSLSPRMTVGQIIAEGlrV 391
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 409 QEVMVNGKPRHvlgylqdflfhpKRAmtpVRAL-----------------SGGERNRLLLAR-LFLKPSnLLILDEPTND 470
Cdd:COG4172 392 HGPGLSAAERR------------ARV---AEALeevgldpaarhryphefSGGQRQRIAIARaLILEPK-LLVLDEPTSA 455

                ...
gi 15830287 471 LDV 473
Cdd:COG4172 456 LDV 458
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
19-473 1.10e-18

ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 89.32  E-value: 1.10e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNreqGL---DDGRIIyeqdlivarlqqdpprnVEGSVYDF--------- 86
Cdd:COG3845  21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILY---GLyqpDSGEIL-----------------IDGKPVRIrsprdaial 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  87 ----------------VAEGIeeqaeylkryhdisrlVM-NDPSEKNLNELAKVQEqldhhnlwqlenRINEVLAQLGL- 148
Cdd:COG3845  81 gigmvhqhfmlvpnltVAENI----------------VLgLEPTKGGRLDRKAARA------------RIRELSERYGLd 132
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 149 -DPNVALSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTF--NG-TIIFISHDRSFIRNMATRIV 224
Cdd:COG3845 133 vDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRLaaEGkSIIFITHKLREVMAIADRVT 212
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 225 DLDRGKLVtypgnydqyllekeEALRVEELQNAEfdrkLAQEEVwirqgikarrtrneGRVRALKAmrrergerrevmgt 304
Cdd:COG3845 213 VLRRGKVV--------------GTVDTAETSEEE----LAELMV--------------GREVLLRV-------------- 246
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 305 akmqVEEASRSGKIVFEMEDVCYQVD-GKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVG---- 379
Cdd:COG3845 247 ----EKAPAEPGEVVLEVENLSVRDDrGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDgedi 322
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 380 --------TKLEVAYF--DQHRAELDPDKTVMDNLAEGKQE-------VMVNGKP--RHVLGYLQDFLFHPKRAMTPVRA 440
Cdd:COG3845 323 tglsprerRRLGVAYIpeDRLGRGLVPDMSVAENLILGRYRrppfsrgGFLDRKAirAFAEELIEEFDVRTPGPDTPARS 402
                       490       500       510
                ....*....|....*....|....*....|...
gi 15830287 441 LSGGERNRLLLARLFLKPSNLLILDEPTNDLDV 473
Cdd:COG3845 403 LSGGNQQKVILARELSRDPKLLIAAQPTRGLDV 435
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
321-496 1.87e-18

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: 85.03  E-value: 1.87e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 321 EMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVgtklevayFDQHRAELDPDK-- 398
Cdd:COG1127   7 EVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILV--------DGQDITGLSEKEly 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 399 -------------------TVMDNLA----E----GKQEV--MVNGKPRHVlGyLQDFlfhpkRAMTPvRALSGGERNRL 449
Cdd:COG1127  79 elrrrigmlfqggalfdslTVFENVAfplrEhtdlSEAEIreLVLEKLELV-G-LPGA-----ADKMP-SELSGGMRKRV 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 15830287 450 LLAR-LFLKPSnLLILDEPTNDLDVETLELLEELI----DSYQGTVLLVSHD 496
Cdd:COG1127 151 ALARaLALDPE-ILLYDEPTAGLDPITSAVIDELIrelrDELGLTSVVVTHD 201
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
331-495 2.73e-18

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: 83.81  E-value: 2.73e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 331 GKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIhvgTKLEVAYFDQHRA-----------ELDPDKT 399
Cdd:cd03268  12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEI---TFDGKSYQKNIEAlrrigalieapGFYPNLT 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 400 VMDNLAEGKQEVMVNGKPRH-VLGY--LQDflfHPKRamtPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETL 476
Cdd:cd03268  89 ARENLRLLARLLGIRKKRIDeVLDVvgLKD---SAKK---KVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGI 162
                       170       180
                ....*....|....*....|..
gi 15830287 477 ELLEELIDSYQ---GTVLLVSH 495
Cdd:cd03268 163 KELRELILSLRdqgITVLISSH 184
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
321-501 2.91e-18

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: 84.08  E-value: 2.91e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 321 EMEDVCYQVDG----KQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV-GTKL------------- 382
Cdd:cd03255   2 ELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVdGTDIsklsekelaafrr 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 383 -EVAY-FDQHRaeLDPDKTVMDNLA-----EGKQEVMVNGKPRHVLGYLQdfLfhPKRAMTPVRALSGGERNRLLLARLF 455
Cdd:cd03255  82 rHIGFvFQSFN--LLPDLTALENVElplllAGVPKKERRERAEELLERVG--L--GDRLNHYPSELSGGQQQRVAIARAL 155
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 15830287 456 LKPSNLLILDEPTNDLDVETLELLEELI----DSYQGTVLLVSHDRQFVD 501
Cdd:cd03255 156 ANDPKIILADEPTGNLDSETGKEVMELLrelnKEAGTTIVVVTHDPELAE 205
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
1-232 3.23e-18

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 84.58  E-value: 3.23e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287    1 MSLISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNR-----------EQGLDDGRIIYEQDLIVA 69
Cdd:PRK14247   1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRlielypearvsGEVYLDGQDIFKMDVIEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   70 RLQ-----QDPPRNVEGSVYDFVAEGIEeqaeylkryhdISRLVmndpseKNLNEL-AKVQEQLDHHNLW-QLENRInev 142
Cdd:PRK14247  81 RRRvqmvfQIPNPIPNLSIFENVALGLK-----------LNRLV------KSKKELqERVRWALEKAQLWdEVKDRL--- 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  143 laqlgldpNVALSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFNG--TIIFISHdrsfIRNMA 220
Cdd:PRK14247 141 --------DAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKdmTIVLVTH----FPQQA 208
                        250
                 ....*....|....*.
gi 15830287  221 TRIVD----LDRGKLV 232
Cdd:PRK14247 209 ARISDyvafLYKGQIV 224
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
12-241 3.29e-18

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


Pssm-ID: 274744 [Multi-domain]  Cd Length: 552  Bit Score: 88.45  E-value: 3.29e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287    12 SFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLIVARLQQ-----DPPRNvegsVYDF 86
Cdd:TIGR03719 331 AFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQsrdalDPNKT----VWEE 406
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287    87 VAEGieeqaeylkryHDISRLvmndpSEKNLNELAKVqeqldhhnlwqleNRINEVlaqlGLDPNVALSSLSGGWLRKAA 166
Cdd:TIGR03719 407 ISGG-----------LDIIKL-----GKREIPSRAYV-------------GRFNFK----GSDQQKKVGQLSGGERNRVH 453
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15830287   167 LGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLD-RGKLVTYPGNYDQY 241
Cdd:TIGR03719 454 LAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIATHILAFEgDSHVEWFEGNFSEY 529
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
335-496 3.93e-18

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: 83.92  E-value: 3.93e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 335 VKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKLEVAYFDQH----------RAELDPDKTVMDNL 404
Cdd:cd03267  37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFlrrigvvfgqKTQLWWDLPVIDSF 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 405 AEGKQevMVNGKPRHV---LGYLQDFLFHPKRAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEE 481
Cdd:cd03267 117 YLLAA--IYDLPPARFkkrLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRN 194
                       170
                ....*....|....*....
gi 15830287 482 LIDSY----QGTVLLVSHD 496
Cdd:cd03267 195 FLKEYnrerGTTVLLTSHY 213
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
34-501 4.33e-18

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 87.94  E-value: 4.33e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   34 LVGRNGAGKSTLMKILNreqglddGRIIyeqdlivarlqqdpPR--NVEGSV-YDFVAE---GIEEQaEYLKR------- 100
Cdd:PRK13409 104 ILGPNGIGKTTAVKILS-------GELI--------------PNlgDYEEEPsWDEVLKrfrGTELQ-NYFKKlyngeik 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  101 ------YHD-ISRLVMNDPSEknlnELAKVQEqldhhnlwqlENRINEVLAQLGLDP--NVALSSLSGGWLRKAALGRAL 171
Cdd:PRK13409 162 vvhkpqYVDlIPKVFKGKVRE----LLKKVDE----------RGKLDEVVERLGLENilDRDISELSGGELQRVAIAAAL 227
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  172 VSNPRVLLLDEPTNHLDI-------ETIDWLegflkTFNGTIIFISHDRSFIRNMATRIVdldrgklVTY--PGNY---- 238
Cdd:PRK13409 228 LRDADFYFFDEPTSYLDIrqrlnvaRLIREL-----AEGKYVLVVEHDLAVLDYLADNVH-------IAYgePGAYgvvs 295
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  239 ---------DQYLlekeealrveelqnaefDRKLAQEEVWIRQgikarrTRNEGRVRAlkamrrergerrevmgtakmqv 309
Cdd:PRK13409 296 kpkgvrvgiNEYL-----------------KGYLPEENMRIRP------EPIEFEERP---------------------- 330
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  310 EEASRSGKIVFEMEDVCYQVDGKQLVKDfSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRihVGTKLEVAYFDQ 389
Cdd:PRK13409 331 PRDESERETLVEYPDLTKKLGDFSLEVE-GGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGE--VDPELKISYKPQ 407
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  390 hRAELDPDKTVMDNLAEGKQEVMVNgkprhvlgYLQDFLFHP---KRAMT-PVRALSGGERNRLLLARLFLKPSNLLILD 465
Cdd:PRK13409 408 -YIKPDYDGTVEDLLRSITDDLGSS--------YYKSEIIKPlqlERLLDkNVKDLSGGELQRVAIAACLSRDADLYLLD 478
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|
gi 15830287  466 EPTNDLDVETLELLEELI----DSYQGTVLLVSHDRQFVD 501
Cdd:PRK13409 479 EPSAHLDVEQRLAVAKAIrriaEEREATALVVDHDIYMID 518
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
14-232 4.61e-18

ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213225 [Multi-domain]  Cd Length: 233  Bit Score: 83.78  E-value: 4.61e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  14 SDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYeQDLIVARLQQDPPRNV-------------- 79
Cdd:cd03258  16 GKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLV-DGTDLTLLSGKELRKArrrigmifqhfnll 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  80 -EGSVYDFVAEGIEeqaeylkryhdisrlvmndpseknlneLAKVQEQldhhnlwQLENRINEVLAQLGLD------Pnv 152
Cdd:cd03258  95 sSRTVFENVALPLE---------------------------IAGVPKA-------EIEERVLELLELVGLEdkadayP-- 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 153 alSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIET----IDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDR 228
Cdd:cd03258 139 --AQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETtqsiLALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEK 216

                ....
gi 15830287 229 GKLV 232
Cdd:cd03258 217 GEVV 220
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
34-232 5.57e-18

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: 83.01  E-value: 5.57e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  34 LVGRNGAGKSTLMKILNREQGLDDGRI-IYEQDL---------IVARLQQDPPRNVEGSVYDFVAegieeqaeYLKRYHD 103
Cdd:cd03264  30 LLGPNGAGKTTLMRILATLTPPSSGTIrIDGQDVlkqpqklrrRIGYLPQEFGVYPNFTVREFLD--------YIAWLKG 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 104 ISrlvmnDPSEKnlnelAKVQEQLDHHNLWQLENRinevlaqlgldpnvALSSLSGGWLRKAALGRALVSNPRVLLLDEP 183
Cdd:cd03264 102 IP-----SKEVK-----ARVDEVLELVNLGDRAKK--------------KIGSLSGGMRRRVGIAQALVGDPSILIVDEP 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 15830287 184 TNHLDIETIDWLEGFLKTF--NGTIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:cd03264 158 TAGLDPEERIRFRNLLSELgeDRIVILSTHIVEDVESLCNQVAVLNKGKLV 208
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
335-496 6.37e-18

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: 83.54  E-value: 6.37e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 335 VKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV-GT--------KLEVAYFDQHRAeLDPDKTVMDNLA 405
Cdd:cd03299  15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLnGKditnlppeKRDISYVPQNYA-LFPHMTVYKNIA 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 406 EG--KQEVMVNGKPRHVL---GYLQ-DFLFHPKramtpVRALSGGERNRLLLAR-LFLKPSnLLILDEPTNDLDVETLEL 478
Cdd:cd03299  94 YGlkKRKVDKKEIERKVLeiaEMLGiDHLLNRK-----PETLSGGEQQRVAIARaLVVNPK-ILLLDEPFSALDVRTKEK 167
                       170       180
                ....*....|....*....|..
gi 15830287 479 LEELI----DSYQGTVLLVSHD 496
Cdd:cd03299 168 LREELkkirKEFGVTVLHVTHD 189
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
13-231 7.48e-18

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: 83.16  E-value: 7.48e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  13 FSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLIVARLQQDppRNV-----------EG 81
Cdd:cd03296  12 FGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE--RNVgfvfqhyalfrHM 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  82 SVYDFVAEGIEEqaeylkryhdisRLVMNDPSEKNLNElaKVQEQLDhhnLWQLENRINEVLAQLgldpnvalsslSGGW 161
Cdd:cd03296  90 TVFDNVAFGLRV------------KPRSERPPEAEIRA--KVHELLK---LVQLDWLADRYPAQL-----------SGGQ 141
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15830287 162 LRKAALGRALVSNPRVLLLDEPTNHLDI----ETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKL 231
Cdd:cd03296 142 RQRVALARALAVEPKVLLLDEPFGALDAkvrkELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRI 215
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
312-516 7.53e-18

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 85.27  E-value: 7.53e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  312 ASRSGK---IVFEMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVgtkLEVAYFD 388
Cdd:PRK13536  31 ASIPGSmstVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITV---LGVPVPA 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  389 QHRA------------ELDPDKTVMDNL-AEGKQEVMVNGKPRHVLGYLQDFLFHPKRAMTPVRALSGGERNRLLLARLF 455
Cdd:PRK13536 108 RARLararigvvpqfdNLDLEFTVRENLlVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARAL 187
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15830287  456 LKPSNLLILDEPTNDLDVETLELLEELIDSY--QG-TVLLVSHDRQFVDNTVTECWIFEGGGKI 516
Cdd:PRK13536 188 INDPQLLILDEPTTGLDPHARHLIWERLRSLlaRGkTILLTTHFMEEAERLCDRLCVLEAGRKI 251
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
19-234 8.47e-18

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: 83.15  E-value: 8.47e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQdlivARLQQDPP--RNVeGSVYD----FVAEGIE 92
Cdd:cd03299  15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNG----KDITNLPPekRDI-SYVPQnyalFPHMTVY 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  93 EQAEY-LKRyhdisRLVMNDPSEKNLNELAKVQeQLDHhnlwqLENRinevlaqlglDPnvalSSLSGGWLRKAALGRAL 171
Cdd:cd03299  90 KNIAYgLKK-----RKVDKKEIERKVLEIAEML-GIDH-----LLNR----------KP----ETLSGGEQQRVAIARAL 144
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15830287 172 VSNPRVLLLDEPTNHLDIET----IDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKLVTY 234
Cdd:cd03299 145 VVNPKILLLDEPFSALDVRTkeklREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQV 211
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
12-232 1.12e-17

ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213267 [Multi-domain]  Cd Length: 232  Bit Score: 82.67  E-value: 1.12e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  12 SFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEqDLIVARLqqdPP--RNVEG-------- 81
Cdd:cd03300   9 FYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLD-GKDITNL---PPhkRPVNTvfqnyalf 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  82 ---SVYDFVAEGieeqaeylkryhdisrLVMNDPSEKNLNElaKVQEQLDHHNLWQLENRinevlaqlglDPnvalSSLS 158
Cdd:cd03300  85 phlTVFENIAFG----------------LRLKKLPKAEIKE--RVAEALDLVQLEGYANR----------KP----SQLS 132
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15830287 159 GGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFNG----TIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:cd03300 133 GGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKelgiTFVFVTHDQEEALTMSDRIAVMNKGKIQ 210
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
315-472 1.15e-17

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 86.76  E-value: 1.15e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 315 SGKIVFEmeDVCYQ-VDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKlEVAYFDQH--R 391
Cdd:COG1132 337 RGEIEFE--NVSFSyPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGV-DIRDLTLEslR 413
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 392 AEL-----DP---DKTVMDNLAEGK-----QEVM-----------VNGKPRhvlGYlqDflfhpkramTPV----RALSG 443
Cdd:COG1132 414 RQIgvvpqDTflfSGTIRENIRYGRpdatdEEVEeaakaaqahefIEALPD---GY--D---------TVVgergVNLSG 479
                       170       180
                ....*....|....*....|....*....
gi 15830287 444 GERNRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:COG1132 480 GQRQRIAIARALLKDPPILILDEATSALD 508
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
17-242 1.38e-17

ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213262 [Multi-domain]  Cd Length: 242  Bit Score: 82.73  E-value: 1.38e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  17 PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRI------IYEQDLIVARlqqdppRNVeGSVYdfvaeg 90
Cdd:cd03295  15 KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIfidgedIREQDPVELR------RKI-GYVI------ 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  91 ieeQAEYLKRYHDISRLVMNDPSeknlneLAKVQEQldhhnlwQLENRINEVLAQLGLDPNVAL----SSLSGGWLRKAA 166
Cdd:cd03295  82 ---QQIGLFPHMTVEENIALVPK------LLKWPKE-------KIRERADELLALVGLDPAEFAdrypHELSGGQQQRVG 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 167 LGRALVSNPRVLLLDEPTNHLDIETIDWL-EGFLK---TFNGTIIFISHDRSFIRNMATRIVDLDRGKLVTYpGNYDQYL 242
Cdd:cd03295 146 VARALAADPPLLLMDEPFGALDPITRDQLqEEFKRlqqELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQV-GTPDEIL 224
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
321-496 1.47e-17

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


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 82.83  E-value: 1.47e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 321 EMEDVC--YQVDGKQL--VKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV------GTKLEVAY-FDQ 389
Cdd:COG1116   9 ELRGVSkrFPTGGGGVtaLDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVdgkpvtGPGPDRGVvFQE 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 390 HRaeLDPDKTVMDNLAEGkqeVMVNGKPR-----HVLGY-----LQDFL-FHPkramtpvRALSGGERNRLLLAR-LFLK 457
Cdd:COG1116  89 PA--LLPWLTVLDNVALG---LELRGVPKaerreRARELlelvgLAGFEdAYP-------HQLSGGMRQRVAIARaLAND 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 15830287 458 PSnLLILDEPTNDLDVETLELLEELI----DSYQGTVLLVSHD 496
Cdd:COG1116 157 PE-VLLMDEPFGALDALTRERLQDELlrlwQETGKTVLFVTHD 198
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
19-232 1.66e-17

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


Pssm-ID: 213223 [Multi-domain]  Cd Length: 241  Bit Score: 82.23  E-value: 1.66e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEqDLIVARLQQDPPRNVEGSVydfvaegieeqAEYL 98
Cdd:cd03256  17 LKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLID-GTDINKLKGKALRQLRRQI-----------GMIF 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  99 KRYHDISRL-VMndpseKNLNELAkvqeqLDHHNLWQ-------LENRIN--EVLAQLGLDP--NVALSSLSGGWLRKAA 166
Cdd:cd03256  85 QQFNLIERLsVL-----ENVLSGR-----LGRRSTWRslfglfpKEEKQRalAALERVGLLDkaYQRADQLSGGQQQRVA 154
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 167 LGRALVSNPRVLLLDEPTNHLDIET----IDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:cd03256 155 IARALMQQPKLILADEPVASLDPASsrqvMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIV 224
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
321-496 1.67e-17

The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.


Pssm-ID: 213268 [Multi-domain]  Cd Length: 213  Bit Score: 81.53  E-value: 1.67e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 321 EMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVG----TKLE-----VAYFDQHR 391
Cdd:cd03301   2 ELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGgrdvTDLPpkdrdIAMVFQNY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 392 AeLDPDKTVMDNLAEG-----KQEVMVNGKPRHVLGYLQ-DFLFHPKramtpVRALSGGERNRLLLARLFLKPSNLLILD 465
Cdd:cd03301  82 A-LYPHMTVYDNIAFGlklrkVPKDEIDERVREVAELLQiEHLLDRK-----PKQLSGGQRQRVALGRAIVREPKVFLMD 155
                       170       180       190
                ....*....|....*....|....*....|....*
gi 15830287 466 EPTNDLDVETLELLEELIDSYQ----GTVLLVSHD 496
Cdd:cd03301 156 EPLSNLDAKLRVQMRAELKRLQqrlgTTTIYVTHD 190
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...
335-500 2.77e-17

ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];


Pssm-ID: 440180 [Multi-domain]  Cd Length: 257  Bit Score: 82.01  E-value: 2.77e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 335 VKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKlEVAYFDQHR------------AELDPDKTVMD 402
Cdd:COG0411  20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGR-DITGLPPHRiarlgiartfqnPRLFPELTVLE 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 403 NlaegkqeVMVNGKPRHVLGYLQDFLFHPK----------RAM-------------TPVRALSGGERNRLLLAR-LFLKP 458
Cdd:COG0411  99 N-------VLVAAHARLGRGLLAALLRLPRarreereareRAEellervgladradEPAGNLSYGQQRRLEIARaLATEP 171
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 15830287 459 SnLLILDEPT---NDLDVETLELLEELIDSYQG-TVLLVSHDRQFV 500
Cdd:COG0411 172 K-LLLLDEPAaglNPEETEELAELIRRLRDERGiTILLIEHDMDLV 216
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
18-232 2.88e-17

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


Pssm-ID: 213193 [Multi-domain]  Cd Length: 205  Bit Score: 80.76  E-value: 2.88e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  18 LLDNAELHIEDNERVCLVGRNGAGKSTLMKILnreQGL---DDGRIIYEQDLIVAR--------LQQDPPRNV-EGSVYD 85
Cdd:cd03226  15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKIL---AGLikeSSGSILLNGKPIKAKerrksigyVMQDVDYQLfTDSVRE 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  86 FVAEGIEEQAEYlkryhdisrlvmndpseknlneLAKVQEQLDHHNLWQLENRinevlaqlglDPnvalSSLSGGWLRKA 165
Cdd:cd03226  92 ELLLGLKELDAG----------------------NEQAETVLKDLDLYALKER----------HP----LSLSGGQKQRL 135
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 166 ALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFNG---TIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:cd03226 136 AIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAqgkAVIVITHDYEFLAKVCDRVLLLANGAIV 205
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
321-500 3.04e-17

ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).


Pssm-ID: 213186 [Multi-domain]  Cd Length: 236  Bit Score: 81.33  E-value: 3.04e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 321 EMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKlEVAYFDQHR--------- 391
Cdd:cd03219   2 EVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGE-DITGLPPHEiarlgigrt 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 392 ---AELDPDKTVMDNlaegkqeVMVNGKPRHVLGYLQDFLFHPKRAM------------------TPVRALSGGERNRLL 450
Cdd:cd03219  81 fqiPRLFPELTVLEN-------VMVAAQARTGSGLLLARARREEREAreraeellervgladladRPAGELSYGQQRRLE 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 15830287 451 LAR-LFLKPSnLLILDEPT---NDLDVETLELLEELIDSYQGTVLLVSHDRQFV 500
Cdd:cd03219 154 IARaLATDPK-LLLLDEPAaglNPEETEELAELIRELRERGITVLLVEHDMDVV 206
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
10-245 3.10e-17

ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213221 [Multi-domain]  Cd Length: 229  Bit Score: 81.12  E-value: 3.10e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  10 WLSF-SDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNR----EQG--LDDGRIIYEQDLIVAR-----LQQDPpr 77
Cdd:cd03254   9 NFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRfydpQKGqiLIDGIDIRDISRKSLRsmigvVLQDT-- 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  78 nvegsvYDF---VAEGIeeqaeylkryhdisRLVMNDPSEKNLNELAKvQEQLdHHNLWQLENRINEVLAQLGldpnval 154
Cdd:cd03254  87 ------FLFsgtIMENI--------------RLGRPNATDEEVIEAAK-EAGA-HDFIMKLPNGYDTVLGENG------- 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 155 SSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWL-EGFLKTFNG-TIIFISHDRSFIRNmATRIVDLDRGKLV 232
Cdd:cd03254 138 GNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIqEALEKLMKGrTSIIIAHRLSTIKN-ADKILVLDDGKII 216
                       250
                ....*....|...
gi 15830287 233 TyPGNYDQyLLEK 245
Cdd:cd03254 217 E-EGTHDE-LLAK 227
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
15-255 3.72e-17

ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.


Pssm-ID: 213219 [Multi-domain]  Cd Length: 237  Bit Score: 81.38  E-value: 3.72e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  15 DAPL-LDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYE-QDLIVArlqqDPP---RNVegsvydfvae 89
Cdd:cd03252  13 DGPViLDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDgHDLALA----DPAwlrRQV---------- 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  90 GIEEQAEYLKRYHDISRLVMNDP--SEKNLNELAKVQEQldHHNLWQLENRINEVLAQLGldpnvalSSLSGGWLRKAAL 167
Cdd:cd03252  79 GVVLQENVLFNRSIRDNIALADPgmSMERVIEAAKLAGA--HDFISELPEGYDTIVGEQG-------AGLSGGQRQRIAI 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 168 GRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTF--NGTIIFISHDRSFIRNmATRIVDLDRGKLVTyPGNYDQYLLEK 245
Cdd:cd03252 150 ARALIHNPRILIFDEATSALDYESEHAIMRNMHDIcaGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVE-QGSHDELLAEN 227
                       250
                ....*....|
gi 15830287 246 EEALRVEELQ 255
Cdd:cd03252 228 GLYAYLYQLQ 237
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
3-473 4.00e-17

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 84.84  E-value: 4.00e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287    3 LISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIiyeqdlivarlqqdpprNVEGS 82
Cdd:PRK09700   5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTI-----------------TINNI 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   83 VYDFVAEGIEEQAEYLKRYHDISrlVMNDPS-EKNL---NELAKVQEQLDHHNLWQLENRINEVLAQLGL--DPNVALSS 156
Cdd:PRK09700  68 NYNKLDHKLAAQLGIGIIYQELS--VIDELTvLENLyigRHLTKKVCGVNIIDWREMRVRAAMMLLRVGLkvDLDEKVAN 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  157 LSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGF---LKTFNGTIIFISHDRSFIRNMATRIVDLDRGklvT 233
Cdd:PRK09700 146 LSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLImnqLRKEGTAIVYISHKLAEIRRICDRYTVMKDG---S 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  234 YPGNYDqyllekeealrVEELQNAEFDRKLAQEEvwirqgIKARRTRNEGRVRALkamrrergerrevmgtakmqveeas 313
Cdd:PRK09700 223 SVCSGM-----------VSDVSNDDIVRLMVGRE------LQNRFNAMKENVSNL------------------------- 260
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  314 rSGKIVFEMEDVCYQVDGKqlVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV-GTKLE--------- 383
Cdd:PRK09700 261 -AHETVFEVRNVTSRDRKK--VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLnGKDISprspldavk 337
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  384 --VAYFDQHRAE--LDPDKTVMDNLAEGKQevMVNGKPRHVLGylqdfLFHPK---------RAMTPVRA---------L 441
Cdd:PRK09700 338 kgMAYITESRRDngFFPNFSIAQNMAISRS--LKDGGYKGAMG-----LFHEVdeqrtaenqRELLALKChsvnqniteL 410
                        490       500       510
                 ....*....|....*....|....*....|..
gi 15830287  442 SGGERNRLLLARLFLKPSNLLILDEPTNDLDV 473
Cdd:PRK09700 411 SGGNQQKVLISKWLCCCPEVIIFDEPTRGIDV 442
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
321-495 4.38e-17

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


Pssm-ID: 273491 [Multi-domain]  Cd Length: 198  Bit Score: 80.10  E-value: 4.38e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   321 EMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTK---------LEVAYFDQHR 391
Cdd:TIGR01189   2 AARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTplaeqrdepHENILYLGHL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   392 AELDPDKTVMDNLAEGkqevmvngkpRHVLGYLQDFLFHPKRAM-------TPVRALSGGERNRLLLARLFLKPSNLLIL 464
Cdd:TIGR01189  82 PGLKPELSALENLHFW----------AAIHGGAQRTIEDALAAVgltgfedLPAAQLSAGQQRRLALARLWLSRRPLWIL 151
                         170       180       190
                  ....*....|....*....|....*....|....
gi 15830287   465 DEPTNDLDVETLELLEELIDSY---QGTVLLVSH 495
Cdd:TIGR01189 152 DEPTTALDKAGVALLAGLLRAHlarGGIVLLTTH 185
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
28-234 4.55e-17

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


Pssm-ID: 213264 [Multi-domain]  Cd Length: 214  Bit Score: 80.42  E-value: 4.55e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  28 DNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIyeqdlivarlqqdpprnVEGSVYDfvaegieeqaeylkryhDiSRL 107
Cdd:cd03297  22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIV-----------------LNGTVLF-----------------D-SRK 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 108 VMNDPSEK--------------NLNELAKVQEQLDHHNLWQLENRINEVLAQLGLDP--NVALSSLSGGWLRKAALGRAL 171
Cdd:cd03297  67 KINLPPQQrkiglvfqqyalfpHLNVRENLAFGLKRKRNREDRISVDELLDLLGLDHllNRYPAQLSGGEKQRVALARAL 146
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15830287 172 VSNPRVLLLDEPTNHLDIETIDWLEGFL----KTFNGTIIFISHDRSFIRNMATRIVDLDRGKLVTY 234
Cdd:cd03297 147 AAQPELLLLDEPFSALDRALRLQLLPELkqikKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYI 213
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
10-232 5.45e-17

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: 79.52  E-value: 5.45e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  10 WLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNreqglddGRIIYEQdlivarlqqdpprnVEGSVYdfvae 89
Cdd:cd03213  16 SPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALA-------GRRTGLG--------------VSGEVL----- 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  90 gIEEQAEYLKRYHDISRLVMndpseknlnelakvQEQLDHHNLWQLENrinevlaqlgLDPNVALSSLSGGWLRKAALGR 169
Cdd:cd03213  70 -INGRPLDKRSFRKIIGYVP--------------QDDILHPTLTVRET----------LMFAAKLRGLSGGERKRVSIAL 124
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15830287 170 ALVSNPRVLLLDEPTNHLDIET----IDWLEGFLKTfNGTIIFISHD-RSFIRNMATRIVDLDRGKLV 232
Cdd:cd03213 125 ELVSNPSLLFLDEPTSGLDSSSalqvMSLLRRLADT-GRTIICSIHQpSSEIFELFDKLLLLSQGRVI 191
PRK13543 PRK13543
heme ABC exporter ATP-binding protein CcmA;
345-495 5.73e-17

heme ABC exporter ATP-binding protein CcmA;


Pssm-ID: 184129 [Multi-domain]  Cd Length: 214  Bit Score: 79.89  E-value: 5.73e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  345 GDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTK--------LEVAYFDqHRAELDPDKTVMDNLaegkqevmvngk 416
Cdd:PRK13543  37 GEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKtatrgdrsRFMAYLG-HLPGLKADLSTLENL------------ 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  417 prHVLGYLQDFlfHPKR--------------AMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEEL 482
Cdd:PRK13543 104 --HFLCGLHGR--RAKQmpgsalaivglagyEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRM 179
                        170
                 ....*....|....*.
gi 15830287  483 IDSY---QGTVLLVSH 495
Cdd:PRK13543 180 ISAHlrgGGAALVTTH 195
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
22-287 6.59e-17

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: 82.47  E-value: 6.59e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287    22 AELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLIV---ARLQQDPPRNVEGSVYD----FVAEGIEEQ 94
Cdd:TIGR02142  16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFdsrKGIFLPPEKRRIGYVFQearlFPHLSVRGN 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287    95 AEY-LKRyhdisrlvmNDPSEKNLNElakvqeqldhhnlwqlenriNEVLAQLGLDPNVA--LSSLSGGWLRKAALGRAL 171
Cdd:TIGR02142  96 LRYgMKR---------ARPSERRISF--------------------ERVIELLGIGHLLGrlPGRLSGGEKQRVAIGRAL 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   172 VSNPRVLLLDEPTNHLDI----ETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKlVTYPGNYDQY------ 241
Cdd:TIGR02142 147 LSSPRLLLMDEPLAALDDprkyEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGR-VAAAGPIAEVwaspdl 225
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 15830287   242 -LLEKEEALRVEELQNAEFDRK-------LAQEEVWIRQGIKARRTRNEGRVRA 287
Cdd:TIGR02142 226 pWLAREDQGSLIEGVVAEHDQHygltalrLGGGHLWVPENLGPTGARLRLRVPA 279
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
15-232 7.21e-17

lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]


Pssm-ID: 131258 [Multi-domain]  Cd Length: 571  Bit Score: 84.00  E-value: 7.21e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287    15 DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYE----QDLIVARLqqdppRN----VEGSVY-- 84
Cdd:TIGR02203 344 DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDghdlADYTLASL-----RRqvalVSQDVVlf 418
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287    85 -DFVAEGIeeqaeylkRYHDISRLVMndpseknlnelAKVQEQLDHHNLWQLENRInevlaQLGLDPNVAL--SSLSGGW 161
Cdd:TIGR02203 419 nDTIANNI--------AYGRTEQADR-----------AEIERALAAAYAQDFVDKL-----PLGLDTPIGEngVLLSGGQ 474
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15830287   162 LRKAALGRALVSNPRVLLLDEPTNHLDIET----IDWLEGFLKtfNGTIIFISHDRSFIRNmATRIVDLDRGKLV 232
Cdd:TIGR02203 475 RQRLAIARALLKDAPILILDEATSALDNESerlvQAALERLMQ--GRTTLVIAHRLSTIEK-ADRIVVMDDGRIV 546
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
34-501 8.14e-17

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: 84.07  E-value: 8.14e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  34 LVGRNGAGKSTLMKILNreqglddGRII-----YEqdlivarlqqDPPRnvegsvYDFVAE---GIEEQaEYLKR----- 100
Cdd:COG1245 104 ILGPNGIGKSTALKILS-------GELKpnlgdYD----------EEPS------WDEVLKrfrGTELQ-DYFKKlange 159
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 101 --------YHD-ISRLVMNDPSEknLneLAKVQEqldhhnlwqlENRINEVLAQLGLDP--NVALSSLSGGWLRKAALGR 169
Cdd:COG1245 160 ikvahkpqYVDlIPKVFKGTVRE--L--LEKVDE----------RGKLDELAEKLGLENilDRDISELSGGELQRVAIAA 225
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 170 ALVSNPRVLLLDEPTNHLDI-------ETIDWLEGFLKTfngtIIFISHDRSFIRNMATRIVdldrgklVTY--PGNY-- 238
Cdd:COG1245 226 ALLRDADFYFFDEPSSYLDIyqrlnvaRLIRELAEEGKY----VLVVEHDLAILDYLADYVH-------ILYgePGVYgv 294
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 239 -----------DQYL---LeKEEALRVeelqnaefdrklaqeevwirqgikaRRTRNEGRVRALkamrrergerrevmgt 304
Cdd:COG1245 295 vskpksvrvgiNQYLdgyL-PEENVRI-------------------------RDEPIEFEVHAP---------------- 332
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 305 akmqveEASRSGKIVFEMEDVCYQVDGKQLVKDfSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHvgTKLEV 384
Cdd:COG1245 333 ------RREKEEETLVEYPDLTKSYGGFSLEVE-GGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVD--EDLKI 403
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 385 AYFDQhRAELDPDKTVMDNLAEgkqevmVNGKPrhvLG--YLQDFLFHP---KRAMT-PVRALSGGERNRLLLARLFLKP 458
Cdd:COG1245 404 SYKPQ-YISPDYDGTVEEFLRS------ANTDD---FGssYYKTEIIKPlglEKLLDkNVKDLSGGELQRVAIAACLSRD 473
                       490       500       510       520
                ....*....|....*....|....*....|....*....|....*..
gi 15830287 459 SNLLILDEPTNDLDVETLELLEELI----DSYQGTVLLVSHDRQFVD 501
Cdd:COG1245 474 ADLYLLDEPSAHLDVEQRLAVAKAIrrfaENRGKTAMVVDHDIYLID 520
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
332-500 9.29e-17

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 80.16  E-value: 9.29e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  332 KQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKLEVAYFDQhRAELDPD-----KTVMDNLAE 406
Cdd:PRK09544  17 RRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQ-KLYLDTTlpltvNRFLRLRPG 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  407 GKQEVMVNGKPRHVLGYLQDFlfhpkramtPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELIDSY 486
Cdd:PRK09544  96 TKKEDILPALKRVQAGHLIDA---------PMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQL 166
                        170
                 ....*....|....*...
gi 15830287  487 QGT----VLLVSHDRQFV 500
Cdd:PRK09544 167 RREldcaVLMVSHDLHLV 184
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
17-246 1.13e-16

ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213218 [Multi-domain]  Cd Length: 234  Bit Score: 79.58  E-value: 1.13e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  17 PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYE----QDLIVARLqqdppRN----VEGSVYDFvA 88
Cdd:cd03251  16 PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDghdvRDYTLASL-----RRqiglVSQDVFLF-N 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  89 EGIEEQAEYLKRyhdisrlvmnDPSEKNLNELAKVQEQldHHNLWQLENRINEVLAQLGldpnvalSSLSGGWLRKAALG 168
Cdd:cd03251  90 DTVAENIAYGRP----------GATREEVEEAARAANA--HEFIMELPEGYDTVIGERG-------VKLSGGQRQRIAIA 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 169 RALVSNPRVLLLDEPTNHLDIET----IDWLEGFLKtfNGTIIFISHDRSFIRNmATRIVDLDRGKLVTYpGNYDQyLLE 244
Cdd:cd03251 151 RALLKDPPILILDEATSALDTESerlvQAALERLMK--NRTTFVIAHRLSTIEN-ADRIVVLEDGKIVER-GTHEE-LLA 225

                ..
gi 15830287 245 KE 246
Cdd:cd03251 226 QG 227
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
4-226 1.22e-16

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: 83.10  E-value: 1.22e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287     4 ISMHGAWLSFSDA-PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRI-IYEQDLI----------VARL 71
Cdd:TIGR02857 322 LEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIaVNGVPLAdadadswrdqIAWV 401
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287    72 QQDPprnveGSVYDFVAEGIeeqaeylkryhdisRLVMNDPSEknlnelAKVQEQLDHHNLWQLENRINEVLA-QLGLDP 150
Cdd:TIGR02857 402 PQHP-----FLFAGTIAENI--------------RLARPDASD------AEIREALERAGLDEFVAALPQGLDtPIGEGG 456
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15830287   151 nvalSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIET-IDWLEGFLKTFNG-TIIFISHDRSFIRNmATRIVDL 226
Cdd:TIGR02857 457 ----AGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETeAEVLEALRALAQGrTVLLVTHRLALAAL-ADRIVVL 529
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
4-231 1.50e-16

ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.


Pssm-ID: 213229 [Multi-domain]  Cd Length: 213  Bit Score: 78.73  E-value: 1.50e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   4 ISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIyeqdlivarlqqdpprnVEGSV 83
Cdd:cd03262   1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTII-----------------IDGLK 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  84 YDFvaegieeqaeylkryhdisrlvmndpSEKNLNEL-AKVQEQLDHHNLWQ----LEN------------------RIN 140
Cdd:cd03262  64 LTD--------------------------DKKNINELrQKVGMVFQQFNLFPhltvLENitlapikvkgmskaeaeeRAL 117
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 141 EVLAQLGLDP--NVALSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTF---NGTIIFISHDRSF 215
Cdd:cd03262 118 ELLEKVGLADkaDAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLaeeGMTMVVVTHEMGF 197
                       250
                ....*....|....*.
gi 15830287 216 IRNMATRIVDLDRGKL 231
Cdd:cd03262 198 AREVADRVIFMDDGRI 213
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
320-495 1.81e-16

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: 77.19  E-value: 1.81e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 320 FEMEDVCYQV-DGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKLEVAYFDQhraeldpdk 398
Cdd:cd03223   1 IELENLSLATpDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLFLPQ--------- 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 399 tvmdnlaegkqevmvngKPRHVLGYLQDFLFHPKRamtpvRALSGGERNRLLLARLFL-KPSnLLILDEPTNDLDVETLE 477
Cdd:cd03223  72 -----------------RPYLPLGTLREQLIYPWD-----DVLSGGEQQRLAFARLLLhKPK-FVFLDEATSALDEESED 128
                       170
                ....*....|....*...
gi 15830287 478 LLEELIDSYQGTVLLVSH 495
Cdd:cd03223 129 RLYQLLKELGITVISVGH 146
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
320-498 1.98e-16

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: 78.76  E-value: 1.98e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 320 FEMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGtklEVAYFDQHRAELDPD-- 397
Cdd:cd03260   1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDEG---EVLLDGKDIYDLDVDvl 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 398 -----------------KTVMDNLAEGKQevmVNG-KPRHVLGYLqdflfhPKRAMTPV------------RALSGGERN 447
Cdd:cd03260  78 elrrrvgmvfqkpnpfpGSIYDNVAYGLR---LHGiKLKEELDER------VEEALRKAalwdevkdrlhaLGLSGGQQQ 148
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 15830287 448 RLLLAR-LFLKPSNLLiLDEPTNDLDVETLELLEELIDSYQG--TVLLVSHDRQ 498
Cdd:cd03260 149 RLCLARaLANEPEVLL-LDEPTSALDPISTAKIEELIAELKKeyTIVIVTHNMQ 201
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
3-232 2.12e-16

ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 78.88  E-value: 2.12e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   3 LISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLIvarlqqdpprnvegs 82
Cdd:COG1126   1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDL--------------- 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  83 vydfvaegieeqaeylkryhdisrlvmnDPSEKNLNEL-AKV----QeqldHHNLWQ----LEN---------------- 137
Cdd:COG1126  66 ----------------------------TDSKKDINKLrRKVgmvfQ----QFNLFPhltvLENvtlapikvkkmskaea 113
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 138 --RINEVLAQLGLD------PnvalSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTF--NG-TI 206
Cdd:COG1126 114 eeRAMELLERVGLAdkadayP----AQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLakEGmTM 189
                       250       260
                ....*....|....*....|....*.
gi 15830287 207 IFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:COG1126 190 VVVTHEMGFAREVADRVVFMDGGRIV 215
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
338-496 2.54e-16

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 78.82  E-value: 2.54e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  338 FSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQAdSGRIHV-GTKLE---VAYFDQHRAEL---DPDKTVMD---NLAEG 407
Cdd:PRK03695  15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFaGQPLEawsAAELARHRAYLsqqQTPPFAMPvfqYLTLH 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  408 KQEVMVNGKPRHVLGYLQDFLFHPKRAMTPVRALSGGERNRLLLARLFLK------P-SNLLILDEPTNDLDVETLELLE 480
Cdd:PRK03695  94 QPDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinPaGQLLLLDEPMNSLDVAQQAALD 173
                        170
                 ....*....|....*....
gi 15830287  481 ELID--SYQG-TVLLVSHD 496
Cdd:PRK03695 174 RLLSelCQQGiAVVMSSHD 192
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
1-232 2.72e-16

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 79.35  E-value: 2.72e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287    1 MSLISMHGAWLSFSDAPL---------LDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYeQDLIVARL 71
Cdd:PRK10419   1 MTLLNVSGLSHHYAHGGLsgkhqhqtvLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSW-RGEPLAKL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   72 QQdpprnvegsvydfvaegieEQAEYLKRyhDIsRLVMND-PSEKNLNEL--AKVQEQLDHhnLWQL-----ENRINEVL 143
Cdd:PRK10419  80 NR-------------------AQRKAFRR--DI-QMVFQDsISAVNPRKTvrEIIREPLRH--LLSLdkaerLARASEML 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  144 AQLGLDPNVA---LSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDI----ETIDWLEGFLKTFNGTIIFISHDRSFI 216
Cdd:PRK10419 136 RAVDLDDSVLdkrPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLvlqaGVIRLLKKLQQQFGTACLFITHDLRLV 215
                        250
                 ....*....|....*.
gi 15830287  217 RNMATRIVDLDRGKLV 232
Cdd:PRK10419 216 ERFCQRVMVMDNGQIV 231
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
19-234 2.82e-16

ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.


Pssm-ID: 213230 [Multi-domain]  Cd Length: 220  Bit Score: 78.32  E-value: 2.82e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEqDLIVARLQQDPPRNVegsvydfvaeGIEEQaeyl 98
Cdd:cd03263  18 VDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYIN-GYSIRTDRKAARQSL----------GYCPQ---- 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  99 kryHDIsrlvmNDPsekNLN--ELAKVQEQLDHHNLWQLENRINEVLAQLGLDP--NVALSSLSGGWLRKAALGRALVSN 174
Cdd:cd03263  83 ---FDA-----LFD---ELTvrEHLRFYARLKGLPKSEIKEEVELLLRVLGLTDkaNKRARTLSGGMKRKLSLAIALIGG 151
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15830287 175 PRVLLLDEPTNHLDI-------ETIDWLEGflktfNGTIIFISHDRSFIRNMATRIVDLDRGKLVTY 234
Cdd:cd03263 152 PSVLLLDEPTSGLDPasrraiwDLILEVRK-----GRSIILTTHSMDEAEALCDRIAIMSDGKLRCI 213
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
17-229 4.26e-16

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: 77.86  E-value: 4.26e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  17 PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLIVARLQQDPPRNVE-------GSV------ 83
Cdd:COG4778  25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWVDLAQASPREILalrrrtiGYVsqflrv 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  84 ------YDFVAEGIEEQAEylkryhdisrlvmnDPSEKnlneLAKVQEQLDHHN----LWQLenrinevlaqlgldpnvA 153
Cdd:COG4778 105 iprvsaLDVVAEPLLERGV--------------DREEA----RARARELLARLNlperLWDL-----------------P 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 154 LSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIET----IDWLEGfLKTFNGTIIFISHDRSFIRNMATRIVDLDRG 229
Cdd:COG4778 150 PATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANravvVELIEE-AKARGTAIIGIFHDEEVREAVADRVVDVTPF 228
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
318-472 4.43e-16

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 78.27  E-value: 4.43e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  318 IVFEMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTK-------LEVAyfdQH 390
Cdd:PRK13548   1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRpladwspAELA---RR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  391 RAELdPDKTVMdNLAEGKQEVMVNGKPRHVLGYLQDFLfHPKRAMTPV----------RALSGGERNRLLLARLFL---- 456
Cdd:PRK13548  78 RAVL-PQHSSL-SFPFTVEEVVAMGRAPHGLSRAEDDA-LVAAALAQVdlahlagrdyPQLSGGEQQRVQLARVLAqlwe 154
                        170
                 ....*....|....*...
gi 15830287  457 --KPSNLLILDEPTNDLD 472
Cdd:PRK13548 155 pdGPPRWLLLDEPTSALD 172
nickel_nikE TIGR02769
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ...
16-232 4.65e-16

nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 131816 [Multi-domain]  Cd Length: 265  Bit Score: 78.69  E-value: 4.65e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287    16 APLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYE-QDLIvarlQQDPprnvegsvydfvaegieEQ 94
Cdd:TIGR02769  24 APVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRgQDLY----QLDR-----------------KQ 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287    95 AEYLKRyhDISRLVMNDPSEKNLNELAK--VQEQLDHhnLWQL-----ENRINEVLAQLGLDPNVAL---SSLSGGWLRK 164
Cdd:TIGR02769  83 RRAFRR--DVQLVFQDSPSAVNPRMTVRqiIGEPLRH--LTSLdeseqKARIAELLDMVGLRSEDADklpRQLSGGQLQR 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15830287   165 AALGRALVSNPRVLLLDEPTNHLDI----ETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:TIGR02769 159 INIARALAVKPKLIVLDEAVSNLDMvlqaVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIV 230
BtuD COG4138
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ...
338-496 5.25e-16

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


Pssm-ID: 443313 [Multi-domain]  Cd Length: 248  Bit Score: 77.96  E-value: 5.25e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 338 FSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQAdSGRIHV-GTKLE---VAYFDQHRAEL---DPDKTVMD-------N 403
Cdd:COG4138  15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPG-QGEILLnGRPLSdwsAAELARHRAYLsqqQSPPFAMPvfqylalH 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 404 LAEGKQEVMVNGKPRHVLGYLQ--DFLfhpkraMTPVRALSGGERNRLLLARLFLK-------PSNLLILDEPTNDLDVE 474
Cdd:COG4138  94 QPAGASSEAVEQLLAQLAEALGleDKL------SRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSLDVA 167
                       170       180
                ....*....|....*....|....*
gi 15830287 475 TLELLEELIDSY---QGTVLLVSHD 496
Cdd:COG4138 168 QQAALDRLLRELcqqGITVVMSSHD 192
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
321-472 7.42e-16

ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213218 [Multi-domain]  Cd Length: 234  Bit Score: 77.27  E-value: 7.42e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 321 EMEDVC--YQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV-GTKLEVAYFDQHRAEL--- 394
Cdd:cd03251   2 EFKNVTfrYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIdGHDVRDYTLASLRRQIglv 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 395 --DP---DKTVMDNLAEGK-----QEVMVNGKprhvLGYLQDFLFH-PKRAMTPV--RA--LSGGERNRLLLARLFLKPS 459
Cdd:cd03251  82 sqDVflfNDTVAENIAYGRpgatrEEVEEAAR----AANAHEFIMElPEGYDTVIgeRGvkLSGGQRQRIAIARALLKDP 157
                       170
                ....*....|...
gi 15830287 460 NLLILDEPTNDLD 472
Cdd:cd03251 158 PILILDEATSALD 170
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
11-245 8.88e-16

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 80.59  E-value: 8.88e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  11 LSFS---DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRI-IYEQDL-------------IVarlQQ 73
Cdd:COG1132 345 VSFSypgDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRIlIDGVDIrdltleslrrqigVV---PQ 421
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  74 DPPRnVEGSVYDFVAEGIEeqaeylkryhDISRlvmndpseknlnelAKVQEQLDHHNLW----QLENRINEVLAQLGld 149
Cdd:COG1132 422 DTFL-FSGTIRENIRYGRP----------DATD--------------EEVEEAAKAAQAHefieALPDGYDTVVGERG-- 474
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 150 pnvalSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIET----IDWLEGFLKtfNGTIIFISHDRSFIRNmATRIVD 225
Cdd:COG1132 475 -----VNLSGGQRQRIAIARALLKDPPILILDEATSALDTETealiQEALERLMK--GRTTIVIAHRLSTIRN-ADRILV 546
                       250       260
                ....*....|....*....|
gi 15830287 226 LDRGKLVTYpGNYDQyLLEK 245
Cdd:COG1132 547 LDDGRIVEQ-GTHEE-LLAR 564
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
321-503 9.77e-16

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: 76.29  E-value: 9.77e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 321 EMEDVCYQVDGKQL-VKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV-GTKL------EVAYFDQHRA 392
Cdd:cd03292   2 EFINVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVnGQDVsdlrgrAIPYLRRKIG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 393 ------ELDPDKTVMDNLAEGKQEVMVNGK--PRHVLGYLQDF-LFHPKRAMTpvRALSGGERNRLLLARLFLKPSNLLI 463
Cdd:cd03292  82 vvfqdfRLLPDRNVYENVAFALEVTGVPPReiRKRVPAALELVgLSHKHRALP--AELSGGEQQRVAIARAIVNSPTILI 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 15830287 464 LDEPTNDLDVETLELLEELIDSYQ---GTVLLVSHDRQFVDNT 503
Cdd:cd03292 160 ADEPTGNLDPDTTWEIMNLLKKINkagTTVVVATHAKELVDTT 202
COG4559 COG4559
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
321-473 1.53e-15

ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 443620 [Multi-domain]  Cd Length: 258  Bit Score: 76.69  E-value: 1.53e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 321 EMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVG-------TKLEVAyfdQHRAE 393
Cdd:COG4559   3 EAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNgrplaawSPWELA---RRRAV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 394 LdPDKTVMdNLAEGKQEVMVNGKPRHVLGYLQDfLFHPKRAMTPV----------RALSGGERNRLLLARLFL------- 456
Cdd:COG4559  80 L-PQHSSL-AFPFTVEEVVALGRAPHGSSAAQD-RQIVREALALVglahlagrsyQTLSGGEQQRVQLARVLAqlwepvd 156
                       170
                ....*....|....*..
gi 15830287 457 KPSNLLILDEPTNDLDV 473
Cdd:COG4559 157 GGPRWLFLDEPTSALDL 173
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
15-232 1.59e-15

ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.


Pssm-ID: 213191 [Multi-domain]  Cd Length: 222  Bit Score: 75.93  E-value: 1.59e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  15 DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILnreQGL---DDGRIIYE-QDLIVARLQQdppRNVEGSVYdfVAEG 90
Cdd:cd03224  12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTI---MGLlppRSGSIRFDgRDITGLPPHE---RARAGIGY--VPEG 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  91 ieeqaeylkryhdisRLVMNDPS-EKNL------NELAKVQEQLDHhnLWQLENRINEVLAQLGldpnvalSSLSGGWLR 163
Cdd:cd03224  84 ---------------RRIFPELTvEENLllgayaRRRAKRKARLER--VYELFPRLKERRKQLA-------GTLSGGEQQ 139
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15830287 164 KAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFNG---TIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:cd03224 140 MLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDegvTILLVEQNARFALEIADRAYVLERGRVV 211
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
321-495 1.66e-15

ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213220 [Multi-domain]  Cd Length: 236  Bit Score: 76.50  E-value: 1.66e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 321 EMEDVCYQVD-GKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVG----TKLEVAYFDQHRAELD 395
Cdd:cd03253   2 EFENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDgqdiREVTLDSLRRAIGVVP 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 396 PD-----KTVMDNLAEGK-----QEVMVNGKPRHVLGYLQDFlfhPKRAMTPV--RA--LSGGERNRLLLARLFLKPSNL 461
Cdd:cd03253  82 QDtvlfnDTIGYNIRYGRpdatdEEVIEAAKAAQIHDKIMRF---PDGYDTIVgeRGlkLSGGEKQRVAIARAILKNPPI 158
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 15830287 462 LILDEPTNDLDVETLELLEELIDSYQG--TVLLVSH 495
Cdd:cd03253 159 LLLDEATSALDTHTEREIQAALRDVSKgrTTIVIAH 194
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
324-496 1.87e-15

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: 75.79  E-value: 1.87e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 324 DVCYQVDGKQlvKDFSAQV---LRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVG---------------TKLEVA 385
Cdd:cd03297   1 MLCVDIEKRL--PDFTLKIdfdLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNgtvlfdsrkkinlppQQRKIG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 386 YFDQHRAeLDPDKTVMDNLAEGKQEVMVNGK---PRHVLGYLQdfLFHPKRAmtPVRALSGGERNRLLLARLFLKPSNLL 462
Cdd:cd03297  79 LVFQQYA-LFPHLNVRENLAFGLKRKRNREDrisVDELLDLLG--LDHLLNR--YPAQLSGGEKQRVALARALAAQPELL 153
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 15830287 463 ILDEPTNDLDVETLELLEELIDS----YQGTVLLVSHD 496
Cdd:cd03297 154 LLDEPFSALDRALRLQLLPELKQikknLNIPVIFVTHD 191
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
316-472 1.91e-15

lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]


Pssm-ID: 131258 [Multi-domain]  Cd Length: 571  Bit Score: 79.76  E-value: 1.91e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   316 GKIVFEMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV-GTKLEVAYFDQHRAEL 394
Cdd:TIGR02203 329 GDVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLdGHDLADYTLASLRRQV 408
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   395 DP--------DKTVMDNLAEGKQEVMVNGKPRHVL--GYLQDFLFH-PKRAMTPVRA----LSGGERNRLLLARLFLKPS 459
Cdd:TIGR02203 409 ALvsqdvvlfNDTIANNIAYGRTEQADRAEIERALaaAYAQDFVDKlPLGLDTPIGEngvlLSGGQRQRLAIARALLKDA 488
                         170
                  ....*....|...
gi 15830287   460 NLLILDEPTNDLD 472
Cdd:TIGR02203 489 PILILDEATSALD 501
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
317-472 2.11e-15

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: 74.89  E-value: 2.11e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 317 KIVFEMEDVCYQVDG------KQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQL--QADSGrihvgtklevayfd 388
Cdd:cd03213   1 GVTLSFRNLTVTVKSspsksgKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRtgLGVSG-------------- 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 389 qhraeldpdktvmdnlaegkqEVMVNGKPRH------VLGY-LQDFLFHPKraMTP---------VRALSGGERNRLLLA 452
Cdd:cd03213  67 ---------------------EVLINGRPLDkrsfrkIIGYvPQDDILHPT--LTVretlmfaakLRGLSGGERKRVSIA 123
                       170       180
                ....*....|....*....|.
gi 15830287 453 R-LFLKPSnLLILDEPTNDLD 472
Cdd:cd03213 124 LeLVSNPS-LLFLDEPTSGLD 143
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
1-237 3.53e-15

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 77.38  E-value: 3.53e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287    1 MSLISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILnreQGLDDgriIYEQDLIVA--RLQQDPP-- 76
Cdd:PRK11000   1 MASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMI---AGLED---ITSGDLFIGekRMNDVPPae 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   77 RNVeGSVYdfvaegiEEQAEY--LKRYHDIS---RLVMNDPSE--KNLNELAKVQeQLDHhnlwQLENRinevlaqlgld 149
Cdd:PRK11000  75 RGV-GMVF-------QSYALYphLSVAENMSfglKLAGAKKEEinQRVNQVAEVL-QLAH----LLDRK----------- 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  150 PNvalsSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLD--------IEtIDWLEgflKTFNGTIIFISHDRSFIRNMAT 221
Cdd:PRK11000 131 PK----ALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDaalrvqmrIE-ISRLH---KRLGRTMIYVTHDQVEAMTLAD 202
                        250       260
                 ....*....|....*....|....*
gi 15830287  222 RIVDLDRGK---------LVTYPGN 237
Cdd:PRK11000 203 KIVVLDAGRvaqvgkpleLYHYPAN 227
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
319-473 3.60e-15

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 74.53  E-value: 3.60e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  319 VFEMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI-------HVGTKLEVAYFDQHR 391
Cdd:PRK13539   2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIkldggdiDDPDVAEACHYLGHR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  392 AELDPDKTVMDNLaEGKQEVMvNGKPRHVLGYLQDF----LFHpkramTPVRALSGGERNRLLLARLFLKPSNLLILDEP 467
Cdd:PRK13539  82 NAMKPALTVAENL-EFWAAFL-GGEELDIAAALEAVglapLAH-----LPFGYLSAGQKRRVALARLLVSNRPIWILDEP 154

                 ....*.
gi 15830287  468 TNDLDV 473
Cdd:PRK13539 155 TAALDA 160
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
4-234 5.12e-15

ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213236 [Multi-domain]  Cd Length: 210  Bit Score: 74.24  E-value: 5.12e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   4 ISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIyeqdlivarlqqdpprnVEGSV 83
Cdd:cd03269   1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVL-----------------FDGKP 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  84 YDFVAegieeqaeylkrYHDISRLvmndPSEKNLNELAKVQEQLDHhnLWQLEN--------RINEVLAQLGLDP--NVA 153
Cdd:cd03269  64 LDIAA------------RNRIGYL----PEERGLYPKMKVIDQLVY--LAQLKGlkkeearrRIDEWLERLELSEyaNKR 125
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 154 LSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGF---LKTFNGTIIFISHDRSFIRNMATRIVDLDRGK 230
Cdd:cd03269 126 VEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVireLARAGKTVILSTHQMELVEELCDRVLLLNKGR 205

                ....
gi 15830287 231 LVTY 234
Cdd:cd03269 206 AVLY 209
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
321-497 5.70e-15

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 76.68  E-value: 5.70e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 321 EMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVG----TKLE-----VAYFDQHR 391
Cdd:COG3842   7 ELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDgrdvTGLPpekrnVGMVFQDY 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 392 AeLDPDKTVMDNLAEG-------KQEV---------MVNgkprhvlgyLQDFLfhpKRAmtpVRALSGGERNRLLLAR-L 454
Cdd:COG3842  87 A-LFPHLTVAENVAFGlrmrgvpKAEIrarvaelleLVG---------LEGLA---DRY---PHQLSGGQQQRVALARaL 150
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 15830287 455 FLKPSnLLILDEPTNDLDVETLELLEELIDSYQ----GTVLLVSHDR 497
Cdd:COG3842 151 APEPR-VLLLDEPLSALDAKLREEMREELRRLQrelgITFIYVTHDQ 196
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
335-496 5.84e-15

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


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 76.28  E-value: 5.84e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 335 VKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVG----TKLEVAY-------FDQhRAELDPDKTVMDN 403
Cdd:COG4586  38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLgyvpFKRRKEFarrigvvFGQ-RSQLWWDLPAIDS 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 404 L-----------AEGKQ--EVMVNgkprhVLGyLQDFLfhpkraMTPVRALSGGERNRL-LLARLFLKPSnLLILDEPTN 469
Cdd:COG4586 117 FrllkaiyripdAEYKKrlDELVE-----LLD-LGELL------DTPVRQLSLGQRMRCeLAAALLHRPK-ILFLDEPTI 183
                       170       180       190
                ....*....|....*....|....*....|.
gi 15830287 470 DLDVETLELLEELI----DSYQGTVLLVSHD 496
Cdd:COG4586 184 GLDVVSKEAIREFLkeynRERGTTILLTSHD 214
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
323-497 6.43e-15

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


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 76.34  E-value: 6.43e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 323 EDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTklEVAYFD------------QH 390
Cdd:COG1118   6 RNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNG--RDLFTNlpprerrvgfvfQH 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 391 RAeLDPDKTVMDNLAEGKQevmVNGKPRH-----VLGYLQdfLFH--------PKRamtpvraLSGGERNRLLLAR-LFL 456
Cdd:COG1118  84 YA-LFPHMTVAENIAFGLR---VRPPSKAeirarVEELLE--LVQlegladryPSQ-------LSGGQRQRVALARaLAV 150
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 15830287 457 KPSnLLILDEPTNDLDVETLELL----EELIDSYQGTVLLVSHDR 497
Cdd:COG1118 151 EPE-VLLLDEPFGALDAKVRKELrrwlRRLHDELGGTTVFVTHDQ 194
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
321-496 6.78e-15

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: 74.33  E-value: 6.78e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 321 EMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV----------GTKLEVAYFDQH 390
Cdd:cd03265   2 EVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVaghdvvreprEVRRRIGIVFQD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 391 RAeLDPDKTVMDNLA-EGKQEVMVNGKPRHVLGYLQDFLFHPKRAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTN 469
Cdd:cd03265  82 LS-VDDELTGWENLYiHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
                       170       180       190
                ....*....|....*....|....*....|.
gi 15830287 470 DLDVETLELLEELI----DSYQGTVLLVSHD 496
Cdd:cd03265 161 GLDPQTRAHVWEYIeklkEEFGMTILLTTHY 191
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
323-496 7.09e-15

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 74.41  E-value: 7.09e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 323 EDVCYQVDGKQLvkDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVG----TKLEVA------YFDQHra 392
Cdd:COG3840   5 DDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNgqdlTALPPAerpvsmLFQEN-- 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 393 ELDPDKTVMDNLAEG-----------KQEVM-----VNgkprhvLGYLQDFLfhpkramtPvRALSGGERNRLLLARLFL 456
Cdd:COG3840  81 NLFPHLTVAQNIGLGlrpglkltaeqRAQVEqalerVG------LAGLLDRL--------P-GQLSGGQRQRVALARCLV 145
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 15830287 457 KPSNLLILDEPTNDLDVETLELLEELID----SYQGTVLLVSHD 496
Cdd:COG3840 146 RKRPILLLDEPFSALDPALRQEMLDLVDelcrERGLTVLMVTHD 189
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
12-250 8.96e-15

Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 77.84  E-value: 8.96e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287    12 SFS-----DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNR------EQGLDDGRII--YEQDLI---VARLQQDP 75
Cdd:TIGR00958 485 SFSypnrpDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNlyqptgGQVLLDGVPLvqYDHHYLhrqVALVGQEP 564
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287    76 PRnVEGSVYDFVAEGieeqaeyLKRYHDisRLVMndpseknlnelAKVQEQLDHHNLWQLENRINEVLAQLGldpnvalS 155
Cdd:TIGR00958 565 VL-FSGSVRENIAYG-------LTDTPD--EEIM-----------AAAKAANAHDFIMEFPNGYDTEVGEKG-------S 616
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   156 SLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIEtIDWLEGFLKTFNG-TIIFISHDRSFIRNmATRIVDLDRGKLVTY 234
Cdd:TIGR00958 617 QLSGGQKQRIAIARALVRKPRVLILDEATSALDAE-CEQLLQESRSRASrTVLLIAHRLSTVER-ADQILVLKKGSVVEM 694
                         250
                  ....*....|....*.
gi 15830287   235 pGNYDQyLLEKEEALR 250
Cdd:TIGR00958 695 -GTHKQ-LMEDQGCYK 708
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
19-232 8.99e-15

ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 75.88  E-value: 8.99e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIY---------EQDLIVAR------------LQQdppR 77
Cdd:COG1135  21 LDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVdgvdltalsERELRAARrkigmifqhfnlLSS---R 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  78 NVegsvYDFVAegieeqaeylkryhdisrLVMndpseknlnELAKVQEQldhhnlwQLENRINEVLAQLGLDP--NVALS 155
Cdd:COG1135  98 TV----AENVA------------------LPL---------EIAGVPKA-------EIRKRVAELLELVGLSDkaDAYPS 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 156 SLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIET---IdwLEgFLKTFNG----TIIFISHDRSFIRNMATRIVDLDR 228
Cdd:COG1135 140 QLSGGQKQRVGIARALANNPKVLLCDEATSALDPETtrsI--LD-LLKDINRelglTIVLITHEMDVVRRICDRVAVLEN 216

                ....
gi 15830287 229 GKLV 232
Cdd:COG1135 217 GRIV 220
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
320-495 9.60e-15

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: 72.08  E-value: 9.60e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 320 FEMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHvgtklevayfdqhraeldpdkt 399
Cdd:cd03216   1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEIL---------------------- 58
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 400 vmdnlaegkqevmVNGKPRHVLGylqdflfhPKRAM----TPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVET 475
Cdd:cd03216  59 -------------VDGKEVSFAS--------PRDARragiAMVYQLSVGERQMVEIARALARNARLLILDEPTAALTPAE 117
                       170       180
                ....*....|....*....|...
gi 15830287 476 LELLEELIDSY--QG-TVLLVSH 495
Cdd:cd03216 118 VERLFKVIRRLraQGvAVIFISH 140
cbiO PRK13637
energy-coupling factor transporter ATPase;
19-232 1.17e-14

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 74.70  E-value: 1.17e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNreqGL---DDGRIIYEQ-DLIVARLQQDPPRNVEGSV-----YDFVAE 89
Cdd:PRK13637  23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLN---GLlkpTSGKIIIDGvDITDKKVKLSDIRKKVGLVfqypeYQLFEE 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   90 GIEEQAEYlkryhdisrlvmnDPSEKNLNELakvqeqldhhnlwQLENRINEVLAQLGLDPNVALS----SLSGGWLRKA 165
Cdd:PRK13637 100 TIEKDIAF-------------GPINLGLSEE-------------EIENRVKRAMNIVGLDYEDYKDkspfELSGGQKRRV 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15830287  166 ALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKT----FNGTIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:PRK13637 154 AIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKElhkeYNMTIILVSHSMEDVAKLADRIIVMNKGKCE 224
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
332-495 1.19e-14

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: 73.08  E-value: 1.19e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 332 KQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV-------GTKLEVAYFDQHRAeLDPDKTVMDNL 404
Cdd:cd03269  13 VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFdgkpldiAARNRIGYLPEERG-LYPKMKVIDQL 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 405 ---AE----GKQEVMvngkpRHVLGYLQDFLFHPKRAmTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLE 477
Cdd:cd03269  92 vylAQlkglKKEEAR-----RRIDEWLERLELSEYAN-KRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVE 165
                       170       180
                ....*....|....*....|.
gi 15830287 478 LLEELIDSYQG---TVLLVSH 495
Cdd:cd03269 166 LLKDVIRELARagkTVILSTH 186
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
15-248 1.39e-14

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 76.98  E-value: 1.39e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   15 DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYE----QDLIVARLqqdppRN----VEGSVY-- 84
Cdd:PRK11176 355 EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDghdlRDYTLASL-----RNqvalVSQNVHlf 429
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   85 -DFVAEGIEEQAEylKRYhdisrlvmndpSEKNLNELAKVQEQLDHHNlwQLENRINEVLAQLGLdpnvalsSLSGGWLR 163
Cdd:PRK11176 430 nDTIANNIAYART--EQY-----------SREQIEEAARMAYAMDFIN--KMDNGLDTVIGENGV-------LLSGGQRQ 487
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  164 KAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTF--NGTIIFISHDRSFIRNmATRIVDLDRGKLVTYpGNYDQy 241
Cdd:PRK11176 488 RIAIARALLRDSPILILDEATSALDTESERAIQAALDELqkNRTSLVIAHRLSTIEK-ADEILVVEDGEIVER-GTHAE- 564

                 ....*..
gi 15830287  242 LLEKEEA 248
Cdd:PRK11176 565 LLAQNGV 571
CeuD COG4604
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ...
4-232 1.41e-14

ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 443654 [Multi-domain]  Cd Length: 252  Bit Score: 73.96  E-value: 1.41e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   4 ISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRI-IYEQDL----------IVARLQ 72
Cdd:COG4604   2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVlVDGLDVattpsrelakRLAILR 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  73 QDPPRNVEGSVYDFVAEGieeqaeylkRY-HDISRLVMNDpseknlneLAKVQEQLDHHNLWQLENRInevlaqlgldpn 151
Cdd:COG4604  82 QENHINSRLTVRELVAFG---------RFpYSKGRLTAED--------REIIDEAIAYLDLEDLADRY------------ 132
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 152 vaLSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDI----ETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLD 227
Cdd:COG4604 133 --LDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMkhsvQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMK 210

                ....*
gi 15830287 228 RGKLV 232
Cdd:COG4604 211 DGRVV 215
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
11-245 1.45e-14

ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]


Pssm-ID: 130261 [Multi-domain]  Cd Length: 708  Bit Score: 77.09  E-value: 1.45e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287    11 LSFS---DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKIL----NREQG--LDDGRIIYEQDLIVAR-----LQQDPp 76
Cdd:TIGR01193 479 VSYSygyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLvgffQARSGeiLLNGFSLKDIDRHTLRqfinyLPQEP- 557
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287    77 RNVEGSVYDFVAEGIEEQAEYlkryHDISRLVmndpseknlnELAKVQEQLDHhnlwqlenrinevlAQLGLDPNVAL-- 154
Cdd:TIGR01193 558 YIFSGSILENLLLGAKENVSQ----DEIWAAC----------EIAEIKDDIEN--------------MPLGYQTELSEeg 609
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   155 SSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIET---IdwLEGFLKTFNGTIIFISHdRSFIRNMATRIVDLDRGKL 231
Cdd:TIGR01193 610 SSISGGQKQRIALARALLTDSKVLILDESTSNLDTITekkI--VNNLLNLQDKTIIFVAH-RLSVAKQSDKIIVLDHGKI 686
                         250
                  ....*....|....
gi 15830287   232 VTyPGNYDQYLLEK 245
Cdd:TIGR01193 687 IE-QGSHDELLDRN 699
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
321-473 1.60e-14

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 76.03  E-value: 1.60e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  321 EMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVG----TKLEVAYFDQHRAELDP 396
Cdd:PRK09536   5 DVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAgddvEALSARAASRRVASVPQ 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  397 DKTVMDNLaEGKQEVMVNGKPrhvlgYLQDFLFHP-------KRAMT----------PVRALSGGERNRLLLARLFLKPS 459
Cdd:PRK09536  85 DTSLSFEF-DVRQVVEMGRTP-----HRSRFDTWTetdraavERAMErtgvaqfadrPVTSLSGGERQRVLLARALAQAT 158
                        170
                 ....*....|....
gi 15830287  460 NLLILDEPTNDLDV 473
Cdd:PRK09536 159 PVLLLDEPTASLDI 172
F420-0_ABC_ATP TIGR03873
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ...
34-232 1.65e-14

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: 73.70  E-value: 1.65e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287    34 LVGRNGAGKSTLMKILNREQGLDDGRIIY-----------EQDLIVARLQQDPPRNVEGSVYDFVAEGieeqaeylkryh 102
Cdd:TIGR03873  32 LLGPNGSGKSTLLRLLAGALRPDAGTVDLagvdlhglsrrARARRVALVEQDSDTAVPLTVRDVVALG------------ 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   103 disrlvmndpseknlnelakvqeQLDHHNLWQLENR-----INEVLAQLGLD--PNVALSSLSGGWLRKAALGRALVSNP 175
Cdd:TIGR03873 100 -----------------------RIPHRSLWAGDSPhdaavVDRALARTELShlADRDMSTLSGGERQRVHVARALAQEP 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   176 RVLLLDEPTNHLDIETIDWLEGFLKTFNG---TIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:TIGR03873 157 KLLLLDEPTNHLDVRAQLETLALVRELAAtgvTVVAALHDLNLAASYCDHVVVLDGGRVV 216
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
19-223 1.71e-14

ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 443658 [Multi-domain]  Cd Length: 329  Bit Score: 74.77  E-value: 1.71e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYE-QDLIVA----------RLQ---QDP-----PRNv 79
Cdd:COG4608  34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDgQDITGLsgrelrplrrRMQmvfQDPyaslnPRM- 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  80 egSVYDFVAEGIEeqaeylkryhdisrlvmndpseknLNELAKVQEQLDhhnlwqlenRINEVLAQLGLDPNVALS---S 156
Cdd:COG4608 113 --TVGDIIAEPLR------------------------IHGLASKAERRE---------RVAELLELVGLRPEHADRyphE 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15830287 157 LSGGWLRKAALGRALVSNPRVLLLDEPTNHLDI----ETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRI 223
Cdd:COG4608 158 FSGGQRQRIGIARALALNPKLIVCDEPVSALDVsiqaQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRV 228
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
12-258 1.73e-14

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 73.59  E-value: 1.73e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   12 SFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGriiyeqDLIVARLQQDPPRNVE-------GSVY 84
Cdd:PRK09493  10 HFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSG------DLIVDGLKVNDPKVDErlirqeaGMVF 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   85 dfvaegieeQAEYLkrYHDISRL--VMNDP------SEKNLNELAKvqeqldhhnlwqlenrinEVLAQLGLDP--NVAL 154
Cdd:PRK09493  84 ---------QQFYL--FPHLTALenVMFGPlrvrgaSKEEAEKQAR------------------ELLAKVGLAEraHHYP 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  155 SSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTF--NG-TIIFISHDRSFIRNMATRIVDLDRGKl 231
Cdd:PRK09493 135 SELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLaeEGmTMVIVTHEIGFAEKVASRLIFIDKGR- 213
                        250       260
                 ....*....|....*....|....*...
gi 15830287  232 VTYPGNYDQyLLEKEEALRVEE-LQNAE 258
Cdd:PRK09493 214 IAEDGDPQV-LIKNPPSQRLQEfLQHVS 240
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
315-497 1.74e-14

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 76.54  E-value: 1.74e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  315 SGKIVFEmeDVCYQVDGK-QLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV-GTKLEvayfDQHRA 392
Cdd:PRK13657 332 KGAVEFD--DVSFSYDNSrQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIdGTDIR----TVTRA 405
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  393 EL---------DP---DKTVMDNLAEGK-----QEVMVNGKPRHVLgylqDFLF-HPKRAMTPV----RALSGGERNRLL 450
Cdd:PRK13657 406 SLrrniavvfqDAglfNRSIEDNIRVGRpdatdEEMRAAAERAQAH----DFIErKPDGYDTVVgergRQLSGGERQRLA 481
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 15830287  451 LARLFLKPSNLLILDEPTNDLDVETLELLEELIDSyqgtvllVSHDR 497
Cdd:PRK13657 482 IARALLKDPPILILDEATSALDVETEAKVKAALDE-------LMKGR 521
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
321-498 1.79e-14

ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213267 [Multi-domain]  Cd Length: 232  Bit Score: 73.04  E-value: 1.79e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 321 EMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKlEVAYFD----------QH 390
Cdd:cd03300   2 ELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGK-DITNLPphkrpvntvfQN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 391 RAeLDPDKTVMDNLAEG-----------KQEVMVNGKPRHVLGYLQDFlfhpkramtpVRALSGGERNRLLLAR-LFLKP 458
Cdd:cd03300  81 YA-LFPHLTVFENIAFGlrlkklpkaeiKERVAEALDLVQLEGYANRK----------PSQLSGGQQQRVAIARaLVNEP 149
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 15830287 459 SnLLILDEPTNDLDVETLELLEELIDSYQG----TVLLVSHDRQ 498
Cdd:cd03300 150 K-VLLLDEPLGALDLKLRKDMQLELKRLQKelgiTFVFVTHDQE 192
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
321-473 2.12e-14

ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]


Pssm-ID: 130261 [Multi-domain]  Cd Length: 708  Bit Score: 76.70  E-value: 2.12e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   321 EMEDVCYQVD-GKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKLeVAYFDQH--RAEL--- 394
Cdd:TIGR01193 475 VINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFS-LKDIDRHtlRQFInyl 553
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   395 --DP---DKTVMDNLAEGKQEVMVNGKPRHV--------------LGYLQDFLFHPKramtpvrALSGGERNRLLLARLF 455
Cdd:TIGR01193 554 pqEPyifSGSILENLLLGAKENVSQDEIWAAceiaeikddienmpLGYQTELSEEGS-------SISGGQKQRIALARAL 626
                         170
                  ....*....|....*...
gi 15830287   456 LKPSNLLILDEPTNDLDV 473
Cdd:TIGR01193 627 LTDSKVLILDESTSNLDT 644
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
1-234 2.25e-14

ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 443326 [Multi-domain]  Cd Length: 242  Bit Score: 73.12  E-value: 2.25e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   1 MSlISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIiyeqdlivarlqqdpprNVE 80
Cdd:COG4161   1 MS-IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQL-----------------NIA 62
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  81 GSVYDFVAEGIEEQAEYLKR--------YHDISRL-VMNDPSEKNLNELAKVQEQLdhhnlwqlENRINEVLAQLGLDP- 150
Cdd:COG4161  63 GHQFDFSQKPSEKAIRLLRQkvgmvfqqYNLWPHLtVMENLIEAPCKVLGLSKEQA--------REKAMKLLARLRLTDk 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 151 -NVALSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFNGTII---FISHDRSFIRNMATRIVDL 226
Cdd:COG4161 135 aDRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGItqvIVTHEVEFARKVASQVVYM 214

                ....*...
gi 15830287 227 DRGKLVTY 234
Cdd:COG4161 215 EKGRIIEQ 222
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
157-500 2.30e-14

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 75.90  E-value: 2.30e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  157 LSGGWLRKAALGRALVSNPRVLLLDEPTNHLDI----ETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVsvqaQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCV 236
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  233 ------------TYPgnYDQYLLEKEEA-------------LRVEELQNAeFDrklaqeevwIRQGIKARRtrnegrvra 287
Cdd:PRK15134 237 eqnraatlfsapTHP--YTQKLLNSEPSgdpvplpepasplLDVEQLQVA-FP---------IRKGILKRT--------- 295
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  288 lkamrrergerrevmgtakmqveeasrsgkivfemedvcyqVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTT----LLK 363
Cdd:PRK15134 296 -----------------------------------------VDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLR 334
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  364 LML--GQLQADSGRIH---------VGTKLEVAYFDQHRAeLDPDKTVMDNLAEGKQ--EVMVNGKPR--HVLGYLQDFL 428
Cdd:PRK15134 335 LINsqGEIWFDGQPLHnlnrrqllpVRHRIQVVFQDPNSS-LNPRLNVLQIIEEGLRvhQPTLSAAQReqQVIAVMEEVG 413
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15830287  429 FHPK-RAMTPVrALSGGERNRLLLAR-LFLKPSnLLILDEPTNDLDVETLELLEELIDSYQGT----VLLVSHDRQFV 500
Cdd:PRK15134 414 LDPEtRHRYPA-EFSGGQRQRIAIARaLILKPS-LIILDEPTSSLDKTVQAQILALLKSLQQKhqlaYLFISHDLHVV 489
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
3-473 2.32e-14

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: 76.02  E-value: 2.32e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287     3 LISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILN--REQGLDDGRIIYEQDLIVARlqqdpprnve 80
Cdd:TIGR02633   1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSgvYPHGTWDGEIYWSGSPLKAS---------- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287    81 gSVYDFVAEGIEEQAEYLKRYHDISRLvmndpseKNL---NELAKVQEQLDHHNLWQlenRINEVLAQLGLDP-NVAL-- 154
Cdd:TIGR02633  71 -NIRDTERAGIVIIHQELTLVPELSVA-------ENIflgNEITLPGGRMAYNAMYL---RAKNLLRELQLDAdNVTRpv 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   155 SSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGF---LKTFNGTIIFISHDRSFIRNMATRIVDLDRGKL 231
Cdd:TIGR02633 140 GDYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIirdLKAHGVACVYISHKLNEVKAVCDTICVIRDGQH 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   232 VTypgnydqyllekeealrVEELQNAEFDRKLAQeevwirqgIKARRTRNegrvralkamrrergerrevmgtakMQVEE 311
Cdd:TIGR02633 220 VA-----------------TKDMSTMSEDDIITM--------MVGREITS-------------------------LYPHE 249
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   312 ASRSGKIVFEMEDV-CYQVDGKQL--VKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLG---------------QLQADS 373
Cdd:TIGR02633 250 PHEIGDVILEARNLtCWDVINPHRkrVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGaypgkfegnvfingkPVDIRN 329
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   374 GRIHVGTKLEVAYFDQHRAELDPDKTVMDNL---------------AEGKQEVMVNGKPRhvlgyLQDFLFHPkraMTPV 438
Cdd:TIGR02633 330 PAQAIRAGIAMVPEDRKRHGIVPILGVGKNItlsvlksfcfkmridAAAELQIIGSAIQR-----LKVKTASP---FLPI 401
                         490       500       510
                  ....*....|....*....|....*....|....*
gi 15830287   439 RALSGGERNRLLLARLFLKPSNLLILDEPTNDLDV 473
Cdd:TIGR02633 402 GRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDV 436
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
11-246 2.66e-14

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 76.02  E-value: 2.66e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   11 LSFS----DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLIvARLQQDPPRN----VEGS 82
Cdd:PRK11160 344 VSFTypdqPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPI-ADYSEAALRQaisvVSQR 422
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   83 VYDFVAEgieeqaeyLKryhdiSRLVMNDPsEKNLNELAKVQEQLDHHNLWQLENRINEVLAQLGldpnvalSSLSGGWL 162
Cdd:PRK11160 423 VHLFSAT--------LR-----DNLLLAAP-NASDEALIEVLQQVGLEKLLEDDKGLNAWLGEGG-------RQLSGGEQ 481
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  163 RKAALGRALVSNPRVLLLDEPTNHLDIET---IdwLEGFLKTFNG-TIIFISHDRSFIRNMaTRIVDLDRGKLVTYpGNY 238
Cdd:PRK11160 482 RRLGIARALLHDAPLLLLDEPTEGLDAETerqI--LELLAEHAQNkTVLMITHRLTGLEQF-DRICVMDNGQIIEQ-GTH 557

                 ....*...
gi 15830287  239 DQyLLEKE 246
Cdd:PRK11160 558 QE-LLAQQ 564
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
13-232 2.88e-14

ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.


Pssm-ID: 213234 [Multi-domain]  Cd Length: 236  Bit Score: 72.75  E-value: 2.88e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  13 FSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNreqGLddgriiyeqdlivarLQqdpPRNVEGSVYDFVAegIE 92
Cdd:cd03267  31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILS---GL---------------LQ---PTSGEVRVAGLVP--WK 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  93 EQAEYLKRyhdISrLVMNDPSEKNLNeLAKVQEQLDHHNLWQLE-----NRINEVLAQLGLDP--NVALSSLSGGWLRKA 165
Cdd:cd03267  88 RRKKFLRR---IG-VVFGQKTQLWWD-LPVIDSFYLLAAIYDLPparfkKRLDELSELLDLEEllDTPVRQLSLGQRMRA 162
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15830287 166 ALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFN----GTIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:cd03267 163 EIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNrergTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
19-232 3.51e-14

ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.


Pssm-ID: 213233 [Multi-domain]  Cd Length: 218  Bit Score: 72.02  E-value: 3.51e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEqDLIVARLQQDPPRN---VEGS--VYDFVAegIEE 93
Cdd:cd03266  21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVD-GFDVVKEPAEARRRlgfVSDStgLYDRLT--ARE 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  94 QAEYLKRYHDISRLvmndpseknlnelakvqeqldhhnlwQLENRINEVLAQLGLDP--NVALSSLSGGWLRKAALGRAL 171
Cdd:cd03266  98 NLEYFAGLYGLKGD--------------------------ELTARLEELADRLGMEEllDRRVGGFSTGMRQKVAIARAL 151
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15830287 172 VSNPRVLLLDEPTNHLDIETIDWLEGFLKTFNG---TIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:cd03266 152 VHDPPVLLLDEPTTGLDVMATRALREFIRQLRAlgkCILFSTHIMQEVERLCDRVVVLHRGRVV 215
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
335-500 3.86e-14

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


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 72.42  E-value: 3.86e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 335 VKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTK----LEVAyfdqhrAELDPDKTVMDNlaegkqe 410
Cdd:COG1134  42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRvsalLELG------AGFHPELTGREN------- 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 411 VMVNGkprHVLGY-----------------LQDFLfhpkraMTPVRALSGGERNRLLLA-RLFLKPsNLLILDEPTNDLD 472
Cdd:COG1134 109 IYLNG---RLLGLsrkeidekfdeivefaeLGDFI------DQPVKTYSSGMRARLAFAvATAVDP-DILLVDEVLAVGD 178
                       170       180       190
                ....*....|....*....|....*....|.
gi 15830287 473 VETLELLEELIDSYQ---GTVLLVSHDRQFV 500
Cdd:COG1134 179 AAFQKKCLARIRELResgRTVIFVSHSMGAV 209
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
330-472 3.93e-14

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: 72.22  E-value: 3.93e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 330 DGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVG----TKLEVAYFDQHRAE---------LDP 396
Cdd:cd03256  12 NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDgtdiNKLKGKALRQLRRQigmifqqfnLIE 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 397 DKTVMDNLAEGKqevmvngkprhvLGYLQDF-----LFHP----------------KRAMTPVRALSGGERNRLLLARLF 455
Cdd:cd03256  92 RLSVLENVLSGR------------LGRRSTWrslfgLFPKeekqralaalervgllDKAYQRADQLSGGQQQRVAIARAL 159
                       170
                ....*....|....*..
gi 15830287 456 LKPSNLLILDEPTNDLD 472
Cdd:cd03256 160 MQQPKLILADEPVASLD 176
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
321-472 5.74e-14

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


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 73.57  E-value: 5.74e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 321 EMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVG----TKLE-----VAY-FdQH 390
Cdd:COG3839   5 ELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGgrdvTDLPpkdrnIAMvF-QS 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 391 RAeLDPDKTVMDNLAEG-------KQEvmVNGKPRHVLGYLQ--DFLfhpKRamtPVRALSGGERNRLLLARLFLKPSNL 461
Cdd:COG3839  84 YA-LYPHMTVYENIAFPlklrkvpKAE--IDRRVREAAELLGleDLL---DR---KPKQLSGGQRQRVALGRALVREPKV 154
                       170
                ....*....|.
gi 15830287 462 LILDEPTNDLD 472
Cdd:COG3839 155 FLLDEPLSNLD 165
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
321-472 6.41e-14

ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213263 [Multi-domain]  Cd Length: 239  Bit Score: 71.60  E-value: 6.41e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 321 EMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTK---------LEVAYFDQHR 391
Cdd:cd03296   4 EVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEdatdvpvqeRNVGFVFQHY 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 392 AeLDPDKTVMDNLAEG---------KQEVMVNGKPRHVLGYLQ-DFLF--HPKRamtpvraLSGGERNRLLLARLFLKPS 459
Cdd:cd03296  84 A-LFRHMTVFDNVAFGlrvkprserPPEAEIRAKVHELLKLVQlDWLAdrYPAQ-------LSGGQRQRVALARALAVEP 155
                       170
                ....*....|...
gi 15830287 460 NLLILDEPTNDLD 472
Cdd:cd03296 156 KVLLLDEPFGALD 168
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
320-516 6.60e-14

ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.


Pssm-ID: 213229 [Multi-domain]  Cd Length: 213  Bit Score: 71.02  E-value: 6.60e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 320 FEMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV-GTKL------------EVAY 386
Cdd:cd03262   1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIdGLKLtddkkninelrqKVGM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 387 FDQHrAELDPDKTVMDNLAEGkqEVMVNGKPR-----HVLGYLQDFLFHPKRAMTPvRALSGGERNRLLLAR-LFLKPSn 460
Cdd:cd03262  81 VFQQ-FNLFPHLTVLENITLA--PIKVKGMSKaeaeeRALELLEKVGLADKADAYP-AQLSGGQQQRVAIARaLAMNPK- 155
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15830287 461 LLILDEPTNDLD---VETLELLEELIDSYQGTVLLVSHDRQFVDNtVTECWIFEGGGKI 516
Cdd:cd03262 156 VMLFDEPTSALDpelVGEVLDVMKDLAEEGMTMVVVTHEMGFARE-VADRVIFMDDGRI 213
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
19-232 6.95e-14

ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 443332 [Multi-domain]  Cd Length: 533  Bit Score: 74.72  E-value: 6.95e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  19 LDNAELHIEDNERVCLVGRNGAGKSTLMK-ILnreqGLDD--GRIIYE-QDL----------IVARLQ---QDP-----P 76
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLaLL----RLIPseGEIRFDgQDLdglsrralrpLRRRMQvvfQDPfgslsP 377
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  77 RNvegSVYDFVAEGIeeqaeylkRYHDIsrlvmnDPSEKnlnelakvqeqldhhnlwQLENRINEVLAQLGLDPNVAL-- 154
Cdd:COG4172 378 RM---TVGQIIAEGL--------RVHGP------GLSAA------------------ERRARVAEALEEVGLDPAARHry 422
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 155 -SSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDI----ETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRG 229
Cdd:COG4172 423 pHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVsvqaQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDG 502

                ...
gi 15830287 230 KLV 232
Cdd:COG4172 503 KVV 505
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
1-232 7.21e-14

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 71.58  E-value: 7.21e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287    1 MSlISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIiyeqdlivarlqqdpprNVE 80
Cdd:PRK11124   1 MS-IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTL-----------------NIA 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   81 GSVYDFVAEgieeqaeylkryhdisrlvmndPSEKNLNEL-AKVQEQLDHHNLWQ----LENRINEVLAQLGLDPNVALS 155
Cdd:PRK11124  63 GNHFDFSKT----------------------PSDKAIRELrRNVGMVFQQYNLWPhltvQQNLIEAPCRVLGLSKDQALA 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  156 S--------------------LSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFNGTII---FISHD 212
Cdd:PRK11124 121 RaekllerlrlkpyadrfplhLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGItqvIVTHE 200
                        250       260
                 ....*....|....*....|
gi 15830287  213 RSFIRNMATRIVDLDRGKLV 232
Cdd:PRK11124 201 VEVARKTASRVVYMENGHIV 220
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
344-512 7.31e-14

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: 71.67  E-value: 7.31e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 344 RGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIhvGTKLE-VAYFDQHrAELDPDKTVMDNLAEG----------KQEVM 412
Cdd:cd03237  24 ESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI--EIELDtVSYKPQY-IKADYEGTVRDLLSSItkdfythpyfKTEIA 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 413 vngKPRHVLGYLQdflfhpkramTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELIDSY----QG 488
Cdd:cd03237 101 ---KPLQIEQILD----------REVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFaennEK 167
                       170       180
                ....*....|....*....|....
gi 15830287 489 TVLLVSHDRQFVDNTVTECWIFEG 512
Cdd:cd03237 168 TAFVVEHDIIMIDYLADRLIVFEG 191
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
10-247 7.55e-14

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 72.00  E-value: 7.55e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   10 WLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRI------------IYEQDLIVARLQ----- 72
Cdd:PRK14246  17 YLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIkvdgkvlyfgkdIFQIDAIKLRKEvgmvf 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   73 QDPPRNVEGSVYDFVAegieeqaeYLKRYHDIsrlvmndpseKNLNELAK-VQEQLDHHNLWQlenrinEVLAQLgldpN 151
Cdd:PRK14246  97 QQPNPFPHLSIYDNIA--------YPLKSHGI----------KEKREIKKiVEECLRKVGLWK------EVYDRL----N 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  152 VALSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFNG--TIIFISHDRSFIRNMATRIVDLDRG 229
Cdd:PRK14246 149 SPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHNPQQVARVADYVAFLYNG 228
                        250
                 ....*....|....*...
gi 15830287  230 KLVTYPGNYDQYLLEKEE 247
Cdd:PRK14246 229 ELVEWGSSNEIFTSPKNE 246
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
322-496 8.88e-14

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 71.63  E-value: 8.88e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  322 MEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKLEVAYFDQHR-----AELDP 396
Cdd:PRK11247  15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTRlmfqdARLLP 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  397 DKTVMDNLAEGkqevmVNGKPR-------HVLGyLQDflfhpkRAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTN 469
Cdd:PRK11247  95 WKKVIDNVGLG-----LKGQWRdaalqalAAVG-LAD------RANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLG 162
                        170       180       190
                 ....*....|....*....|....*....|.
gi 15830287  470 DLDVETLELLEELIDS----YQGTVLLVSHD 496
Cdd:PRK11247 163 ALDALTRIEMQDLIESlwqqHGFTVLLVTHD 193
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
11-212 8.95e-14

thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.


Pssm-ID: 274331 [Multi-domain]  Cd Length: 530  Bit Score: 74.32  E-value: 8.95e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287    11 LSFS---DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEqDLIVARLQQDPPRNVEGsvydFV 87
Cdd:TIGR02868 340 LSAGypgAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLD-GVPVSSLDQDEVRRRVS----VC 414
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287    88 AEgieeqaeylkRYH-------DISRLVMNDPSEKnlnELAKVQEQLDHHNLWQ-LENRINEVLAQLGldpnvalSSLSG 159
Cdd:TIGR02868 415 AQ----------DAHlfdttvrENLRLARPDATDE---ELWAALERVGLADWLRaLPDGLDTVLGEGG-------ARLSG 474
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 15830287   160 GWLRKAALGRALVSNPRVLLLDEPTNHLDIETID-WLEGFLKTFNG-TIIFISHD 212
Cdd:TIGR02868 475 GERQRLALARALLADAPILLLDEPTEHLDAETADeLLEDLLAALSGrTVVLITHH 529
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
317-498 9.52e-14

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 70.84  E-value: 9.52e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 317 KIVFEMEDVC--YQVDGKQLV--KDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVG----TKLEVAYFD 388
Cdd:COG1136   2 SPLLELRNLTksYGTGEGEVTalRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDgqdiSSLSERELA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 389 QHRAE----------LDPDKTVMDNLA-----EGKQEVMVNGKPRHVLGYLQdfLFHpkRAMTPVRALSGGERNRLLLAR 453
Cdd:COG1136  82 RLRRRhigfvfqffnLLPELTALENVAlplllAGVSRKERRERARELLERVG--LGD--RLDHRPSQLSGGQQQRVAIAR 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 15830287 454 -LFLKPSnLLILDEPTNDLDvetlELLEELI--------DSYQGTVLLVSHDRQ 498
Cdd:COG1136 158 aLVNRPK-LILADEPTGNLD----SKTGEEVlellrelnRELGTTIVMVTHDPE 206
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
330-495 9.96e-14

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 74.11  E-value: 9.96e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  330 DGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLqADSGRIHVG----TKLEVAYFDQHRAELD-----PDKTV 400
Cdd:PRK11174 361 DGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINgielRELDPESWRKHLSWVGqnpqlPHGTL 439
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  401 MDNLAEGKQEvMVNGKPRHVL--GYLQDFLF-HPKRAMTPVR----ALSGGERNRLLLARLFLKPSNLLILDEPTNDLDV 473
Cdd:PRK11174 440 RDNVLLGNPD-ASDEQLQQALenAWVSEFLPlLPQGLDTPIGdqaaGLSVGQAQRLALARALLQPCQLLLLDEPTASLDA 518
                        170       180
                 ....*....|....*....|....
gi 15830287  474 ETLELLEELIDSY--QGTVLLVSH 495
Cdd:PRK11174 519 HSEQLVMQALNAAsrRQTTLMVTH 542
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
12-226 1.01e-13

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 69.96  E-value: 1.01e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   12 SFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLIVARLQQ--DPPRNVEGSVYDFVAE 89
Cdd:NF040873   1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQrsEVPDSLPLTVRDLVAM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   90 GIEEQAEYLKRYHDISRLVmndpseknlnelakVQEQLDHHNLWQLENRinevlaqlgldpnvALSSLSGGWLRKAALGR 169
Cdd:NF040873  81 GRWARRGLWRRLTRDDRAA--------------VDDALERVGLADLAGR--------------QLGELSGGQRQRALLAQ 132
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  170 ALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFNG---TIIFISHDRSFIRNmATRIVDL 226
Cdd:NF040873 133 GLAQEADLLLLDEPTTGLDAESRERIIALLAEEHArgaTVVVVTHDLELVRR-ADPCVLL 191
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
1-189 1.05e-13

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 73.34  E-value: 1.05e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287    1 MSLISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLIVARLQQDPPRNV- 79
Cdd:PRK09536   1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVa 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   80 ----EGSV-YDFVAEGIEEqaeyLKRYHDISRLVMNDPSEKnlnelAKVQEQLDHHNLWQLENRinevlaqlgldpnvAL 154
Cdd:PRK09536  81 svpqDTSLsFEFDVRQVVE----MGRTPHRSRFDTWTETDR-----AAVERAMERTGVAQFADR--------------PV 137
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 15830287  155 SSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDI 189
Cdd:PRK09536 138 TSLSGGERQRVLLARALAQATPVLLLDEPTASLDI 172
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
1-230 1.19e-13

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 73.06  E-value: 1.19e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287    1 MSLISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYE-QDliVARLqqdPP--R 77
Cdd:PRK09452  12 SPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDgQD--ITHV---PAenR 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   78 NVEG-----------SVYDFVAEGIEEQ----AEYLKRYHDISRLVmndpseknlnelakvqeqldhhnlwQLENRINEV 142
Cdd:PRK09452  87 HVNTvfqsyalfphmTVFENVAFGLRMQktpaAEITPRVMEALRMV-------------------------QLEEFAQRK 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  143 LAQLgldpnvalsslSGGWLRKAALGRALVSNPRVLLLDEPTNHLD--------IEtidwLEGFLKTFNGTIIFISHDRS 214
Cdd:PRK09452 142 PHQL-----------SGGQQQRVAIARAVVNKPKVLLLDESLSALDyklrkqmqNE----LKALQRKLGITFVFVTHDQE 206
                        250
                 ....*....|....*.
gi 15830287  215 FIRNMATRIVDLDRGK 230
Cdd:PRK09452 207 EALTMSDRIVVMRDGR 222
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
19-234 1.35e-13

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: 70.25  E-value: 1.35e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIyeqdlivarlqqdpprnVEGSVYDFVAEGI------- 91
Cdd:cd03220  38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT-----------------VRGRVSSLLGLGGgfnpelt 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  92 -EEQAEYLKRYHDISRlvmndpseknlnelakvqEQLDhhnlwQLENRINEvLAQLGLDPNVALSSLSGGWLRKAALGRA 170
Cdd:cd03220 101 gRENIYLNGRLLGLSR------------------KEID-----EKIDEIIE-FSELGDFIDLPVKTYSSGMKARLAFAIA 156
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15830287 171 LVSNPRVLLLDEPTNHLDIET----IDWLEGFLKTfNGTIIFISHDRSFIRNMATRIVDLDRGKLVTY 234
Cdd:cd03220 157 TALEPDILLIDEVLAVGDAAFqekcQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFD 223
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
319-472 1.53e-13

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 72.56  E-value: 1.53e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  319 VFEMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI--------HVGTKLEVAYFDQH 390
Cdd:PRK11607  19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQImldgvdlsHVPPYQRPINMMFQ 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  391 RAELDPDKTVMDNLAEG-KQEVM----VNGKPRHVLG--YLQDFlfhpkrAMTPVRALSGGERNRLLLARLFLKPSNLLI 463
Cdd:PRK11607  99 SYALFPHMTVEQNIAFGlKQDKLpkaeIASRVNEMLGlvHMQEF------AKRKPHQLSGGQRQRVALARSLAKRPKLLL 172

                 ....*....
gi 15830287  464 LDEPTNDLD 472
Cdd:PRK11607 173 LDEPMGALD 181
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
17-245 1.58e-13

ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213220 [Multi-domain]  Cd Length: 236  Bit Score: 70.34  E-value: 1.58e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  17 PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRI-IYEQDliVARLQQDPPRNVEGSV-------YDFVA 88
Cdd:cd03253  15 PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSIlIDGQD--IREVTLDSLRRAIGVVpqdtvlfNDTIG 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  89 EGIeeqaeylkRYHDIsrlvmnDPSEKNLNELAKVQEQldHHNLWQLENRINEVLAQLGLdpnvalsSLSGGWLRKAALG 168
Cdd:cd03253  93 YNI--------RYGRP------DATDEEVIEAAKAAQI--HDKIMRFPDGYDTIVGERGL-------KLSGGEKQRVAIA 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 169 RALVSNPRVLLLDEPTNHLDIET---IdwLEGFLKTFNG-TIIFISHDRSFIRNmATRIVDLDRGKLVTyPGNYDQYLLE 244
Cdd:cd03253 150 RAILKNPPILLLDEATSALDTHTereI--QAALRDVSKGrTTIVIAHRLSTIVN-ADKIIVLKDGRIVE-RGTHEELLAK 225

                .
gi 15830287 245 K 245
Cdd:cd03253 226 G 226
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
320-467 1.65e-13

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: 70.26  E-value: 1.65e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 320 FEMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVG----TKLEV--------AYF 387
Cdd:cd03218   1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDgqdiTKLPMhkrarlgiGYL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 388 DQhRAELDPDKTVMDNLAEGKQEVMVNGKPRH-VLGYLQDfLFHPKR-AMTPVRALSGGERNRLLLAR-LFLKPSNLLiL 464
Cdd:cd03218  81 PQ-EASIFRKLTVEENILAVLEIRGLSKKEREeKLEELLE-EFHITHlRKSKASSLSGGERRRVEIARaLATNPKFLL-L 157

                ...
gi 15830287 465 DEP 467
Cdd:cd03218 158 DEP 160
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
3-241 1.69e-13

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 73.67  E-value: 1.69e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287    3 LISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLIVARLQQdpprnvegs 82
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQ--------- 382
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   83 vydfvaegieEQAEYLKryhdisrlvmndPSEKNLNELAKVQEQldhhnlwQLENRINEVLAQLGLDPNV---ALSSLSG 159
Cdd:PRK10636 383 ----------HQLEFLR------------ADESPLQHLARLAPQ-------ELEQKLRDYLGGFGFQGDKvteETRRFSG 433
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  160 GwlRKAALGRALV--SNPRVLLLDEPTNHLDIETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKLVTYPGN 237
Cdd:PRK10636 434 G--EKARLVLALIvwQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVEPFDGD 511

                 ....
gi 15830287  238 YDQY 241
Cdd:PRK10636 512 LEDY 515
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
15-248 1.94e-13

ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.


Pssm-ID: 213216 [Multi-domain]  Cd Length: 238  Bit Score: 70.26  E-value: 1.94e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  15 DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLI-----------VARLQQDPprnV--EG 81
Cdd:cd03249  15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIrdlnlrwlrsqIGLVSQEP---VlfDG 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  82 SVYDFVAEG----IEEQAEYLKRYHDISRLVMNDPseknlnelakvqeqldhhnlwqleNRINEVLAQLGldpnvalSSL 157
Cdd:cd03249  92 TIAENIRYGkpdaTDEEVEEAAKKANIHDFIMSLP------------------------DGYDTLVGERG-------SQL 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 158 SGGWLRKAALGRALVSNPRVLLLDEPTNHLDIET----IDWLEGFLKtfNGTIIFISHDRSFIRNmATRIVDLDRGKLVT 233
Cdd:cd03249 141 SGGQKQRIAIARALLRNPKILLLDEATSALDAESeklvQEALDRAMK--GRTTIVIAHRLSTIRN-ADLIAVLQNGQVVE 217
                       250
                ....*....|....*
gi 15830287 234 YpGNYDQyLLEKEEA 248
Cdd:cd03249 218 Q-GTHDE-LMAQKGV 230
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
333-468 2.22e-13

ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.


Pssm-ID: 213191 [Multi-domain]  Cd Length: 222  Bit Score: 69.77  E-value: 2.22e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 333 QLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVG----TKLE--------VAYFDQHRaELDPDKTV 400
Cdd:cd03224  14 QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDgrdiTGLPpheraragIGYVPEGR-RIFPELTV 92
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15830287 401 MDNLAEGKQeVMVNGKPRHVLGYLQDfLFhPK---RAMTPVRALSGGERNRLLLAR-LFLKPSnLLILDEPT 468
Cdd:cd03224  93 EENLLLGAY-ARRRAKRKARLERVYE-LF-PRlkeRRKQLAGTLSGGEQQMLAIARaLMSRPK-LLLLDEPS 160
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
12-277 2.30e-13

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


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 71.29  E-value: 2.30e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  12 SFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNreqGL---DDGRIIYEQdlivARLQQDPPRNV-----EGSV 83
Cdd:COG4152  10 RFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIIL---GIlapDSGEVLWDG----EPLDPEDRRRIgylpeERGL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  84 YDfvAEGIEEQAEYLKRYHDISRlvmndpseknlnelAKVQEQLDHhnlWqlenrinevLAQLGLDP--NVALSSLSGGW 161
Cdd:COG4152  83 YP--KMKVGEQLVYLARLKGLSK--------------AEAKRRADE---W---------LERLGLGDraNKKVEELSKGN 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 162 LRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTF--NG-TIIFISHDRSFIRNMATRIVDLDRGKLVTYpGN- 237
Cdd:COG4152 135 QQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELaaKGtTVIFSSHQMELVEELCDRIVIINKGRKVLS-GSv 213
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 15830287 238 ---YDQYlleKEEALRVEELQNAEFDRKLAQEEVWIRQGIKAR 277
Cdd:COG4152 214 deiRRQF---GRNTLRLEADGDAGWLRALPGVTVVEEDGDGAE 253
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
2-233 2.39e-13

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


Pssm-ID: 443338 [Multi-domain]  Cd Length: 233  Bit Score: 69.77  E-value: 2.39e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   2 SLISMHGAWLSFSDA--PL--LDNAELHIEDNERVCLVGRNGAGKSTLMKILnreQGLD---DGRI-IYEQDLivARLQQ 73
Cdd:COG4181   7 PIIELRGLTKTVGTGagELtiLKGISLEVEAGESVAIVGASGSGKSTLLGLL---AGLDrptSGTVrLAGQDL--FALDE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  74 DP-----PRNVegsvydfvaeGIEEQAEYLkryhdISRL-----VM--------NDPSEKNLNELAKV--QEQLDHHnlw 133
Cdd:COG4181  82 DArarlrARHV----------GFVFQSFQL-----LPTLtalenVMlplelagrRDARARARALLERVglGHRLDHY--- 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 134 qlenrinevlaqlgldPNValssLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIET----IDWLEGFLKTFNGTIIFI 209
Cdd:COG4181 144 ----------------PAQ----LSGGEQQRVALARAFATEPAILFADEPTGNLDAATgeqiIDLLFELNRERGTTLVLV 203
                       250       260
                ....*....|....*....|....
gi 15830287 210 SHDRSFIRnMATRIVDLDRGKLVT 233
Cdd:COG4181 204 THDPALAA-RCDRVLRLRAGRLVE 226
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
310-472 2.68e-13

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 72.94  E-value: 2.68e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  310 EEASRSGKIVFEMEDVC--YQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKLEVAYF 387
Cdd:PRK11160 329 TSTAAADQVSLTLNNVSftYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYS 408
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  388 DQ----------HRAELDPDkTVMDNLAEGK----QEVMVngkprHVL---GyLQDFLFHPKRAMTPV----RALSGGER 446
Cdd:PRK11160 409 EAalrqaisvvsQRVHLFSA-TLRDNLLLAApnasDEALI-----EVLqqvG-LEKLLEDDKGLNAWLgeggRQLSGGEQ 481
                        170       180
                 ....*....|....*....|....*.
gi 15830287  447 NRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:PRK11160 482 RRLGIARALLHDAPLLLLDEPTEGLD 507
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
329-513 3.35e-13

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: 69.10  E-value: 3.35e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 329 VDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTK----LEVAYFdqhraeLDPDKTVMDNl 404
Cdd:cd03220  32 VGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRvsslLGLGGG------FNPELTGREN- 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 405 aegkqeVMVNGKprhVLGYLQDFLfhpkRAM---------------TPVRALSGGERNRLLLA-RLFLKPsNLLILDEPT 468
Cdd:cd03220 105 ------IYLNGR---LLGLSRKEI----DEKideiiefselgdfidLPVKTYSSGMKARLAFAiATALEP-DILLIDEVL 170
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 15830287 469 NDLDVETLELLEELIDSYQ---GTVLLVSHDRQFVDNTVTECWIFEGG 513
Cdd:cd03220 171 AVGDAAFQEKCQRRLRELLkqgKTVILVSHDPSSIKRLCDRALVLEKG 218
PLN03073 PLN03073
ABC transporter F family; Provisional
277-545 3.40e-13

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 72.59  E-value: 3.40e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  277 RRTRNEGRVRALKAMRRERGERREVMGTAKMQVEEASRSGKIV---FEMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGP 353
Cdd:PLN03073 132 RRKRKEERQREVQYQAHVAEMEAAKAGMPGVYVNHDGNGGGPAikdIHMENFSISVGGRDLIVDASVTLAFGRHYGLVGR 211
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  354 NGCGKTTLLKLMlgQLQADSGR------IHVG---------------------TKL--EVAYFDQHRAELD--------- 395
Cdd:PLN03073 212 NGTGKTTFLRYM--AMHAIDGIpkncqiLHVEqevvgddttalqcvlntdierTQLleEEAQLVAQQRELEfetetgkgk 289
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  396 -PDKTVMDNLAEGKQEVMVNGKPRHVLGY---------LQDFLFHPKRAMTPVRALSGGERNRLLLAR-LFLKPsNLLIL 464
Cdd:PLN03073 290 gANKDGVDKDAVSQRLEEIYKRLELIDAYtaearaasiLAGLSFTPEMQVKATKTFSGGWRMRIALARaLFIEP-DLLLL 368
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  465 DEPTNDLDVETLELLEELIDSYQGTVLLVSHDRQFVDNTVTECWIFEGGgKIGRYVGGYHDARGQQEQYVALKQPAVKKN 544
Cdd:PLN03073 369 DEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLHGQ-KLVTYKGDYDTFERTREEQLKNQQKAFESN 447

                 .
gi 15830287  545 E 545
Cdd:PLN03073 448 E 448
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
317-505 3.85e-13

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 68.97  E-value: 3.85e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  317 KIVFEMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV-GTKL----------EVA 385
Cdd:PRK10247   5 SPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFeGEDIstlkpeiyrqQVS 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  386 YFDQHRAeLDPDkTVMDNLAEGKQEVMVNGKPRHVLGYLQDFLFHPKRAMTPVRALSGGERNRLLLARLFLKPSNLLILD 465
Cdd:PRK10247  85 YCAQTPT-LFGD-TVYDNLIFPWQIRNQQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLD 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 15830287  466 EPTNDLDVETLELLEELIDSY----QGTVLLVSHDR---QFVDNTVT 505
Cdd:PRK10247 163 EITSALDESNKHNVNEIIHRYvreqNIAVLWVTHDKdeiNHADKVIT 209
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
18-266 3.87e-13

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


Pssm-ID: 440718 [Multi-domain]  Cd Length: 264  Bit Score: 69.73  E-value: 3.87e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  18 LLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRI-IYEQDlivarlqqdpprnvegsvydfvaegIEEQAE 96
Cdd:COG1101  21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSIlIDGKD-------------------------VTKLPE 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  97 YlKRYHDISRlVMNDPS---------EKNL------------------NELAKVQEQLDHHNLwQLENRINevlAQLGLd 149
Cdd:COG1101  76 Y-KRAKYIGR-VFQDPMmgtapsmtiEENLalayrrgkrrglrrgltkKRRELFRELLATLGL-GLENRLD---TKVGL- 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 150 pnvalssLSGGWlRKA-ALGRALVSNPRVLLLDEPTNHLDIET----IDWLEGFLKTFNGTIIFISHDRSFIRNMATRIV 224
Cdd:COG1101 149 -------LSGGQ-RQAlSLLMATLTKPKLLLLDEHTAALDPKTaalvLELTEKIVEENNLTTLMVTHNMEQALDYGNRLI 220
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 15830287 225 DLDRGKLVtypgnYDqylLEKEE--ALRVEELQnAEFDRKLAQE 266
Cdd:COG1101 221 MMHEGRII-----LD---VSGEEkkKLTVEDLL-ELFEEIRGEE 255
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
321-472 3.95e-13

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: 68.76  E-value: 3.95e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 321 EMEDVCYQVDGKQLVKDFSAQVLRGdKIALIGPNGCGKTTLLKLMLGQLQADSGRIhvgtklevaYFDQHRAELDPDKTv 400
Cdd:cd03264   2 QLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTI---------RIDGQDVLKQPQKL- 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 401 mdnlaegkqevmvngkpRHVLGYL-QDFLFHPK------------------------------------RAMTPVRALSG 443
Cdd:cd03264  71 -----------------RRRIGYLpQEFGVYPNftvrefldyiawlkgipskevkarvdevlelvnlgdRAKKKIGSLSG 133
                       170       180
                ....*....|....*....|....*....
gi 15830287 444 GERNRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:cd03264 134 GMRRRVGIAQALVGDPSILIVDEPTAGLD 162
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
311-472 4.16e-13

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 71.13  E-value: 4.16e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  311 EASRSGKIVFEMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI-------------- 376
Cdd:PRK09452   6 KQPSSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRImldgqdithvpaen 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  377 -HVGTKLevayfdQHRAeLDPDKTVMDNLAEG-------KQEVmvngKPRhVLG-----YLQDFlfhpkrAMTPVRALSG 443
Cdd:PRK09452  86 rHVNTVF------QSYA-LFPHMTVFENVAFGlrmqktpAAEI----TPR-VMEalrmvQLEEF------AQRKPHQLSG 147
                        170       180
                 ....*....|....*....|....*....
gi 15830287  444 GERNRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:PRK09452 148 GQQQRVAIARAVVNKPKVLLLDESLSALD 176
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
332-472 4.47e-13

White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.


Pssm-ID: 213201 [Multi-domain]  Cd Length: 226  Bit Score: 68.84  E-value: 4.47e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 332 KQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQAD---SGRIHVG--------TKLEVAYFDQHRAELdPDKTV 400
Cdd:cd03234  20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNgqprkpdqFQKCVAYVRQDDILL-PGLTV 98
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15830287 401 MDNLAEGKQEVMVNGKPRHVLGYLQDFLFHPKRAMTPVR-----ALSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:cd03234  99 RETLTYTAILRLPRKSSDAIRKKRVEDVLLRDLALTRIGgnlvkGISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
4-234 5.10e-13

ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.


Pssm-ID: 213211 [Multi-domain]  Cd Length: 221  Bit Score: 68.67  E-value: 5.10e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   4 ISMHGAWLSFSD--APLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIY-EQDLIVARLQ-------- 72
Cdd:cd03244   3 IEFKNVSLRYRPnlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIdGVDISKIGLHdlrsrisi 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  73 --QDPprnvegsvydFVAEG-IEEQAEYLKRYHDisrlvmndpsEKNLNELAKVQeqldhhnlwqLENRINEVLAQLGLD 149
Cdd:cd03244  83 ipQDP----------VLFSGtIRSNLDPFGEYSD----------EELWQALERVG----------LKEFVESLPGGLDTV 132
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 150 PNVALSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTF--NGTIIFISHdRsfIRNMAT--RIVD 225
Cdd:cd03244 133 VEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIREAfkDCTVLTIAH-R--LDTIIDsdRILV 209

                ....*....
gi 15830287 226 LDRGKLVTY 234
Cdd:cd03244 210 LDKGRVVEF 218
cbiO PRK13646
energy-coupling factor transporter ATPase;
19-232 5.41e-13

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 69.81  E-value: 5.41e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEqDLIVARLQQD----PPRNVEGSVYDFVAEGIEEQ 94
Cdd:PRK13646  23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVD-DITITHKTKDkyirPVRKRIGMVFQFPESQLFED 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   95 aeylkryhDISRLVMNDPseKNLNelakvqeqldhHNLWQLENRINEVLAQLGLDPNVALSS---LSGGWLRKAALGRAL 171
Cdd:PRK13646 102 --------TVEREIIFGP--KNFK-----------MNLDEVKNYAHRLLMDLGFSRDVMSQSpfqMSGGQMRKIAIVSIL 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15830287  172 VSNPRVLLLDEPTNHLDIETIDWLEGFLKTF----NGTIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:PRK13646 161 AMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLqtdeNKTIILVSHDMNEVARYADEVIVMKEGSIV 225
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
316-473 5.64e-13

ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213221 [Multi-domain]  Cd Length: 229  Bit Score: 68.79  E-value: 5.64e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 316 GKIVFEmeDVCYQVDGKQLV-KDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGtklEVAYFDQHRAEL 394
Cdd:cd03254   1 GEIEFE--NVNFSYDEKKPVlKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILID---GIDIRDISRKSL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 395 ---------DP---DKTVMDNLAEGKQ-----EVMVNGKPRHvlgyLQDFLFH-PKRAMTPVR----ALSGGERNRLLLA 452
Cdd:cd03254  76 rsmigvvlqDTflfSGTIMENIRLGRPnatdeEVIEAAKEAG----AHDFIMKlPNGYDTVLGenggNLSQGERQLLAIA 151
                       170       180
                ....*....|....*....|.
gi 15830287 453 RLFLKPSNLLILDEPTNDLDV 473
Cdd:cd03254 152 RAMLRDPKILILDEATSNIDT 172
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
19-232 5.97e-13

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 70.60  E-value: 5.97e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIY---------EQDLIVARlqqdppRNVeG-------- 81
Cdd:PRK11153  21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVdgqdltalsEKELRKAR------RQI-Gmifqhfnl 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   82 ----SVYDFVAegieeqaeylkryhdisrLVMndpseknlnELAKVQEQldhhnlwQLENRINEVLAQLGLDP--NVALS 155
Cdd:PRK11153  94 lssrTVFDNVA------------------LPL---------ELAGTPKA-------EIKARVTELLELVGLSDkaDRYPA 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  156 SLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIET----IDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKL 231
Cdd:PRK11153 140 QLSGGQKQRVAIARALASNPKVLLCDEATSALDPATtrsiLELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRL 219

                 .
gi 15830287  232 V 232
Cdd:PRK11153 220 V 220
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
330-473 6.68e-13

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 67.91  E-value: 6.68e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  330 DGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVG----TKLEVAYFDQ-----HRAELDPDKTV 400
Cdd:PRK13538  12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQgepiRRQRDEYHQDllylgHQPGIKTELTA 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  401 MDNLA-------EGKQEVMVNGKPRHVLGylqdflfhpKRAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDV 473
Cdd:PRK13538  92 LENLRfyqrlhgPGDDEALWEALAQVGLA---------GFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDK 162
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
15-231 7.09e-13

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


Pssm-ID: 213213 [Multi-domain]  Cd Length: 173  Bit Score: 67.24  E-value: 7.09e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  15 DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILnreqglddgriiyeqdlivARLQQDpprnVEGSVYdfvAEGIEEQ 94
Cdd:cd03246  14 EPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLI-------------------LGLLRP----TSGRVR---LDGADIS 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  95 AEYLKRYHDISRLVMNDpseknlNELakvqeqldhhnlwqLENRINEvlaqlgldpNValssLSGGWLRKAALGRALVSN 174
Cdd:cd03246  68 QWDPNELGDHVGYLPQD------DEL--------------FSGSIAE---------NI----LSGGQRQRLGLARALYGN 114
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 175 PRVLLLDEPTNHLDIETIDWLE---GFLKTFNGTIIFISHDRSFIRnMATRIVDLDRGKL 231
Cdd:cd03246 115 PRILVLDEPNSHLDVEGERALNqaiAALKAAGATRIVIAHRPETLA-SADRILVLEDGRV 173
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
304-513 7.14e-13

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: 68.23  E-value: 7.14e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 304 TAKMQVEEASRSgkivFEMedvcYQVDGKQL--VKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV--- 378
Cdd:COG4778   2 TTLLEVENLSKT----FTL----HLQGGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhd 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 379 GTKLEVAyfdqhRAeldPDKTVMDNLaegkqevmvngkpRHVLGYLQDFLfhpkRAMTPVRAL----------------- 441
Cdd:COG4778  74 GGWVDLA-----QA---SPREILALR-------------RRTIGYVSQFL----RVIPRVSALdvvaepllergvdreea 128
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 442 -------------------------SGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELIDSY--QGTVLL-V 493
Cdd:COG4778 129 rararellarlnlperlwdlppatfSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAkaRGTAIIgI 208
                       250       260
                ....*....|....*....|
gi 15830287 494 SHDRQFVDNTVTECWIFEGG 513
Cdd:COG4778 209 FHDEEVREAVADRVVDVTPF 228
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
1-232 7.26e-13

putative amino-acid ABC transporter ATP-binding protein YecC; Provisional


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 69.01  E-value: 7.26e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287    1 MSLISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRI------------IYEQDLIV 68
Cdd:PRK11264   1 MSAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgditidtarsLSQQKGLI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   69 ARLQQD-----------PPRnvegSVYDFVAEGieeqaeylkryhdiSRLVMNDPSEknlnelakvqeqldhhnlwQLEN 137
Cdd:PRK11264  81 RQLRQHvgfvfqnfnlfPHR----TVLENIIEG--------------PVIVKGEPKE-------------------EATA 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  138 RINEVLAQLGLD--PNVALSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLegfLKTFNG------TIIFI 209
Cdd:PRK11264 124 RARELLAKVGLAgkETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEV---LNTIRQlaqekrTMVIV 200
                        250       260
                 ....*....|....*....|...
gi 15830287  210 SHDRSFIRNMATRIVDLDRGKLV 232
Cdd:PRK11264 201 THEMSFARDVADRAIFMDQGRIV 223
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
19-258 7.79e-13

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


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 69.73  E-value: 7.79e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNreqGL---DDGRIiyeqdlivarlqqdpprnvegSVYDFVAegIEEQA 95
Cdd:COG4586  38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLT---GIlvpTSGEV---------------------RVLGYVP--FKRRK 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  96 EYLKRyhdISrLVMndpSEKNlnelakvqeQLdhhnLWQL--------------------ENRINEVLAQLGLDP--NVA 153
Cdd:COG4586  92 EFARR---IG-VVF---GQRS---------QL----WWDLpaidsfrllkaiyripdaeyKKRLDELVELLDLGEllDTP 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 154 LSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFN----GTIIFISHDRSFIRNMATRIVDLDRG 229
Cdd:COG4586 152 VRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNrergTTILLTSHDMDDIEALCDRVIVIDHG 231
                       250       260
                ....*....|....*....|....*....
gi 15830287 230 KLVtYPGNYDQyLLEKEEALRVEELQNAE 258
Cdd:COG4586 232 RII-YDGSLEE-LKERFGPYKTIVLELAE 258
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
1-520 8.74e-13

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 70.81  E-value: 8.74e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287    1 MSLISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDG----------RIIYEQdlivar 70
Cdd:PRK10938   1 MSSLQISQGTFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGerqsqfshitRLSFEQ------ 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   71 LQQdpprnvegsvydfvaegIEEQaEYLKRYHDisrlvMNDPSEKNLNELAKVQEQLDHHNlwqlENRINEVLAQLGLDP 150
Cdd:PRK10938  75 LQK-----------------LVSD-EWQRNNTD-----MLSPGEDDTGRTTAEIIQDEVKD----PARCEQLAQQFGITA 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  151 --NVALSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFNG---TIIFISHDRSFIRNMATRIVD 225
Cdd:PRK10938 128 llDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQsgiTLVLVLNRFDEIPDFVQFAGV 207
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  226 LDRGKLvTYPGNYDQYLlekEEALrVEELQNAEfdrKLAQEEVWIRQGIKARRTRNEGRVRalkamrrergerrevmgta 305
Cdd:PRK10938 208 LADCTL-AETGEREEIL---QQAL-VAQLAHSE---QLEGVQLPEPDEPSARHALPANEPR------------------- 260
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  306 kmqveeasrsgkivFEMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLG-QLQADSGRIHVgtklev 384
Cdd:PRK10938 261 --------------IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdHPQGYSNDLTL------ 320
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  385 ayFDQHRAEldpDKTVMDNlaegKQ-----------EVMVNGKPRHVL--GYLQ--------------------DFLFHP 431
Cdd:PRK10938 321 --FGRRRGS---GETIWDI----KKhigyvssslhlDYRVSTSVRNVIlsGFFDsigiyqavsdrqqklaqqwlDILGID 391
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  432 KR-AMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELIDSYQG---TVLL-VSHDRQFVDNTVTE 506
Cdd:PRK10938 392 KRtADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISegeTQLLfVSHHAEDAPACITH 471
                        570
                 ....*....|....
gi 15830287  507 CWIFEGGGKIGRYV 520
Cdd:PRK10938 472 RLEFVPDGDIYRYV 485
PLN03073 PLN03073
ABC transporter F family; Provisional
11-241 1.02e-12

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 71.04  E-value: 1.02e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   11 LSFSDA-------PLL-DNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLIVARLQQdpprnvegs 82
Cdd:PLN03073 509 ISFSDAsfgypggPLLfKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAVFSQ--------- 579
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   83 vydfvaegieeqaeylkryHDISRLvmnDPSEKNLNELAKVQEQLdhhnlwqLENRINEVLAQLGLDPNVALSS---LSG 159
Cdd:PLN03073 580 -------------------HHVDGL---DLSSNPLLYMMRCFPGV-------PEQKLRAHLGSFGVTGNLALQPmytLSG 630
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  160 GWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKLVTYPGNYD 239
Cdd:PLN03073 631 GQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKVTPFHGTFH 710

                 ..
gi 15830287  240 QY 241
Cdd:PLN03073 711 DY 712
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
11-234 1.02e-12

ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 68.52  E-value: 1.02e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  11 LSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNReqgLDD--------GRIIYEQDLIVARlQQDPP---RNV 79
Cdd:COG1117  19 VYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNR---MNDlipgarveGEILLDGEDIYDP-DVDVVelrRRV 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  80 eG-----------SVYDFVAEGIeeqaeylkRYHDISrlvmndpSEKNLNELakVQEQLDHHNLWqlenriNEV---LAQ 145
Cdd:COG1117  95 -GmvfqkpnpfpkSIYDNVAYGL--------RLHGIK-------SKSELDEI--VEESLRKAALW------DEVkdrLKK 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 146 LGLdpnvalsSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLD------IE-TIDwlEgfLKTfNGTIIFISHdrsfirN 218
Cdd:COG1117 151 SAL-------GLSGGQQQRLCIARALAVEPEVLLMDEPTSALDpistakIEeLIL--E--LKK-DYTIVIVTH------N 212
                       250       260
                ....*....|....*....|..
gi 15830287 219 M--ATRIVD----LDRGKLVTY 234
Cdd:COG1117 213 MqqAARVSDytafFYLGELVEF 234
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
31-225 1.12e-12

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 68.66  E-value: 1.12e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   31 RVC-LVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLI-----------VARL-QQDPPrnVEG-SVYDFVAEGieeqae 96
Cdd:PRK10575  38 KVTgLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLeswsskafarkVAYLpQQLPA--AEGmTVRELVAIG------ 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   97 ylkRYhdisrlvmndPSEKNLNELAKVQEQldhhnlwqlenRINEVLAQLGLDP--NVALSSLSGGWLRKAALGRALVSN 174
Cdd:PRK10575 110 ---RY----------PWHGALGRFGAADRE-----------KVEEAISLVGLKPlaHRLVDSLSGGERQRAWIAMLVAQD 165
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 15830287  175 PRVLLLDEPTNHLDI----ETIDWLEGFLKTFNGTIIFISHDrsfiRNMATRIVD 225
Cdd:PRK10575 166 SRCLLLDEPTSALDIahqvDVLALVHRLSQERGLTVIAVLHD----INMAARYCD 216
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
14-231 1.23e-12

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: 67.88  E-value: 1.23e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  14 SDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRII--------YEQDLI---VARLQQDPPRnVEGS 82
Cdd:cd03248  25 PDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLldgkpisqYEHKYLhskVSLVGQEPVL-FARS 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  83 VYDFVAEGieeqaeylkryhdisrlvMNDPSEKNLNELAkvQEQLDHHNLWQLENRINEVLAQLGldpnvalSSLSGGWL 162
Cdd:cd03248 104 LQDNIAYG------------------LQSCSFECVKEAA--QKAHAHSFISELASGYDTEVGEKG-------SQLSGGQK 156
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15830287 163 RKAALGRALVSNPRVLLLDEPTNHLDIET--------IDWLEgflktfNGTIIFISHDRSFIRNmATRIVDLDRGKL 231
Cdd:cd03248 157 QRVAIARALIRNPQVLILDEATSALDAESeqqvqqalYDWPE------RRTVLVIAHRLSTVER-ADQILVLDGGRI 226
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
12-231 1.30e-12

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 69.34  E-value: 1.30e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   12 SFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYE-QDliVARLQ-QDppRNV---------- 79
Cdd:PRK10851  11 SFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHgTD--VSRLHaRD--RKVgfvfqhyalf 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   80 -EGSVYDFVAEGIEeqaeYLKRYHDISRLVMNdpseknlnelAKVQEQLDHHNLWQLENRInevlaqlgldPnvalSSLS 158
Cdd:PRK10851  87 rHMTVFDNIAFGLT----VLPRRERPNAAAIK----------AKVTQLLEMVQLAHLADRY----------P----AQLS 138
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15830287  159 GGWLRKAALGRALVSNPRVLLLDEPTNHLDI----ETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKL 231
Cdd:PRK10851 139 GGQKQRVALARALAVEPQILLLDEPFGALDAqvrkELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNI 215
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
12-231 1.45e-12

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 68.17  E-value: 1.45e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   12 SFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILnreQGL-------------------DDGRIIYeQDlivARLQ 72
Cdd:PRK11247  21 RYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLL---AGLetpsagellagtaplaearEDTRLMF-QD---ARLL 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   73 qdPPRnvegSVYDFVAEGIEeqaeylkryhdisrlvmNDPSEKNLNELAKVQeqldhhnlwqLENRINEVLAqlgldpnv 152
Cdd:PRK11247  94 --PWK----KVIDNVGLGLK-----------------GQWRDAALQALAAVG----------LADRANEWPA-------- 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  153 alsSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLD----IETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDR 228
Cdd:PRK11247 133 ---ALSGGQKQRVALARALIHRPGLLLLDEPLGALDaltrIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEE 209

                 ...
gi 15830287  229 GKL 231
Cdd:PRK11247 210 GKI 212
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
24-232 1.86e-12

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: 67.31  E-value: 1.86e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  24 LHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYE-QDLivarLQQDPPRNVE-GSVYdfVAEG--------IEE 93
Cdd:COG0410  24 LEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDgEDI----TGLPPHRIARlGIGY--VPEGrrifpsltVEE 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  94 qaeylkryhdisrlvmndpsekNLnELAKVQEQLDHHNLWQLEN------RINEVLAQLGldpnvalSSLSGGWLRKAAL 167
Cdd:COG0410  98 ----------------------NL-LLGAYARRDRAEVRADLERvyelfpRLKERRRQRA-------GTLSGGEQQMLAI 147
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15830287 168 GRALVSNPRVLLLDEPTNHL------DI-ETIDWL--EGFlktfngTIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:COG0410 148 GRALMSRPKLLLLDEPSLGLapliveEIfEIIRRLnrEGV------TILLVEQNARFALEIADRAYVLERGRIV 215
cbiO TIGR01166
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ...
330-496 1.96e-12

cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 130234 [Multi-domain]  Cd Length: 190  Bit Score: 66.29  E-value: 1.96e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   330 DGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKlEVAY----FDQHRAEL-----DPDK-- 398
Cdd:TIGR01166   3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGE-PLDYsrkgLLERRQRVglvfqDPDDql 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   399 ---TVMDNLA-----EGKQEVMVNGKPRHVLGYLqDFLFHPKRamtPVRALSGGERNRLLLA-RLFLKPsNLLILDEPTN 469
Cdd:TIGR01166  82 faaDVDQDVAfgplnLGLSEAEVERRVREALTAV-GASGLRER---PTHCLSGGEKKRVAIAgAVAMRP-DVLLLDEPTA 156
                         170       180       190
                  ....*....|....*....|....*....|
gi 15830287   470 DLDVETLELLEELIDSY--QG-TVLLVSHD 496
Cdd:TIGR01166 157 GLDPAGREQMLAILRRLraEGmTVVISTHD 186
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
335-468 2.22e-12

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: 66.93  E-value: 2.22e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 335 VKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVG----TKLE--------VAYFDQHRaELDPDKTVMD 402
Cdd:COG0410  19 LHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDgediTGLPphriarlgIGYVPEGR-RIFPSLTVEE 97
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 403 NLAEGKQEVMVNGKPRHVLGYLQDfLFhPK---RAMTPVRALSGGERNRLLLAR-LFLKPSnLLILDEPT 468
Cdd:COG0410  98 NLLLGAYARRDRAEVRADLERVYE-LF-PRlkeRRRQRAGTLSGGEQQMLAIGRaLMSRPK-LLLLDEPS 164
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
11-232 2.40e-12

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 67.71  E-value: 2.40e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   11 LSFS----DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKIL----NREQG--LDDGRIIYEQDLIVAR-----LQQDP 75
Cdd:PRK13632  13 VSFSypnsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILtgllKPQSGeiKIDGITISKENLKEIRkkigiIFQNP 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   76 PRNVEGS-VYDFVAEGIEEqaeylKRyhdISRLVMNDPseknLNELAKV---QEQLDHhnlwqlenrinevlaqlglDPn 151
Cdd:PRK13632  93 DNQFIGAtVEDDIAFGLEN-----KK---VPPKKMKDI----IDDLAKKvgmEDYLDK-------------------EP- 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  152 valSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLD-------IETIDWLEgflKTFNGTIIFISHDRSFIRNmATRIV 224
Cdd:PRK13632 141 ---QNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDpkgkreiKKIMVDLR---KTRKKTLISITHDMDEAIL-ADKVI 213

                 ....*...
gi 15830287  225 DLDRGKLV 232
Cdd:PRK13632 214 VFSEGKLI 221
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
14-212 2.53e-12

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 67.47  E-value: 2.53e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   14 SDAPL-LDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLI-----------VARLQQDPPRNVEG 81
Cdd:PRK13648  19 SDASFtLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAItddnfeklrkhIGIVFQNPDNQFVG 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   82 SVYDF-VAEGIEEQAEylkryhdisrlvmndPSEKNLNELAKVQEQLDhhnlwqlenrineVLAQLGLDPNvalsSLSGG 160
Cdd:PRK13648  99 SIVKYdVAFGLENHAV---------------PYDEMHRRVSEALKQVD-------------MLERADYEPN----ALSGG 146
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15830287  161 WLRKAALGRALVSNPRVLLLDEPTNHLDIET----IDWLEGFLKTFNGTIIFISHD 212
Cdd:PRK13648 147 QKQRVAIAGVLALNPSVIILDEATSMLDPDArqnlLDLVRKVKSEHNITIISITHD 202
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
19-237 2.60e-12

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 69.75  E-value: 2.60e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGriIYE---QDliVARLQQDPPRNVEGSVYDFVaegieeqa 95
Cdd:PRK10535  24 LKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSG--TYRvagQD--VATLDADALAQLRREHFGFI-------- 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   96 eyLKRYHDISRLVmndpSEKNLnELAKVQEQLDHHnlwQLENRINEVLAQLGLDPNVAL--SSLSGGWLRKAALGRALVS 173
Cdd:PRK10535  92 --FQRYHLLSHLT----AAQNV-EVPAVYAGLERK---QRLLRAQELLQRLGLEDRVEYqpSQLSGGQQQRVSIARALMN 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15830287  174 NPRVLLLDEPTNHLDIETIDWLEGFLKTFNG---TIIFISHDRSfIRNMATRIVDLDRGKLVTYPGN 237
Cdd:PRK10535 162 GGQVILADEPTGALDSHSGEEVMAILHQLRDrghTVIIVTHDPQ-VAAQAERVIEIRDGEIVRNPPA 227
TauB COG4525
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
332-472 3.33e-12

ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 443596 [Multi-domain]  Cd Length: 262  Bit Score: 67.19  E-value: 3.33e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 332 KQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV------GTKLEVAYFDQHRAeLDPDKTVMDNLA 405
Cdd:COG4525  20 QPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLdgvpvtGPGADRGVVFQKDA-LLPWLNVLDNVA 98
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15830287 406 EGKQevmVNGKPRH-----------VLGyLQDFlfhpkrAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:COG4525  99 FGLR---LRGVPKAerraraeellaLVG-LADF------ARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALD 166
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
320-467 3.52e-12

ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.


Pssm-ID: 213217 [Multi-domain]  Cd Length: 204  Bit Score: 65.95  E-value: 3.52e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 320 FEMEDVCYQVDGKQ-----LVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKleVAY-------- 386
Cdd:cd03250   1 ISVEDASFTWDSGEqetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS--IAYvsqepwiq 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 387 -------------FDQHRAE-------LDPDktvMDNLAEGKQ-EVMVNGkprhvlgylqdflfhpkramtpvRALSGGE 445
Cdd:cd03250  79 ngtirenilfgkpFDEERYEkvikacaLEPD---LEILPDGDLtEIGEKG-----------------------INLSGGQ 132
                       170       180
                ....*....|....*....|..
gi 15830287 446 RNRLLLARLFLKPSNLLILDEP 467
Cdd:cd03250 133 KQRISLARAVYSDADIYLLDDP 154
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
320-496 3.69e-12

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 67.12  E-value: 3.69e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  320 FEMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKlMLGQLQ-ADSGRIHVGTKL-----------EVAYF 387
Cdd:PRK10575  12 FALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLK-MLGRHQpPSEGEILLDAQPleswsskafarKVAYL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  388 DQhraELDPdktvmdnlAEG---KQEVMVNGKPRHvlGYLQDFLFHPKR---------AMTP-----VRALSGGERNRLL 450
Cdd:PRK10575  91 PQ---QLPA--------AEGmtvRELVAIGRYPWH--GALGRFGAADREkveeaislvGLKPlahrlVDSLSGGERQRAW 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 15830287  451 LARLFLKPSNLLILDEPTNDLDVETLELLEELID--SYQG--TVLLVSHD 496
Cdd:PRK10575 158 IAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHrlSQERglTVIAVLHD 207
CeuD COG4604
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ...
321-496 3.82e-12

ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 443654 [Multi-domain]  Cd Length: 252  Bit Score: 66.65  E-value: 3.82e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 321 EMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGtKLEVAYFdqhraeldPDKTV 400
Cdd:COG4604   3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVD-GLDVATT--------PSREL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 401 MDNLAEGKQEVMVN------------------GKP-----RHV---LGYLQdflfhpkraMTPVRA-----LSGGERNRL 449
Cdd:COG4604  74 AKRLAILRQENHINsrltvrelvafgrfpyskGRLtaedrEIIdeaIAYLD---------LEDLADryldeLSGGQRQRA 144
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 15830287 450 LLARLFLKPSNLLILDEPTNDLD----VETLELLEELIDSYQGTVLLVSHD 496
Cdd:COG4604 145 FIAMVLAQDTDYVLLDEPLNNLDmkhsVQMMKLLRRLADELGKTVVIVLHD 195
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
3-496 3.94e-12

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 68.92  E-value: 3.94e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287    3 LISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIiyeqdlivarlqqdpprNVEGS 82
Cdd:PRK15439  11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTL-----------------EIGGN 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   83 VYdfvAEGIEEQAEYLKRYhdisrLVmndPSEKNLNELAKVQEQ----LDHHNLwqLENRINEVLAQLG--LDPNVALSS 156
Cdd:PRK15439  74 PC---ARLTPAKAHQLGIY-----LV---PQEPLLFPNLSVKENilfgLPKRQA--SMQKMKQLLAALGcqLDLDSSAGS 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  157 LSGGWLRKAALGRALVSNPRVLLLDEPTNHLD-IET---IDWLEGFLKTFNGtIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:PRK15439 141 LEVADRQIVEILRGLMRDSRILILDEPTASLTpAETerlFSRIRELLAQGVG-IVFISHKLPEIRQLADRISVMRDGTIA 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  233 typgnydqyLLEKEEALRVEELQNAefdrklaqeevwirqgiKARRTRNEGRVRALKA-MRRERGERREVMGTAKMQVEE 311
Cdd:PRK15439 220 ---------LSGKTADLSTDDIIQA-----------------ITPAAREKSLSASQKLwLELPGNRRQQAAGAPVLTVED 273
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  312 ASRSGkivfemedvcyqvdgkqlVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIhvgtklevaYFDQHr 391
Cdd:PRK15439 274 LTGEG------------------FRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRI---------MLNGK- 325
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  392 aELDPDKTVmDNLAEGkqeVMVNGKPRHVLG-YL---------------QDFLFHPKR------------------AMTP 437
Cdd:PRK15439 326 -EINALSTA-QRLARG---LVYLPEDRQSSGlYLdaplawnvcalthnrRGFWIKPARenavleryrralnikfnhAEQA 400
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15830287  438 VRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELIDSY--QGT-VLLVSHD 496
Cdd:PRK15439 401 ARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIaaQNVaVLFISSD 462
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
17-211 4.24e-12

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 65.67  E-value: 4.24e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   17 PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQdlivarlqqdpprnvEGSVYDFVAEgieeQAE 96
Cdd:PRK13539  16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG---------------GDIDDPDVAE----ACH 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   97 YLkryhdisrlvmndpSEKN-LNELAKVQEQLDhhnLW-----QLENRINEVLAQLGLDP--NVALSSLSGGWLRKAALG 168
Cdd:PRK13539  77 YL--------------GHRNaMKPALTVAENLE---FWaaflgGEELDIAAALEAVGLAPlaHLPFGYLSAGQKRRVALA 139
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 15830287  169 RALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTF---NGTIIFISH 211
Cdd:PRK13539 140 RLLVSNRPIWILDEPTAALDAAAVALFAELIRAHlaqGGIVIAATH 185
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
333-495 4.76e-12

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: 65.85  E-value: 4.76e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 333 QLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIhvgtklEVAYFDQHRAELD--------PDK------ 398
Cdd:cd03266  19 QAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFA------TVDGFDVVKEPAEarrrlgfvSDStglydr 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 399 -TVMDNLA-----EGKQEVMVNGKPRHVLGYLQDFLFHPKRamtpVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:cd03266  93 lTARENLEyfaglYGLKGDELTARLEELADRLGMEELLDRR----VGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLD 168
                       170       180
                ....*....|....*....|....*.
gi 15830287 473 VETLELLEELIDSY---QGTVLLVSH 495
Cdd:cd03266 169 VMATRALREFIRQLralGKCILFSTH 194
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
321-516 4.93e-12

putative amino-acid ABC transporter ATP-binding protein YecC; Provisional


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 66.31  E-value: 4.93e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  321 EMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVG------------TKLEVAYFD 388
Cdd:PRK11264   5 EVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGditidtarslsqQKGLIRQLR 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  389 QHRA------ELDPDKTVMDNLAEGKqeVMVNGKPRHVLGYLQDFLFHP-----KRAMTPvRALSGGERNRLLLARLFLK 457
Cdd:PRK11264  85 QHVGfvfqnfNLFPHRTVLENIIEGP--VIVKGEPKEEATARARELLAKvglagKETSYP-RRLSGGQQQRVAIARALAM 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15830287  458 PSNLLILDEPTNDLDVETLELLEELIDSY---QGTVLLVSHDRQFVDNtVTECWIFEGGGKI 516
Cdd:PRK11264 162 RPEVILFDEPTSALDPELVGEVLNTIRQLaqeKRTMVIVTHEMSFARD-VADRAIFMDQGRI 222
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
21-250 6.00e-12

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 65.93  E-value: 6.00e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  21 NAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYE-QDliVARLqqdPP--RNV-----EG------SVYDF 86
Cdd:COG3840  17 RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNgQD--LTAL---PPaeRPVsmlfqENnlfphlTVAQN 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  87 VAEGIeeqaeylkryhdisrlvmnDPSEKnLNELAKvqeqldhhnlwqleNRINEVLAQLGLD------PnvalSSLSGG 160
Cdd:COG3840  92 IGLGL-------------------RPGLK-LTAEQR--------------AQVEQALERVGLAglldrlP----GQLSGG 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 161 WLRKAALGRALVSNPRVLLLDEPTNHLDI----ETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKlVTYPG 236
Cdd:COG3840 134 QRQRVALARCLVRKRPILLLDEPFSALDPalrqEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGR-IAADG 212
                       250
                ....*....|....*
gi 15830287 237 NYDQYL-LEKEEALR 250
Cdd:COG3840 213 PTAALLdGEPPPALA 227
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
320-498 6.22e-12

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


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 65.20  E-value: 6.22e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 320 FEMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQAD---SGRIhvgtklevaYFDQHRaeldp 396
Cdd:COG4136   2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEV---------LLNGRR----- 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 397 dktvmdnLAEGKQEvmvngkPRHVlGYL-QDFLFHP----------------KRAMTPVRA------------------- 440
Cdd:COG4136  68 -------LTALPAE------QRRI-GILfQDDLLFPhlsvgenlafalpptiGRAQRRARVeqaleeaglagfadrdpat 133
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15830287 441 LSGGERNRLLLAR-LFLKPSNLLiLDEPTNDLDVETLELLEE----LIDSYQGTVLLVSHDRQ 498
Cdd:COG4136 134 LSGGQRARVALLRaLLAEPRALL-LDEPFSKLDAALRAQFREfvfeQIRQRGIPALLVTHDEE 195
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
3-473 6.46e-12

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 68.42  E-value: 6.46e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287    3 LISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILN--REQGLDDGRIIYEQDLIVARlqqdpprnve 80
Cdd:PRK13549   5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSgvYPHGTYEGEIIFEGEELQAS---------- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   81 gSVYDFVAEGI----EEQAeylkryhdisrLVMNDPSEKNL---NELAKvQEQLDHHNLWQlenRINEVLAQLGLDPNVA 153
Cdd:PRK13549  75 -NIRDTERAGIaiihQELA-----------LVKELSVLENIflgNEITP-GGIMDYDAMYL---RAQKLLAQLKLDINPA 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  154 L--SSLSGGWLRKAALGRALVSNPRVLLLDEPTNHL-DIET---IDWLEGfLKTFNGTIIFISHDRSFIRNMATRIVDLD 227
Cdd:PRK13549 139 TpvGNLGLGQQQLVEIAKALNKQARLLILDEPTASLtESETavlLDIIRD-LKAHGIACIYISHKLNEVKAISDTICVIR 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  228 RGKLV-TYPGnydqyllekeealrveelqnaefdRKLAQEEVwIRQGIKarrtrnegrvRALKAMRRergerrevmgtak 306
Cdd:PRK13549 218 DGRHIgTRPA------------------------AGMTEDDI-ITMMVG----------RELTALYP------------- 249
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  307 mqvEEASRSGKIVFEMEDV-CYQVD--GKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQ-ADSGRIHV-GTK 381
Cdd:PRK13549 250 ---REPHTIGEVILEVRNLtAWDPVnpHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIdGKP 326
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  382 LEV-----------AYF--DQHRAELDPDKTVMDN--LAEGKQEV---MVNG--KPRHVLGYLQDFLFHPKRAMTPVRAL 441
Cdd:PRK13549 327 VKIrnpqqaiaqgiAMVpeDRKRDGIVPVMGVGKNitLAALDRFTggsRIDDaaELKTILESIQRLKVKTASPELAIARL 406
                        490       500       510
                 ....*....|....*....|....*....|..
gi 15830287  442 SGGERNRLLLARLFLKPSNLLILDEPTNDLDV 473
Cdd:PRK13549 407 SGGNQQKAVLAKCLLLNPKILILDEPTRGIDV 438
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
12-232 6.54e-12

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 67.55  E-value: 6.54e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   12 SFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYE-QDLIVARLQQDPPRNVEGSVYDFVAEG 90
Cdd:PRK11607  28 SFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDgVDLSHVPPYQRPINMMFQSYALFPHMT 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   91 IEEQAEYLKRYHDISRLVMNDpseknlnelaKVQEQLDHHNLWQLENRinevlaqlglDPNvalsSLSGGWLRKAALGRA 170
Cdd:PRK11607 108 VEQNIAFGLKQDKLPKAEIAS----------RVNEMLGLVHMQEFAKR----------KPH----QLSGGQRQRVALARS 163
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  171 LVSNPRVLLLDEPTNHLD--------IETIDWLEgflkTFNGTIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:PRK11607 164 LAKRPKLLLLDEPMGALDkklrdrmqLEVVDILE----RVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFV 229
LPS_export_lptB TIGR04406
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ...
319-467 6.82e-12

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: 65.76  E-value: 6.82e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   319 VFEMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI------------HVGTKLEVAY 386
Cdd:TIGR04406   1 TLVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKIlidgqdithlpmHERARLGIGY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   387 FDQHrAELDPDKTVMDNLA---EGKQEVMVNGKPRHVLGYLQDF-LFHPKRAmtPVRALSGGERNRLLLARLFLKPSNLL 462
Cdd:TIGR04406  81 LPQE-ASIFRKLTVEENIMavlEIRKDLDRAEREERLEALLEEFqISHLRDN--KAMSLSGGERRRVEIARALATNPKFI 157

                  ....*
gi 15830287   463 ILDEP 467
Cdd:TIGR04406 158 LLDEP 162
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
12-232 7.66e-12

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: 65.08  E-value: 7.66e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  12 SFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIyeqdlivarlqqdpprnVEGsvYDFVAEGI 91
Cdd:cd03265   9 KYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRAT-----------------VAG--HDVVREPR 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  92 EEQAEylkryhdISrLVMNDPSEKNlnELAKVQEQLDHHNLW-----QLENRINEVLAQLGL--DPNVALSSLSGGWLRK 164
Cdd:cd03265  70 EVRRR-------IG-IVFQDLSVDD--ELTGWENLYIHARLYgvpgaERRERIDELLDFVGLleAADRLVKTYSGGMRRR 139
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15830287 165 AALGRALVSNPRVLLLDEPTNHLDIETID--W--LEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:cd03265 140 LEIARSLVHRPEVLFLDEPTIGLDPQTRAhvWeyIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRII 211
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
331-467 7.81e-12

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


Pssm-ID: 440752 [Multi-domain]  Cd Length: 240  Bit Score: 65.44  E-value: 7.81e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 331 GKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIhvgtklevaYFDQH---------RAEL------- 394
Cdd:COG1137  15 KRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRI---------FLDGEdithlpmhkRARLgigylpq 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 395 DP----DKTVMDNLAEGKQEVMVNGKPRH--VLGYLQDF-LFHPKRamTPVRALSGGERNRLLLAR-LFLKPSNLLiLDE 466
Cdd:COG1137  86 EAsifrKLTVEDNILAVLELRKLSKKEREerLEELLEEFgITHLRK--SKAYSLSGGERRRVEIARaLATNPKFIL-LDE 162

                .
gi 15830287 467 P 467
Cdd:COG1137 163 P 163
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
14-229 8.11e-12

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 67.91  E-value: 8.11e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  14 SDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNreqGL---DDGRIIYEQDLIVARLQQDP--PrnvEGS-----V 83
Cdd:COG4178 374 DGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIA---GLwpyGSGRIARPAGARVLFLPQRPylP---LGTlrealL 447
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  84 YDFVAEGIEEQAeylkrYHDISRLVmndpsekNLNELAkvqEQLDHHNLWQLEnrinevlaqlgldpnvalssLSGGWLR 163
Cdd:COG4178 448 YPATAEAFSDAE-----LREALEAV-------GLGHLA---ERLDEEADWDQV--------------------LSLGEQQ 492
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15830287 164 KAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKT--FNGTIIFISHdRSFIRNMATRIVDLDRG 229
Cdd:COG4178 493 RLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREelPGTTVISVGH-RSTLAAFHDRVLELTGD 559
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
338-495 9.99e-12

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 64.99  E-value: 9.99e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  338 FSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI------HVGT---KLEVAYFDQHRaELDPDKTVMDNLAEGK 408
Cdd:PRK10771  18 FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLtlngqdHTTTppsRRPVSMLFQEN-NLFSHLTVAQNIGLGL 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  409 QE-VMVNGKPRHVLGY------LQDFLfhpkrAMTPvRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEE 481
Cdd:PRK10771  97 NPgLKLNAAQREKLHAiarqmgIEDLL-----ARLP-GQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLT 170
                        170
                 ....*....|....*...
gi 15830287  482 LIDSY----QGTVLLVSH 495
Cdd:PRK10771 171 LVSQVcqerQLTLLMVSH 188
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
311-498 1.01e-11

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 65.45  E-value: 1.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  311 EASRSGKIVFEMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKleVAYFDQH 390
Cdd:PRK14246   2 EAGKSAEDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGK--VLYFGKD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  391 RAELD------------------PDKTVMDNLAEGKQEVMVNGKpRHVLGYLQDFLFHP-------KRAMTPVRALSGGE 445
Cdd:PRK14246  80 IFQIDaiklrkevgmvfqqpnpfPHLSIYDNIAYPLKSHGIKEK-REIKKIVEECLRKVglwkevyDRLNSPASQLSGGQ 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15830287  446 RNRLLLAR-LFLKPsNLLILDEPTNDLDVETLELLEELIDSYQG--TVLLVSHDRQ 498
Cdd:PRK14246 159 QQRLTIARaLALKP-KVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHNPQ 213
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
321-496 1.01e-11

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 65.49  E-value: 1.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  321 EMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV------GTKLEVAYFDQHRAEL 394
Cdd:PRK11248   3 QISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLdgkpveGPGAERGVVFQNEGLL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  395 dPDKTVMDNLAEGKQEVMVNGKPRHVLGylQDFL-------FHPKRamtpVRALSGGERNRLLLARLFLKPSNLLILDEP 467
Cdd:PRK11248  83 -PWRNVQDNVAFGLQLAGVEKMQRLEIA--HQMLkkvglegAEKRY----IWQLSGGQRQRVGIARALAANPQLLLLDEP 155
                        170       180       190
                 ....*....|....*....|....*....|...
gi 15830287  468 TNDLDV-ETLELLEELIDSYQGT---VLLVSHD 496
Cdd:PRK11248 156 FGALDAfTREQMQTLLLKLWQETgkqVLLITHD 188
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
30-240 1.15e-11

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 67.68  E-value: 1.15e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   30 ERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYE----QDLIVARLqqdppRNVEGSVYdfvaegieEQAEYLKR-YHDI 104
Cdd:PRK13657 362 QTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDgtdiRTVTRASL-----RRNIAVVF--------QDAGLFNRsIEDN 428
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  105 SRLVMNDPSEKNLNELAKVQEQLDHhnlwqLENRINevlaqlGLDPNVAL--SSLSGGWLRKAALGRALVSNPRVLLLDE 182
Cdd:PRK13657 429 IRVGRPDATDEEMRAAAERAQAHDF-----IERKPD------GYDTVVGErgRQLSGGERQRLAIARALLKDPPILILDE 497
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  183 PTNHLDIETIDWLEGFLKTF--NGTIIFISHDRSFIRNmATRIVDLDRGKLVTyPGNYDQ 240
Cdd:PRK13657 498 ATSALDVETEAKVKAALDELmkGRTTFIIAHRLSTVRN-ADRILVFDNGRVVE-SGSFDE 555
COG4559 COG4559
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
11-232 1.30e-11

ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 443620 [Multi-domain]  Cd Length: 258  Bit Score: 65.14  E-value: 1.30e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  11 LSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYE---------QDLivAR----LQQDPPR 77
Cdd:COG4559   9 VRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNgrplaawspWEL--ARrravLPQHSSL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  78 NVEGSVYDFVAEGIEEQAEYLKRYHDISRLVMndpseknlnelakvqEQLDhhnLWQLENRinevlaqlgldpnvALSSL 157
Cdd:COG4559  87 AFPFTVEEVVALGRAPHGSSAAQDRQIVREAL---------------ALVG---LAHLAGR--------------SYQTL 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 158 SGGWLRKAALGRALV-------SNPRVLLLDEPTNHLDI----ETIDWLEGFLKTfNGTIIFISHDrsfiRNMAT----R 222
Cdd:COG4559 135 SGGEQQRVQLARVLAqlwepvdGGPRWLFLDEPTSALDLahqhAVLRLARQLARR-GGGVVAVLHD----LNLAAqyadR 209
                       250
                ....*....|
gi 15830287 223 IVDLDRGKLV 232
Cdd:COG4559 210 ILLLHQGRLV 219
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
11-232 1.73e-11

ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.


Pssm-ID: 213214 [Multi-domain]  Cd Length: 178  Bit Score: 63.10  E-value: 1.73e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  11 LSFS----DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIyeqdlivarLQQDPPRNVEGSVYDF 86
Cdd:cd03247   6 VSFSypeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEIT---------LDGVPVSDLEKALSSL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  87 VaeGIEEQAEYLkryhdisrlvMNDPSEKNLNElakvqeqldhhnlwqlenrinevlaqlgldpnvalsSLSGGWLRKAA 166
Cdd:cd03247  77 I--SVLNQRPYL----------FDTTLRNNLGR------------------------------------RFSGGERQRLA 108
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 167 LGRALVSNPRVLLLDEPTNHLDIET----IDWLEGFLKtfNGTIIFISHDRSFIRNMaTRIVDLDRGKLV 232
Cdd:cd03247 109 LARILLQDAPIVLLDEPTVGLDPITerqlLSLIFEVLK--DKTLIWITHHLTGIEHM-DKILFLENGKII 175
ABC_tran_Xtn pfam12848
ABC transporter; This domain is an extension of some members of pfam00005 and other ...
224-291 2.00e-11

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: 60.28  E-value: 2.00e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   224 VDLDRGKLVTYPGNYDQYLLEKEEALRVEELQNAEFDRKLAQEEVWI-RQGIKARRTR-NEGRVRALKAM 291
Cdd:pfam12848   1 VELERGKLTTYKGNYSTFLEQKEERLEQQEKAYEKQQKEIKKLEEFIdRFRAKASKAKqAQSRIKALEKM 70
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
14-234 2.04e-11

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 64.82  E-value: 2.04e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   14 SDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNreqglddGRIIYEQDLIVARLQQDPPRNVEgSVYDFVAegiee 93
Cdd:PRK13652  15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFN-------GILKPTSGSVLIRGEPITKENIR-EVRKFVG----- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   94 qaeylkryhdisrLVMNDPSEKNLNELAKVQEQLDHHNLW----QLENRINEVLAQLGLDP--NVALSSLSGGWLRKAAL 167
Cdd:PRK13652  82 -------------LVFQNPDDQIFSPTVEQDIAFGPINLGldeeTVAHRVSSALHMLGLEElrDRVPHHLSGGEKKRVAI 148
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15830287  168 GRALVSNPRVLLLDEPTNHLD----IETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKLVTY 234
Cdd:PRK13652 149 AGVIAMEPQVLVLDEPTAGLDpqgvKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAY 219
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
349-498 2.08e-11

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: 65.90  E-value: 2.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   349 ALIGPNGCGKTTLLKLMLGQLQADSGRIHV-GTKLE--------------VAYFDQhRAELDPDKTVMDNLAEGKQEVMV 413
Cdd:TIGR02142  27 AIFGRSGSGKTTLIRLIAGLTRPDEGEIVLnGRTLFdsrkgiflppekrrIGYVFQ-EARLFPHLSVRGNLRYGMKRARP 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   414 ---NGKPRHVLGYLQdfLFHPKRamTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELI----DSY 486
Cdd:TIGR02142 106 serRISFERVIELLG--IGHLLG--RLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLerlhAEF 181
                         170
                  ....*....|..
gi 15830287   487 QGTVLLVSHDRQ 498
Cdd:TIGR02142 182 GIPILYVSHSLQ 193
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
136-231 2.81e-11

Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.


Pssm-ID: 213182 [Multi-domain]  Cd Length: 182  Bit Score: 62.83  E-value: 2.81e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 136 ENRINE-VLAQLGLDPNVALSS-LSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTF---NGTIIFIS 210
Cdd:cd03215  82 EDRKREgLVLDLSVAENIALSSlLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELadaGKAVLLIS 161
                        90       100
                ....*....|....*....|.
gi 15830287 211 HDRSFIRNMATRIVDLDRGKL 231
Cdd:cd03215 162 SELDELLGLCDRILVMYEGRI 182
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
316-473 2.94e-11

Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.


Pssm-ID: 213182 [Multi-domain]  Cd Length: 182  Bit Score: 62.45  E-value: 2.94e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 316 GKIVFEMEDVCyqvdGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVG------------TKLE 383
Cdd:cd03215   1 GEPVLEVRGLS----VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDgkpvtrrsprdaIRAG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 384 VAYF--DQHRAELDPDKTVMDNLAegkqevmvngkprhvLGYLqdflfhpkramtpvraLSGGERNRLLLARLFLKPSNL 461
Cdd:cd03215  77 IAYVpeDRKREGLVLDLSVAENIA---------------LSSL----------------LSGGNQQKVVLARWLARDPRV 125
                       170
                ....*....|..
gi 15830287 462 LILDEPTNDLDV 473
Cdd:cd03215 126 LILDEPTRGVDV 137
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
11-232 3.77e-11

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 64.02  E-value: 3.77e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   11 LSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRI-IYEQDlivarLQQDPPRnvegsvydfvae 89
Cdd:PRK13548  10 VRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVrLNGRP-----LADWSPA------------ 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   90 gieEQAeylKRyhdisRLVMndPSEKNLNELAKVQE----QLDHHNLWQLENR--INEVLAQLGLDP--NVALSSLSGGW 161
Cdd:PRK13548  73 ---ELA---RR-----RAVL--PQHSSLSFPFTVEEvvamGRAPHGLSRAEDDalVAAALAQVDLAHlaGRDYPQLSGGE 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  162 LRKAALGRALV------SNPRVLLLDEPTNHLDI----ETIDWLEGFLKTFNGTIIFISHDrsfiRNMAT----RIVDLD 227
Cdd:PRK13548 140 QQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLahqhHVLRLARQLAHERGLAVIVVLHD----LNLAAryadRIVLLH 215

                 ....*
gi 15830287  228 RGKLV 232
Cdd:PRK13548 216 QGRLV 220
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
319-472 3.82e-11

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 64.27  E-value: 3.82e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  319 VFEMEDVCYQVDG--KQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV-GTKLEVAYFDQHRAEL- 394
Cdd:PRK13635   5 IIRVEHISFRYPDaaTYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVgGMVLSEETVWDVRRQVg 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  395 ----DPDK-----TVMDNLAEGKQEvmvNGKPR-----------HVLGyLQDFLFH-PKRamtpvraLSGGERNRLLLAR 453
Cdd:PRK13635  85 mvfqNPDNqfvgaTVQDDVAFGLEN---IGVPReemvervdqalRQVG-MEDFLNRePHR-------LSGGQKQRVAIAG 153
                        170       180
                 ....*....|....*....|
gi 15830287  454 -LFLKPSnLLILDEPTNDLD 472
Cdd:PRK13635 154 vLALQPD-IIILDEATSMLD 172
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
24-232 6.01e-11

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: 62.51  E-value: 6.01e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  24 LHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRI-IYEQDLIVArlqqDPPRNVEGSVY---DFVAEGIEEQAEYLK 99
Cdd:cd03298  19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVlINGVDVTAA----PPADRPVSMLFqenNLFAHLTVEQNVGLG 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 100 RyhdisrlvmnDPSEKnlneLAKVQEQldhhnlwqlenRINEVLAQLGLDPNVAL--SSLSGGWLRKAALGRALVSNPRV 177
Cdd:cd03298  95 L----------SPGLK----LTAEDRQ-----------AIEVALARVGLAGLEKRlpGELSGGERQRVALARVLVRDKPV 149
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15830287 178 LLLDEPTNHLD----IETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:cd03298 150 LLLDEPFAALDpalrAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIA 208
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
11-226 6.02e-11

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 63.52  E-value: 6.02e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   11 LSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLD-----DGRI------IYEQDLIVARLQQD----- 74
Cdd:PRK14258  15 FYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVeffnqnIYERRVNLNRLRRQvsmvh 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   75 -PPRNVEGSVYDFVAEGIEeqaeyLKRYHdiSRLVMNDpseknlnelaKVQEQLDHHNLWqleNRINEVLAQLGLDpnva 153
Cdd:PRK14258  95 pKPNLFPMSVYDNVAYGVK-----IVGWR--PKLEIDD----------IVESALKDADLW---DEIKHKIHKSALD---- 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15830287  154 lssLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFN----GTIIFISHDRSFIrnmaTRIVDL 226
Cdd:PRK14258 151 ---LSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlrseLTMVIVSHNLHQV----SRLSDF 220
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
330-472 6.19e-11

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 65.21  E-value: 6.19e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 330 DGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKLEVAYFDQ----------------HRAE 393
Cdd:COG4178 374 DGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGARVLFLPQrpylplgtlreallypATAE 453
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 394 LDPDKTVMDNLAEgkqevmVNgkprhvLGYLQDFLFHPKRAMtpvRALSGGERNRLLLARLFL-KPSnLLILDEPTNDLD 472
Cdd:COG4178 454 AFSDAELREALEA------VG------LGHLAERLDEEADWD---QVLSLGEQQRLAFARLLLhKPD-WLFLDEATSALD 517
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
332-473 6.28e-11

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 63.11  E-value: 6.28e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  332 KQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKLEVAYFDQHRAE---LDPDKTVMdnlAEG- 407
Cdd:PRK11231  15 KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARrlaLLPQHHLT---PEGi 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  408 -KQEVMVNGKPRHV--LGYL-QDFLFHPKRAMT----------PVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDV 473
Cdd:PRK11231  92 tVRELVAYGRSPWLslWGRLsAEDNARVNQAMEqtrinhladrRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDI 171
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
334-497 6.57e-11

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127 [Multi-domain]  Cd Length: 200  Bit Score: 62.27  E-value: 6.57e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  334 LVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV---GTKLEVAYFDQ------HRAELDPDKTVMDNL 404
Cdd:PRK13540  16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFerqSIKKDLCTYQKqlcfvgHRSGINPYLTLRENC 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  405 ---------AEGKQEVMVNGKprhvLGYLQDFlfhpkramtPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVET 475
Cdd:PRK13540  96 lydihfspgAVGITELCRLFS----LEHLIDY---------PCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELS 162
                        170       180
                 ....*....|....*....|....*
gi 15830287  476 LELLEELIDSYQ---GTVLLVSHDR 497
Cdd:PRK13540 163 LLTIITKIQEHRakgGAVLLTSHQD 187
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
18-212 6.71e-11

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 62.49  E-value: 6.71e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   18 LLDNAELHIEDNERVCLVGRNGAGKSTLMKILnreQGLDDGRIiYEQDLIVARLQQdpprnvegsvydfvaegIEEQAEY 97
Cdd:PRK10584  25 ILTGVELVVKRGETIALIGESGSGKSTLLAIL---AGLDDGSS-GEVSLVGQPLHQ-----------------MDEEARA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   98 LKRYHDISRLVMNDPSEKNLNELAKVQ--EQLDHHNLWQLENRINEVLAQLGLDPNVAL--SSLSGGWLRKAALGRALVS 173
Cdd:PRK10584  84 KLRAKHVGFVFQSFMLIPTLNALENVElpALLRGESSRQSRNGAKALLEQLGLGKRLDHlpAQLSGGEQQRVALARAFNG 163
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 15830287  174 NPRVLLLDEPTNHLDIETIDWLEGFLKTFN----GTIIFISHD 212
Cdd:PRK10584 164 RPDVLFADEPTGNLDRQTGDKIADLLFSLNrehgTTLILVTHD 206
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
329-472 8.16e-11

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


Pssm-ID: 440718 [Multi-domain]  Cd Length: 264  Bit Score: 62.80  E-value: 8.16e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 329 VDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKlEVAYFDQH-RAEL------DP----- 396
Cdd:COG1101  16 VNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGK-DVTKLPEYkRAKYigrvfqDPmmgta 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 397 -DKTVMDNLA----EGKQEVMVNGKPRHVLGYLQDFLFH-----PKRAMTPVRALSGGERNRLLLARLFLKPSNLLILDE 466
Cdd:COG1101  95 pSMTIEENLAlayrRGKRRGLRRGLTKKRRELFRELLATlglglENRLDTKVGLLSGGQRQALSLLMATLTKPKLLLLDE 174

                ....*.
gi 15830287 467 PTNDLD 472
Cdd:COG1101 175 HTAALD 180
ABCG_PDR_domain2 cd03232
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...
319-472 9.00e-11

Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213199 [Multi-domain]  Cd Length: 192  Bit Score: 61.49  E-value: 9.00e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 319 VFEMEDVCYQVDG----KQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMlgqlqadSGRIHVGTklevayfdqhrael 394
Cdd:cd03232   3 VLTWKNLNYTVPVkggkRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVL-------AGRKTAGV-------------- 61
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 395 dpdktvmdnlAEGkqEVMVNGKP-----RHVLGYLQDFLFHPK--------RAMTPVRALSGGERNRLLLA-RLFLKPSn 460
Cdd:cd03232  62 ----------ITG--EILINGRPldknfQRSTGYVEQQDVHSPnltvrealRFSALLRGLSVEQRKRLTIGvELAAKPS- 128
                       170
                ....*....|..
gi 15830287 461 LLILDEPTNDLD 472
Cdd:cd03232 129 ILFLDEPTSGLD 140
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
138-232 9.83e-11

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


Pssm-ID: 443319 [Multi-domain]  Cd Length: 358  Bit Score: 63.58  E-value: 9.83e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 138 RINEVLAQLGLDPnvaL-----SSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDI----ETIDWLEGFLKTFNGTIIF 208
Cdd:COG4148 113 SFDEVVELLGIGH---LldrrpATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLarkaEILPYLERLRDELDIPILY 189
                        90       100
                ....*....|....*....|....
gi 15830287 209 ISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:COG4148 190 VSHSLDEVARLADHVVLLEQGRVV 213
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
344-503 1.01e-10

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 60.08  E-value: 1.01e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287    344 RGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVgtklevayfdqhraeLDPDKTVMDNLAEGKQEVMVNGKprhvlgy 423
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY---------------IDGEDILEEVLDQLLLIIVGGKK------- 58
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287    424 lqdflfhpkramtpvRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELIDSYQGTVLLVSHDRQFVDNT 503
Cdd:smart00382  59 ---------------ASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLTVILTT 123
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
321-495 1.02e-10

ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.


Pssm-ID: 213184 [Multi-domain]  Cd Length: 200  Bit Score: 61.39  E-value: 1.02e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 321 EMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGqlqadsgriHVG---TKLEVAYFDQHRAELDPD 397
Cdd:cd03217   2 EIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG---------HPKyevTEGEILFKGEDITDLPPE 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 398 KTVMDNLAEGKQEvmvngkPRHVLGY-LQDFLfhpkRAMTpvRALSGGERNRL-LLARLFLKPSnLLILDEPTNDLDVET 475
Cdd:cd03217  73 ERARLGIFLAFQY------PPEIPGVkNADFL----RYVN--EGFSGGEKKRNeILQLLLLEPD-LAILDEPDSGLDIDA 139
                       170       180
                ....*....|....*....|...
gi 15830287 476 LELLEELIDSYQG---TVLLVSH 495
Cdd:cd03217 140 LRLVAEVINKLREegkSVLIITH 162
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
337-495 1.13e-10

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: 61.74  E-value: 1.13e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 337 DFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVG----TKLEVA------YFDQHraELDPDKTVMDNLAE 406
Cdd:cd03298  16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINgvdvTAAPPAdrpvsmLFQEN--NLFAHLTVEQNVGL 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 407 GKQ-EVMVNGKPRH-VLGYLQDFLFHPKRAMTPvRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELID 484
Cdd:cd03298  94 GLSpGLKLTAEDRQaIEVALARVGLAGLEKRLP-GELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVL 172
                       170
                ....*....|....*
gi 15830287 485 SY----QGTVLLVSH 495
Cdd:cd03298 173 DLhaetKMTVLMVTH 187
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
332-537 1.17e-10

Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 64.74  E-value: 1.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   332 KQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVG----TKLEVAYFDQHRAELDPD-----KTVMD 402
Cdd:TIGR00958 494 VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDgvplVQYDHHYLHRQVALVGQEpvlfsGSVRE 573
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   403 NLAEG-----KQEVMVNGKPRHVLGYLQDFlfhPKRAMTPV----RALSGGERNRLLLARLFLKPSNLLILDEPTNDLDV 473
Cdd:TIGR00958 574 NIAYGltdtpDEEIMAAAKAANAHDFIMEF---PNGYDTEVgekgSQLSGGQKQRIAIARALVRKPRVLILDEATSALDA 650
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15830287   474 ETLELLEELIDSYQGTVLLVSHDRQFVDNtVTECwIFEGGGKIGRyvGGYHDA-RGQQEQYVALK 537
Cdd:TIGR00958 651 ECEQLLQESRSRASRTVLLIAHRLSTVER-ADQI-LVLKKGSVVE--MGTHKQlMEDQGCYKHLV 711
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
331-496 1.28e-10

ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 443660 [Multi-domain]  Cd Length: 563  Bit Score: 64.38  E-value: 1.28e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 331 GKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI-----------------HVGtklevaYFDQH--- 390
Cdd:COG4618 344 KRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVrldgadlsqwdreelgrHIG------YLPQDvel 417
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 391 ----------R-AELDPDKTVMDNLAEGKQEvMVNGKPrhvLGYlqDflfhpkramTPV----RALSGGERNRLLLAR-L 454
Cdd:COG4618 418 fdgtiaeniaRfGDADPEKVVAAAKLAGVHE-MILRLP---DGY--D---------TRIgeggARLSGGQRQRIGLARaL 482
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 15830287 455 FLKPSnLLILDEPTNDLDVETLELLEELIDSY---QGTVLLVSHD 496
Cdd:COG4618 483 YGDPR-LVVLDEPNSNLDDEGEAALAAAIRALkarGATVVVITHR 526
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
11-233 1.37e-10

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 62.34  E-value: 1.37e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   11 LSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRI-IYEQDLI----------VARLQQDPPrNV 79
Cdd:PRK11231  10 VGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVfLGDKPISmlssrqlarrLALLPQHHL-TP 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   80 EG-SVYDFVAEGieeQAEYLKRYhdiSRLVMNDpseKNLNELAKVQEQLDHhnlwqLENRinevlaqlgldpnvALSSLS 158
Cdd:PRK11231  89 EGiTVRELVAYG---RSPWLSLW---GRLSAED---NARVNQAMEQTRINH-----LADR--------------RLTDLS 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  159 GGWLRKAALGRALVSNPRVLLLDEPTNHLDI----ETIDwLEGFLKTFNGTIIFISHDrsfiRNMATRIVD----LDRGK 230
Cdd:PRK11231 141 GGQRQRAFLAMVLAQDTPVVLLDEPTTYLDInhqvELMR-LMRELNTQGKTVVTVLHD----LNQASRYCDhlvvLANGH 215

                 ...
gi 15830287  231 LVT 233
Cdd:PRK11231 216 VMA 218
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
14-236 1.38e-10

White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.


Pssm-ID: 213201 [Multi-domain]  Cd Length: 226  Bit Score: 61.52  E-value: 1.38e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  14 SDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMK-ILNREQGLD--DGRIIY-EQDL-------IVARLQQDpprnvegs 82
Cdd:cd03234  18 KYARILNDVSLHVESGQVMAILGSSGSGKTTLLDaISGRVEGGGttSGQILFnGQPRkpdqfqkCVAYVRQD-------- 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  83 vyDFVAEGIEeQAEYLkRYHDISRLvmndPSEKNLNELAKVQEQldhhnlwqlenrinEVLAQLGLDP--NVALSSLSGG 160
Cdd:cd03234  90 --DILLPGLT-VRETL-TYTAILRL----PRKSSDAIRKKRVED--------------VLLRDLALTRigGNLVKGISGG 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 161 WLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTF---NGTIIFISHD-RSFIRNMATRIVDLDRGKLVtYPG 236
Cdd:cd03234 148 ERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLarrNRIVILTIHQpRSDLFRLFDRILLLSSGEIV-YSG 226
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
330-495 1.54e-10

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: 60.97  E-value: 1.54e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 330 DGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI---------HVGTKLEVAYFDQHRAELDPDKTV 400
Cdd:cd03231  11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVllnggpldfQRDSIARGLLYLGHAPGIKTTLSV 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 401 MDNL----AEGKQEVMVNGKPRHVLGYLQDflfhpkramTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETL 476
Cdd:cd03231  91 LENLrfwhADHSDEQVEEALARVGLNGFED---------RPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGV 161
                       170       180
                ....*....|....*....|..
gi 15830287 477 ELLEELIDSYQ---GTVLLVSH 495
Cdd:cd03231 162 ARFAEAMAGHCargGMVVLTTH 183
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
11-257 1.76e-10

SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 63.97  E-value: 1.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   11 LSFS---DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLI-----------VARLQQDPP 76
Cdd:PRK10790 346 VSFAyrdDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLsslshsvlrqgVAMVQQDPV 425
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   77 RnVEGSVYDFVAEGieeqaeylkryHDISRLVMNDPSEK-NLNELAKvqeqldhhnlwQLENRINEVLAQLGldpnvalS 155
Cdd:PRK10790 426 V-LADTFLANVTLG-----------RDISEEQVWQALETvQLAELAR-----------SLPDGLYTPLGEQG-------N 475
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  156 SLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTF--NGTIIFISHDRSFIRNmATRIVDLDRGKLVT 233
Cdd:PRK10790 476 NLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVreHTTLVVIAHRLSTIVE-ADTILVLHRGQAVE 554
                        250       260
                 ....*....|....*....|....
gi 15830287  234 YpGNYDQYLLEKEEALRVEELQNA 257
Cdd:PRK10790 555 Q-GTHQQLLAAQGRYWQMYQLQLA 577
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
30-232 1.85e-10

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 63.57  E-value: 1.85e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   30 ERVCLVGRNGAGKST----LMKILNREQGLD-DGRIIYEQDlivaRLQQDPPRnvegsvydfvaegieeqaeylkryHDI 104
Cdd:PRK15134 313 ETLGLVGESGSGKSTtglaLLRLINSQGEIWfDGQPLHNLN----RRQLLPVR------------------------HRI 364
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  105 sRLVMNDP-SEKN--LNELAKVQEQLDHH----NLWQLENRINEVLAQLGLDPNVAL---SSLSGGWLRKAALGRALVSN 174
Cdd:PRK15134 365 -QVVFQDPnSSLNprLNVLQIIEEGLRVHqptlSAAQREQQVIAVMEEVGLDPETRHrypAEFSGGQRQRIAIARALILK 443
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15830287  175 PRVLLLDEPTNHLD----IETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:PRK15134 444 PSLIILDEPTSSLDktvqAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVV 505
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
15-232 2.04e-10

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 61.95  E-value: 2.04e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   15 DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILN----REQGLD--DGRIIYEQDLIVARLQ-----QDPPRNVEGS- 82
Cdd:PRK13635  19 ATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNglllPEAGTItvGGMVLSEETVWDVRRQvgmvfQNPDNQFVGAt 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   83 VYDFVAEGIEEQAeylkryhdISRLVMndpseknlneLAKVQEQLDHHNLWQLENRinevlaqlglDPnvalSSLSGGWL 162
Cdd:PRK13635  99 VQDDVAFGLENIG--------VPREEM----------VERVDQALRQVGMEDFLNR----------EP----HRLSGGQK 146
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15830287  163 RKAALGRALVSNPRVLLLDEPTNHLD----IETIDWLEGFLKTFNGTIIFISHDRSFIRNmATRIVDLDRGKLV 232
Cdd:PRK13635 147 QRVAIAGVLALQPDIIILDEATSMLDprgrREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEIL 219
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
318-472 2.19e-10

ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.


Pssm-ID: 213219 [Multi-domain]  Cd Length: 237  Bit Score: 61.35  E-value: 2.19e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 318 IVFEMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV-GTKLEVAYFDQHRAELDP 396
Cdd:cd03252   1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVdGHDLALADPAWLRRQVGV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 397 --------DKTVMDNLAEGKQevmvnGKPRHVLGYL------QDFLFH-PKRAMTPV----RALSGGERNRLLLARLFLK 457
Cdd:cd03252  81 vlqenvlfNRSIRDNIALADP-----GMSMERVIEAaklagaHDFISElPEGYDTIVgeqgAGLSGGQRQRIAIARALIH 155
                       170
                ....*....|....*
gi 15830287 458 PSNLLILDEPTNDLD 472
Cdd:cd03252 156 NPRILIFDEATSALD 170
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
19-237 2.65e-10

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 61.68  E-value: 2.65e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRI-----------IYEQDLIVARLQQDPPRNV-EGSVYDF 86
Cdd:PRK13647  21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVkvmgrevnaenEKWVRSKVGLVFQDPDDQVfSSTVWDD 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   87 VAEGIEEQaeylkryhdisRLvmnDPSEKNlnelAKVQEQLDHHNLWQLENRinevlaqlgldpnvALSSLSGGWLRKAA 166
Cdd:PRK13647 101 VAFGPVNM-----------GL---DKDEVE----RRVEEALKAVRMWDFRDK--------------PPYHLSYGQKKRVA 148
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15830287  167 LGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFNG---TIIFISHDRSFIRNMATRIVDLDRGKLVTYPGN 237
Cdd:PRK13647 149 IAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNqgkTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDK 222
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
349-467 2.83e-10

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


Pssm-ID: 443319 [Multi-domain]  Cd Length: 358  Bit Score: 62.43  E-value: 2.83e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 349 ALIGPNGCGKTTLLKLMLGQLQADSGRIHVGtklEVAYFDQ--------HR---------AELDPDKTVMDNLAEG-KQE 410
Cdd:COG4148  29 ALFGPSGSGKTTLLRAIAGLERPDSGRIRLG---GEVLQDSargiflppHRrrigyvfqeARLFPHLSVRGNLLYGrKRA 105
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15830287 411 VMVNGKPRH-----VLGyLQDFLfhpKRamtPVRALSGGERNRLLLAR-LFLKPSnLLILDEP 467
Cdd:COG4148 106 PRAERRISFdevveLLG-IGHLL---DR---RPATLSGGERQRVAIGRaLLSSPR-LLLMDEP 160
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
323-472 3.02e-10

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 61.06  E-value: 3.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  323 EDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI------------HVGTKLEVAYFDQh 390
Cdd:PRK10895   7 KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIiiddedisllplHARARRGIGYLPQ- 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  391 RAELDPDKTVMDNLA---EGKQEVMVNGKPRHVLGYLQDF-LFHPKRAMTpvRALSGGERNRLLLARLFLKPSNLLILDE 466
Cdd:PRK10895  86 EASIFRRLSVYDNLMavlQIRDDLSAEQREDRANELMEEFhIEHLRDSMG--QSLSGGERRRVEIARALAANPKFILLDE 163

                 ....*.
gi 15830287  467 PTNDLD 472
Cdd:PRK10895 164 PFAGVD 169
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
155-234 3.20e-10

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 62.20  E-value: 3.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  155 SSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDI----ETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGK 230
Cdd:PRK11144 127 GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLprkrELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGK 206

                 ....
gi 15830287  231 LVTY 234
Cdd:PRK11144 207 VKAF 210
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
317-468 3.59e-10

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 62.73  E-value: 3.59e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 317 KIVFEMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKlEVAYFDQHRA---- 392
Cdd:COG1129   2 EPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGE-PVRFRSPRDAqaag 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 393 ------ELD--PDKTVMDNLAEGKQevmvngkPRHvlgylqdFLFHPKRAM------------------TPVRALSGGER 446
Cdd:COG1129  81 iaiihqELNlvPNLSVAENIFLGRE-------PRR-------GGLIDWRAMrrrarellarlgldidpdTPVGDLSVAQQ 146
                       170       180
                ....*....|....*....|..
gi 15830287 447 NRLLLARLFLKPSNLLILDEPT 468
Cdd:COG1129 147 QLVEIARALSRDARVLILDEPT 168
LolD_lipo_ex TIGR02211
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ...
319-499 4.10e-10

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: 60.06  E-value: 4.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   319 VFEMEDVC--YQvDGK---QLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKLEVAYFDQHRAE 393
Cdd:TIGR02211   1 LLKCENLGkrYQ-EGKldtRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   394 LD--------------PDKTVMDNLAE----GKQEVMvNGKPRHVLGYLQDFLFHpkRAMTPVRALSGGERNRLLLARLF 455
Cdd:TIGR02211  80 LRnkklgfiyqfhhllPDFTALENVAMplliGKKSVK-EAKERAYEMLEKVGLEH--RINHRPSELSGGERQRVAIARAL 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 15830287   456 LKPSNLLILDEPTNDLDVETLELLEELI---DSYQGT-VLLVSHDRQF 499
Cdd:TIGR02211 157 VNQPSLVLADEPTGNLDNNNAKIIFDLMlelNRELNTsFLVVTHDLEL 204
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
319-472 4.49e-10

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: 60.14  E-value: 4.49e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 319 VFEMEDVCYQVDG--KQLV--KDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV-GTKL------EVAYF 387
Cdd:COG4181   8 IIELRGLTKTVGTgaGELTilKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLaGQDLfaldedARARL 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 388 dqhRAE----------LDPDKTVMDNlaegkqeVMV----NGKP------RHVLGY--LQDFLFH-PKRamtpvraLSGG 444
Cdd:COG4181  88 ---RARhvgfvfqsfqLLPTLTALEN-------VMLplelAGRRdararaRALLERvgLGHRLDHyPAQ-------LSGG 150
                       170       180
                ....*....|....*....|....*...
gi 15830287 445 ERNRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:COG4181 151 EQQRVALARAFATEPAILFADEPTGNLD 178
cbiO PRK13645
energy-coupling factor transporter ATPase;
19-233 7.33e-10

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 60.41  E-value: 7.33e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLIVARLQQ-----DPPRNVeGSVYDFvaegiee 93
Cdd:PRK13645  27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKikevkRLRKEI-GLVFQF------- 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   94 qAEYLKRYHDISRLVMNDPSekNLNElakvqeqldhhNLWQLENRINEVLAQLGLDPNVALSS---LSGGWLRKAALGRA 170
Cdd:PRK13645  99 -PEYQLFQETIEKDIAFGPV--NLGE-----------NKQEAYKKVPELLKLVQLPEDYVKRSpfeLSGGQKRRVALAGI 164
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15830287  171 LVSNPRVLLLDEPTNHLDI----ETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKLVT 233
Cdd:PRK13645 165 IAMDGNTLVLDEPTGGLDPkgeeDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVIS 231
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
333-472 8.59e-10

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 60.87  E-value: 8.59e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  333 QLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTK---------LEVAYFDQHRAeLDPDKTVMDN 403
Cdd:PRK10851  16 QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTdvsrlhardRKVGFVFQHYA-LFRHMTVFDN 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  404 LAEG---------------KQEV-----MVNgkprhvLGYLQDflFHPKRamtpvraLSGGERNRLLLARLFLKPSNLLI 463
Cdd:PRK10851  95 IAFGltvlprrerpnaaaiKAKVtqlleMVQ------LAHLAD--RYPAQ-------LSGGQKQRVALARALAVEPQILL 159

                 ....*....
gi 15830287  464 LDEPTNDLD 472
Cdd:PRK10851 160 LDEPFGALD 168
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
318-472 1.19e-09

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


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 58.82  E-value: 1.19e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 318 IVFEMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQL--QADSGRIHVGTKlevayfdqhraELD 395
Cdd:COG2401  29 IVLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDN-----------QFG 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 396 PDKTVMDNLAEgkqevmvNGKPRHVLGYLQD------FLFhpkraMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTN 469
Cdd:COG2401  98 REASLIDAIGR-------KGDFKDAVELLNAvglsdaVLW-----LRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCS 165

                ...
gi 15830287 470 DLD 472
Cdd:COG2401 166 HLD 168
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
18-231 1.35e-09

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 58.67  E-value: 1.35e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   18 LLDNAELHIEDNERVCLVGRNGAGKSTLMKILNreqGLD---DGRIIYE-QDL-IVARLQQDPPRNVE-GSVYDFvaegi 91
Cdd:PRK11629  24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLG---GLDtptSGDVIFNgQPMsKLSSAAKAELRNQKlGFIYQF----- 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   92 eeqaeylkrYHDISrlvmndpsekNLNELAKVQEQL--DHHNLWQLENRINEVLAQLGLD--PNVALSSLSGGWLRKAAL 167
Cdd:PRK11629  96 ---------HHLLP----------DFTALENVAMPLliGKKKPAEINSRALEMLAAVGLEhrANHRPSELSGGERQRVAI 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15830287  168 GRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFN---GT-IIFISHDRSFIRNMaTRIVDLDRGKL 231
Cdd:PRK11629 157 ARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNrlqGTaFLVVTHDLQLAKRM-SRQLEMRDGRL 223
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
329-473 1.44e-09

ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 443658 [Multi-domain]  Cd Length: 329  Bit Score: 59.75  E-value: 1.44e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 329 VDGkqlVkDFSaqVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVG----TKLEVAYFDQHR-----------AE 393
Cdd:COG4608  34 VDG---V-SFD--IRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDgqdiTGLSGRELRPLRrrmqmvfqdpyAS 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 394 LDPDKTVMDNLAEGkqeVMVNGkprhvlgylqdfLFHPKRAMTPVRAL------------------SGGERNRLLLAR-L 454
Cdd:COG4608 108 LNPRMTVGDIIAEP---LRIHG------------LASKAERRERVAELlelvglrpehadryphefSGGQRQRIGIARaL 172
                       170
                ....*....|....*....
gi 15830287 455 FLKPSnLLILDEPTNDLDV 473
Cdd:COG4608 173 ALNPK-LIVCDEPVSALDV 190
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
26-232 1.48e-09

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 59.65  E-value: 1.48e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   26 IEDNERVCLVGRNGAGKSTLMKILNreqGL---DDGRIIYEQDLIVARLQQD---PPRNVEGSVYDFV-AEGIEEQAEyl 98
Cdd:PRK13634  30 IPSGSYVAIIGHTGSGKSTLLQHLN---GLlqpTSGTVTIGERVITAGKKNKklkPLRKKVGIVFQFPeHQLFEETVE-- 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   99 kryHDISRLVMN-DPSEKNLNELAKvqeqldhhnlwqlenrinEVLAQLGLDPNVALSS---LSGGWLRKAALGRALVSN 174
Cdd:PRK13634 105 ---KDICFGPMNfGVSEEDAKQKAR------------------EMIELVGLPEELLARSpfeLSGGQMRRVAIAGVLAME 163
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15830287  175 PRVLLLDEPTNHLD----IETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:PRK13634 164 PEVLVLDEPTAGLDpkgrKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVF 225
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
321-472 1.69e-09

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: 60.59  E-value: 1.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   321 EMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLG--QLQADSGRI--HVG----------------- 379
Cdd:TIGR03269   2 EVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIiyHVAlcekcgyverpskvgep 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   380 --------TKLEVAYFD-----------------QHRAELDPDKTVMDNLAEGKQEVMVNGKP---RHVLGYLQDFLFHp 431
Cdd:TIGR03269  82 cpvcggtlEPEEVDFWNlsdklrrrirkriaimlQRTFALYGDDTVLDNVLEALEEIGYEGKEavgRAVDLIEMVQLSH- 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 15830287   432 kRAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:TIGR03269 161 -RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLD 200
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
333-501 1.73e-09

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: 58.25  E-value: 1.73e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 333 QLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKLEVAYfdQHR--------AELDP---DKTVM 401
Cdd:cd03248  28 LVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQY--EHKylhskvslVGQEPvlfARSLQ 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 402 DNLAEGKQ-----EVMVNGKPRHVLGYLQDFlfhPKRAMTPV----RALSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:cd03248 106 DNIAYGLQscsfeCVKEAAQKAHAHSFISEL---ASGYDTEVgekgSQLSGGQKQRVAIARALIRNPQVLILDEATSALD 182
                       170       180       190
                ....*....|....*....|....*....|...
gi 15830287 473 VETLELLEELIdsYQG----TVLLVSHDRQFVD 501
Cdd:cd03248 183 AESEQQVQQAL--YDWperrTVLVIAHRLSTVE 213
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
341-631 1.75e-09

multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]


Pssm-ID: 188098 [Multi-domain]  Cd Length: 1522  Bit Score: 61.11  E-value: 1.75e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287    341 QVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVgtKLEVAYFDQhRAELDPDkTVMDNLAEGKQevMVNGKPRHV 420
Cdd:TIGR00957  660 SIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHM--KGSVAYVPQ-QAWIQND-SLRENILFGKA--LNEKYYQQV 733
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287    421 L---GYLQDFLFHPKRAMTPVRA----LSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELIDSYQG----- 488
Cdd:TIGR00957  734 LeacALLPDLEILPSGDRTEIGEkgvnLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIGPEGvlknk 813
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287    489 TVLLVSHDRQFVDNtvTECWIFEGGGKIGRyVGGYHD---------------ARGQQEQYVALKQPAVKKNEEPAAPKAE 553
Cdd:TIGR00957  814 TRILVTHGISYLPQ--VDVIIVMSGGKISE-MGSYQEllqrdgafaeflrtyAPDEQQGHLEDSWTALVSGEGKEAKLIE 890
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287    554 TVKRSSSKLSYKLQRELEQLPQLLEDLEAKLEAL-QTQVADASffsqphEQTQKVL-ADMAAAEQELEQAFerWEYLEAL 631
Cdd:TIGR00957  891 NGMLVTDVVGKQLQRQLSASSSDSGDQSRHHGSSaELQKAEAK------EETWKLMeADKAQTGQVELSVY--WDYMKAI 962
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
11-240 1.81e-09

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 60.63  E-value: 1.81e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   11 LSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILnreqgLddGRIIYEQDLIV-----------------ARLQQ 73
Cdd:PRK11174 358 LSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNAL-----L--GFLPYQGSLKIngielreldpeswrkhlSWVGQ 430
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   74 DPpRNVEGSVYDFVAEGieeqaeylkrYHDISrlvmndpseknlnelakvQEQLDHhnlwQLEN-RINEVLAQL--GLDP 150
Cdd:PRK11174 431 NP-QLPHGTLRDNVLLG----------NPDAS------------------DEQLQQ----ALENaWVSEFLPLLpqGLDT 477
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  151 NVALSS--LSGGWLRKAALGRALVSNPRVLLLDEPTNHLDI---ETIdwLEGFLKTFNG-TIIFISHDRSFIRNMATrIV 224
Cdd:PRK11174 478 PIGDQAagLSVGQAQRLALARALLQPCQLLLLDEPTASLDAhseQLV--MQALNAASRRqTTLMVTHQLEDLAQWDQ-IW 554
                        250
                 ....*....|....*.
gi 15830287  225 DLDRGKLVTyPGNYDQ 240
Cdd:PRK11174 555 VMQDGQIVQ-QGDYAE 569
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
26-227 1.88e-09

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


Pssm-ID: 213204 [Multi-domain]  Cd Length: 246  Bit Score: 58.57  E-value: 1.88e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  26 IEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLIVARLQQDPPRNvEGSVYDFVaegieeqaeylkryHDIS 105
Cdd:cd03237  22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIKADY-EGTVRDLL--------------SSIT 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 106 RLVMNDPSEKNlnELAK-VQ-EQLdhhnlwqLENRINEvlaqlgldpnvalssLSGGWLRKAALGRALVSNPRVLLLDEP 183
Cdd:cd03237  87 KDFYTHPYFKT--EIAKpLQiEQI-------LDREVPE---------------LSGGELQRVAIAACLSKDADIYLLDEP 142
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 15830287 184 TNHLDIETIDWLEGFLKTF----NGTIIFISHDRSFIRNMATRIVDLD 227
Cdd:cd03237 143 SAYLDVEQRLMASKVIRRFaennEKTAFVVEHDIIMIDYLADRLIVFE 190
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
14-227 2.04e-09

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: 56.78  E-value: 2.04e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  14 SDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNreqGL---DDGRIIYeqdlivarlqqdPPRNvegSVYdFVAeg 90
Cdd:cd03223  12 DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALA---GLwpwGSGRIGM------------PEGE---DLL-FLP-- 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  91 ieeQAEYLKRyhdisrlvmndpseKNLnelakvQEQLDHhnLWQLEnrinevlaqlgldpnvalssLSGGWLRKAALGRA 170
Cdd:cd03223  71 ---QRPYLPL--------------GTL------REQLIY--PWDDV--------------------LSGGEQQRLAFARL 105
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15830287 171 LVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFNGTIIFISHdRSFIRNMATRIVDLD 227
Cdd:cd03223 106 LLHKPKFVFLDEATSALDEESEDRLYQLLKELGITVISVGH-RPSLWKFHDRVLDLD 161
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
13-232 2.11e-09

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 58.70  E-value: 2.11e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   13 FSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDD-----------GRIIYEQDL--IVARLQ-----QD 74
Cdd:PRK14267  14 YGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearvegevrlfGRNIYSPDVdpIEVRREvgmvfQY 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   75 PPRNVEGSVYDFVAEGIEeqaeylkryhdisrlvmndpseknLNELAKVQEQLDHHNLWQLENRI--NEVLAQLGLDPnv 152
Cdd:PRK14267  94 PNPFPHLTIYDNVAIGVK------------------------LNGLVKSKKELDERVEWALKKAAlwDEVKDRLNDYP-- 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  153 alSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLD---IETIDWLEGFLKTfNGTIIFISHDRSFIRNMATRIVDLDRG 229
Cdd:PRK14267 148 --SNLSGGQRQRLVIARALAMKPKILLMDEPTANIDpvgTAKIEELLFELKK-EYTIVLVTHSPAQAARVSDYVAFLYLG 224

                 ...
gi 15830287  230 KLV 232
Cdd:PRK14267 225 KLI 227
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
330-472 3.03e-09

First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213200 [Multi-domain]  Cd Length: 202  Bit Score: 57.27  E-value: 3.03e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 330 DGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQAD---SGRIHVGTKLEVAYFDQHRAELdpdktvmdnlae 406
Cdd:cd03233  18 SKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGEI------------ 85
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15830287 407 gkqeVMVNGKPRHV--LGYLQDFLFHPK-RAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:cd03233  86 ----IYVSEEDVHFptLTVRETLDFALRcKGNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
324-472 3.50e-09

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 58.89  E-value: 3.50e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  324 DVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKL---------EVAYFDQHRAeL 394
Cdd:PRK11000   8 NVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRmndvppaerGVGMVFQSYA-L 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  395 DPDKTVMDNLAEG-------KQEvmVNGKPRHVLGYLQdfLFH-----PKramtpvrALSGGERNRLLLARLFLKPSNLL 462
Cdd:PRK11000  87 YPHLSVAENMSFGlklagakKEE--INQRVNQVAEVLQ--LAHlldrkPK-------ALSGGQRQRVAIGRTLVAEPSVF 155
                        170
                 ....*....|
gi 15830287  463 ILDEPTNDLD 472
Cdd:PRK11000 156 LLDEPLSNLD 165
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
21-232 3.50e-09

ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213261 [Multi-domain]  Cd Length: 269  Bit Score: 58.04  E-value: 3.50e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  21 NAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYE-QDliVARLQQDPPRNVEG----------------SV 83
Cdd:cd03294  42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDgQD--IAAMSRKELRELRRkkismvfqsfallphrTV 119
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  84 YDFVAEGIEeqaeylkryhdisrlvmndpseknlneLAKVQEQldhhnlwQLENRINEVLAQLGLDP--NVALSSLSGGW 161
Cdd:cd03294 120 LENVAFGLE---------------------------VQGVPRA-------EREERAAEALELVGLEGweHKYPDELSGGM 165
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15830287 162 LRKAALGRALVSNPRVLLLDEPTNHLD----IETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:cd03294 166 QQRVGLARALAVDPDILLMDEAFSALDplirREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLV 240
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
335-500 3.90e-09

ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.


Pssm-ID: 213257 [Multi-domain]  Cd Length: 218  Bit Score: 57.34  E-value: 3.90e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 335 VKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKLE---------------VAYFDQHRAELDpdKT 399
Cdd:cd03290  17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNEsepsfeatrsrnrysVAYAAQKPWLLN--AT 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 400 VMDNLAEGKQEVMVNGKPRHVLGYLQ---DFLFHPKRAMTPVRA--LSGGERNRLLLARLFLKPSNLLILDEPTNDLDVE 474
Cdd:cd03290  95 VEENITFGSPFNKQRYKAVTDACSLQpdiDLLPFGDQTEIGERGinLSGGQRQRICVARALYQNTNIVFLDDPFSALDIH 174
                       170       180       190
                ....*....|....*....|....*....|.
gi 15830287 475 TLELLEEL-----IDSYQGTVLLVSHDRQFV 500
Cdd:cd03290 175 LSDHLMQEgilkfLQDDKRTLVLVTHKLQYL 205
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
17-234 4.22e-09

ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.


Pssm-ID: 213269 [Multi-domain]  Cd Length: 207  Bit Score: 57.04  E-value: 4.22e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  17 PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRI-IYEQDLIVARLQ----------QDPPRnVEGSVyd 85
Cdd:cd03369  22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIeIDGIDISTIPLEdlrssltiipQDPTL-FSGTI-- 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  86 fvaegieeqAEYLKRYhdisrlvmNDPSEKNLNELAKVQEQldhhnlwqlenrinevlaqlGLDpnvalssLSGGWLRKA 165
Cdd:cd03369  99 ---------RSNLDPF--------DEYSDEEIYGALRVSEG--------------------GLN-------LSQGQRQLL 134
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15830287 166 ALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFL-KTFNG-TIIFISHDRSFIRNMAtRIVDLDRGKLVTY 234
Cdd:cd03369 135 CLARALLKRPRVLVLDEATASIDYATDALIQKTIrEEFTNsTILTIAHRLRTIIDYD-KILVMDAGEVKEY 204
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
330-496 5.02e-09

ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213262 [Multi-domain]  Cd Length: 242  Bit Score: 57.31  E-value: 5.02e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 330 DGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKlEVAYFDQHR-----------AELDPDK 398
Cdd:cd03295  12 GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGE-DIREQDPVElrrkigyviqqIGLFPHM 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 399 TVMDNLAEGKQevmVNGKPRH-----VLGYLQDFLFHPK--RAMTPvRALSGGERNRLLLARLFLKPSNLLILDEPTNDL 471
Cdd:cd03295  91 TVEENIALVPK---LLKWPKEkirerADELLALVGLDPAefADRYP-HELSGGQQQRVGVARALAADPPLLLMDEPFGAL 166
                       170       180
                ....*....|....*....|....*....
gi 15830287 472 DVETLELLEELIDSYQ----GTVLLVSHD 496
Cdd:cd03295 167 DPITRDQLQEEFKRLQqelgKTIVFVTHD 195
cbiO PRK13644
energy-coupling factor transporter ATPase;
3-232 5.66e-09

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 57.69  E-value: 5.66e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287    3 LISMHGAWLSFSDA-PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILN---REQ-------GLDDGRIIYEQDL--IVA 69
Cdd:PRK13644   1 MIRLENVSYSYPDGtPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNgllRPQkgkvlvsGIDTGDFSKLQGIrkLVG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   70 RLQQDPPRNvegsvydFVAEGIEEQAEYlkryhdisrlvmnDPSEKNLNELakvqeqldhhnlwQLENRINEVLAQLGLD 149
Cdd:PRK13644  81 IVFQNPETQ-------FVGRTVEEDLAF-------------GPENLCLPPI-------------EIRKRVDRALAEIGLE 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  150 PNVALS--SLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIET-IDWLEGFLKTFN--GTIIFISHDRSFIRNmATRIV 224
Cdd:PRK13644 128 KYRHRSpkTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSgIAVLERIKKLHEkgKTIVYITHNLEELHD-ADRII 206

                 ....*...
gi 15830287  225 DLDRGKLV 232
Cdd:PRK13644 207 VMDRGKIV 214
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
333-472 5.76e-09

ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.


Pssm-ID: 213216 [Multi-domain]  Cd Length: 238  Bit Score: 57.16  E-value: 5.76e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 333 QLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVG----TKLEVAYFDQHRA--ELDP---DKTVMDN 403
Cdd:cd03249  17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDgvdiRDLNLRWLRSQIGlvSQEPvlfDGTIAEN 96
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15830287 404 LAEGK-----QEVMVNGKprhvLGYLQDFLFH-PKRAMTPVRA----LSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:cd03249  97 IRYGKpdatdEEVEEAAK----KANIHDFIMSlPDGYDTLVGErgsqLSGGQKQRIAIARALLRNPKILLLDEATSALD 171
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
1-184 5.95e-09

high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 56.81  E-value: 5.95e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287    1 MSLISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLIVarlqQDPPRNVE 80
Cdd:PRK11614   3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDIT----DWQTAKIM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   81 GSVYDFVAEGieeqaeylKRYhdISRLVMndpsEKNLNE----LAKVQEQLDHHNLWQLENRINEVLAQLGldpnvalSS 156
Cdd:PRK11614  79 REAVAIVPEG--------RRV--FSRMTV----EENLAMggffAERDQFQERIKWVYELFPRLHERRIQRA-------GT 137
                        170       180
                 ....*....|....*....|....*...
gi 15830287  157 LSGGWLRKAALGRALVSNPRVLLLDEPT 184
Cdd:PRK11614 138 MSGGEQQMLAIGRALMSQPRLLLLDEPS 165
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
30-211 6.00e-09

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


Pssm-ID: 213198 [Multi-domain]  Cd Length: 201  Bit Score: 56.35  E-value: 6.00e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  30 ERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQdlivARLQQDPPRNVEGSVYDFVAEGIE---EQAEYLKRYHDIsr 106
Cdd:cd03231  27 EALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNG----GPLDFQRDSIARGLLYLGHAPGIKttlSVLENLRFWHAD-- 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 107 lvmndpseknlNELAKVQEQLDHHNLWQLENRinevlaqlgldpnvALSSLSGGWLRKAALGRALVSNPRVLLLDEPTNH 186
Cdd:cd03231 101 -----------HSDEQVEEALARVGLNGFEDR--------------PVAQLSAGQQRRVALARLLLSGRPLWILDEPTTA 155
                       170       180
                ....*....|....*....|....*...
gi 15830287 187 LDIETIDWLEGFLKTF---NGTIIFISH 211
Cdd:cd03231 156 LDKAGVARFAEAMAGHcarGGMVVLTTH 183
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
19-232 6.16e-09

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 56.81  E-value: 6.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQdlivarlqqdpprnvegsvydfvaegieeqaeyl 98
Cdd:PRK10908  18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSG---------------------------------- 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   99 kryHDISRLvmndpseKNlNELAKVQEQL-----DHHNLWQ--------------------LENRINEVLAQLGL---DP 150
Cdd:PRK10908  64 ---HDITRL-------KN-REVPFLRRQIgmifqDHHLLMDrtvydnvaipliiagasgddIRRRVSAALDKVGLldkAK 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  151 NVALSsLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFNG---TIIFISHDRSFIRNMATRIVDLD 227
Cdd:PRK10908 133 NFPIQ-LSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRvgvTVLMATHDIGLISRRSYRMLTLS 211

                 ....*
gi 15830287  228 RGKLV 232
Cdd:PRK10908 212 DGHLH 216
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
319-472 6.21e-09

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 57.55  E-value: 6.21e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  319 VFEMEDVCYQV-DGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKlEVAYFDQHRAEL--- 394
Cdd:PRK13636   5 ILKVEELNYNYsDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGK-PIDYSRKGLMKLres 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  395 ------DPDKTVMD------------NLAEGKQEV---MVNGKPRHVLGYLQDflfhpkramTPVRALSGGERNRLLLAR 453
Cdd:PRK13636  84 vgmvfqDPDNQLFSasvyqdvsfgavNLKLPEDEVrkrVDNALKRTGIEHLKD---------KPTHCLSFGQKKRVAIAG 154
                        170
                 ....*....|....*....
gi 15830287  454 LFLKPSNLLILDEPTNDLD 472
Cdd:PRK13636 155 VLVMEPKVLVLDEPTAGLD 173
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
17-473 7.32e-09

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 58.71  E-value: 7.32e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   17 PLLDNAELHIEDNERVCLVGRNGAGKS----TLMKILnrEQGldDGRIIYEQDLIVARLQQdpprnvegsvydfVAEGIE 92
Cdd:PRK10261  30 AAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLL--EQA--GGLVQCDKMLLRRRSRQ-------------VIELSE 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   93 EQAEYLKRYH--DISrLVMNDPSeKNLNELAKVQEQLD-----HHNLWQLEN-----------RINEVLAQLGLDPNval 154
Cdd:PRK10261  93 QSAAQMRHVRgaDMA-MIFQEPM-TSLNPVFTVGEQIAesirlHQGASREEAmveakrmldqvRIPEAQTILSRYPH--- 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  155 sSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDI----ETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGK 230
Cdd:PRK10261 168 -QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVtiqaQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGE 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  231 LV------------TYPgnYDQYLLEKeeALRVEELQNAEFDRKLAqeevWIRQGIKARRTrnegrvralkamrRERGER 298
Cdd:PRK10261 247 AVetgsveqifhapQHP--YTRALLAA--VPQLGAMKGLDYPRRFP----LISLEHPAKQE-------------PPIEQD 305
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  299 REVMGTAKMQVEE-----ASRSGKIVFEMEDVcyqvdgkQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADS 373
Cdd:PRK10261 306 TVVDGEPILQVRNlvtrfPLRSGLLNRVTREV-------HAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQG 378
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  374 GRIHV---------GTKLEVA------YFDQHRAELDPDKTVMDNLAEG-KQEVMVNGKP--RHVLGYLQDFLFHPKRAM 435
Cdd:PRK10261 379 GEIIFngqridtlsPGKLQALrrdiqfIFQDPYASLDPRQTVGDSIMEPlRVHGLLPGKAaaARVAWLLERVGLLPEHAW 458
                        490       500       510
                 ....*....|....*....|....*....|....*....
gi 15830287  436 TPVRALSGGERNRLLLAR-LFLKPsNLLILDEPTNDLDV 473
Cdd:PRK10261 459 RYPHEFSGGQRQRICIARaLALNP-KVIIADEAVSALDV 496
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
17-183 7.53e-09

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


Pssm-ID: 213185 [Multi-domain]  Cd Length: 232  Bit Score: 56.40  E-value: 7.53e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  17 PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILnreQGL---DDGRIIYEQDLIV-------ARLqqdpprnvegsvydf 86
Cdd:cd03218  14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMI---VGLvkpDSGKILLDGQDITklpmhkrARL--------------- 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  87 vaeGIEeqaeYLKRYHDI-SRLVMndpsEKNLNELAKVQEQLDhhnlWQLENRINEVLAQLGLDP---NVAlSSLSGGWL 162
Cdd:cd03218  76 ---GIG----YLPQEASIfRKLTV----EENILAVLEIRGLSK----KEREEKLEELLEEFHITHlrkSKA-SSLSGGER 139
                       170       180
                ....*....|....*....|.
gi 15830287 163 RKAALGRALVSNPRVLLLDEP 183
Cdd:cd03218 140 RRVEIARALATNPKFLLLDEP 160
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
26-244 7.83e-09

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 56.86  E-value: 7.83e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   26 IEDNERVCLVGRNGAGKSTLmkiLNREQGLDD--GRII-----------YEQDLIVARL--QQDPPRNVEgsVYdfvaeg 90
Cdd:PRK03695  19 VRAGEILHLVGPNGAGKSTL---LARMAGLLPgsGSIQfagqpleawsaAELARHRAYLsqQQTPPFAMP--VF------ 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   91 ieeqaEYLKRYhdisrlvmndpseknlnelakvqeQLDHHNLWQLENRINEVLAQLGLDPNVA--LSSLSGG-W--LRKA 165
Cdd:PRK03695  88 -----QYLTLH------------------------QPDKTRTEAVASALNEVAEALGLDDKLGrsVNQLSGGeWqrVRLA 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  166 A--LGRALVSNP--RVLLLDEPTNHLDIETIDWLEGFLKTF---NGTIIFISHDRSFIRNMATRIVDLDRGKLVTYpGNY 238
Cdd:PRK03695 139 AvvLQVWPDINPagQLLLLDEPMNSLDVAQQAALDRLLSELcqqGIAVVMSSHDLNHTLRHADRVWLLKQGKLLAS-GRR 217

                 ....*.
gi 15830287  239 DQYLLE 244
Cdd:PRK03695 218 DEVLTP 223
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
11-225 9.30e-09

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 56.71  E-value: 9.30e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   11 LSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLD-----DGRIIYEQDLIVAR--------------L 71
Cdd:PRK14239  13 VYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIYSPrtdtvdlrkeigmvF 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   72 QQdpPRNVEGSVYDFVAEGIEeqaeyLKRYHDISRLvmnDpseknlnelAKVQEQLDHHNLWqlenriNEVLAQLGldpN 151
Cdd:PRK14239  93 QQ--PNPFPMSIYENVVYGLR-----LKGIKDKQVL---D---------EAVEKSLKGASIW------DEVKDRLH---D 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  152 VALsSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLD------IEtiDWLEGFLKTFngTIIFISHdrsfirNM--ATRI 223
Cdd:PRK14239 145 SAL-GLSGGQQQRVCIARVLATSPKIILLDEPTSALDpisagkIE--ETLLGLKDDY--TMLLVTR------SMqqASRI 213

                 ..
gi 15830287  224 VD 225
Cdd:PRK14239 214 SD 215
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
12-214 9.81e-09

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 57.42  E-value: 9.81e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   12 SFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILnreQGLD---DGRI-IYEQDLIVARLQQDPPRNVEGSVYDFV 87
Cdd:PRK11432  15 RFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLV---AGLEkptEGQIfIDGEDVTHRSIQQRDICMVFQSYALFP 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   88 AEGIEEQAEYLKRYHDISRlvmndpSEKNlnelAKVQEQLDHHNLWQLENRInevlaqlgldpnvaLSSLSGGWLRKAAL 167
Cdd:PRK11432  92 HMSLGENVGYGLKMLGVPK------EERK----QRVKEALELVDLAGFEDRY--------------VDQISGGQQQRVAL 147
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 15830287  168 GRALVSNPRVLLLDEPTNHLDI-------ETIDWLEgflKTFNGTIIFISHDRS 214
Cdd:PRK11432 148 ARALILKPKVLLFDEPLSNLDAnlrrsmrEKIRELQ---QQFNITSLYVTHDQS 198
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
321-496 9.96e-09

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 56.58  E-value: 9.96e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  321 EMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKlMLGQLQADSGRIHVGTKLEvaYFDQH----RAELD- 395
Cdd:PRK14258   9 KVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLK-CLNRMNELESEVRVEGRVE--FFNQNiyerRVNLNr 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  396 -----------PD---KTVMDNLAEGKQevMVNGKPRHVL----------GYLQDFLFHP--KRAMTpvraLSGGERNRL 449
Cdd:PRK14258  86 lrrqvsmvhpkPNlfpMSVYDNVAYGVK--IVGWRPKLEIddivesalkdADLWDEIKHKihKSALD----LSGGQQQRL 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15830287  450 LLAR-LFLKPsNLLILDEPTNDLDVETLELLEELIDSY----QGTVLLVSHD 496
Cdd:PRK14258 160 CIARaLAVKP-KVLLMDEPCFGLDPIASMKVESLIQSLrlrsELTMVIVSHN 210
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
12-473 1.02e-08

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 58.09  E-value: 1.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   12 SFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYE------------QDLIVARLQQDppRNV 79
Cdd:PRK10762  13 AFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLgkevtfngpkssQEAGIGIIHQE--LNL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   80 EGSVYdfVAEGIEEQAEYLKRYHDISRLVMNDPSEKnlnelakvqeqldhhnlwqlenrineVLAQLGL--DPNVALSSL 157
Cdd:PRK10762  91 IPQLT--IAENIFLGREFVNRFGRIDWKKMYAEADK--------------------------LLARLNLrfSSDKLVGEL 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  158 SGGWLRKAALGRALVSNPRVLLLDEPTNHL-DIETIDWLE--GFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGklvty 234
Cdd:PRK10762 143 SIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTETESLFRviRELKSQGRGIVYISHRLKEIFEICDDVTVFRDG----- 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  235 pgnydQYLLEKE-EALRVEELQNAEFDRKLaqEEVWirqgikARRTRNEGRVRalkamrrergerrevmgtakMQVEEAS 313
Cdd:PRK10762 218 -----QFIAEREvADLTEDSLIEMMVGRKL--EDQY------PRLDKAPGEVR--------------------LKVDNLS 264
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  314 RSGkivfemedvcyqvdgkqlVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV------------GTK 381
Cdd:PRK10762 265 GPG------------------VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLdghevvtrspqdGLA 326
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  382 LEVAYF--DQHRAELDPDKTVMDNLA--------------EGKQEVMVNGkprhvlgylqDF--LFHPKramTPVRA--- 440
Cdd:PRK10762 327 NGIVYIseDRKRDGLVLGMSVKENMSltalryfsraggslKHADEQQAVS----------DFirLFNIK---TPSMEqai 393
                        490       500       510
                 ....*....|....*....|....*....|....*.
gi 15830287  441 --LSGGERNRLLLAR-LFLKPsNLLILDEPTNDLDV 473
Cdd:PRK10762 394 glLSGGNQQKVAIARgLMTRP-KVLILDEPTRGVDV 428
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
20-237 1.03e-08

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 57.41  E-value: 1.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   20 DNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIY-EQDLI-------------VARLQQDP-----PRNVE 80
Cdd:PRK15079  38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWlGKDLLgmkddewravrsdIQMIFQDPlaslnPRMTI 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   81 GSVYdfvaegieeqAEYLKRYHdisrlvmndPseknlnELAKvQEqldhhnlwqLENRINEVLAQLGLDPNVA---LSSL 157
Cdd:PRK15079 118 GEII----------AEPLRTYH---------P------KLSR-QE---------VKDRVKAMMLKVGLLPNLInryPHEF 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  158 SGGWLRKAALGRALVSNPRVLLLDEPTNHLDI----ETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIvdldrgkLVT 233
Cdd:PRK15079 163 SGGQCQRIGIARALILEPKLIICDEPVSALDVsiqaQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRV-------LVM 235

                 ....
gi 15830287  234 YPGN 237
Cdd:PRK15079 236 YLGH 239
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
332-514 1.08e-08

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 56.62  E-value: 1.08e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  332 KQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIH-VGTKLEVAYFDQHRA--------------ELDP 396
Cdd:PRK10419  25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSwRGEPLAKLNRAQRKAfrrdiqmvfqdsisAVNP 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  397 DKTVMDNLAEgkqevmvngkP-RHVLGYLQDFLFHPKRAMtpVRA--------------LSGGERNRLLLARLFLKPSNL 461
Cdd:PRK10419 105 RKTVREIIRE----------PlRHLLSLDKAERLARASEM--LRAvdlddsvldkrppqLSGGQLQRVCLARALAVEPKL 172
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 15830287  462 LILDEPTNDLDVETLELLEELIDSYQ---GTV-LLVSHDRQFVDNTVTECWIFEGGG 514
Cdd:PRK10419 173 LILDEAVSNLDLVLQAGVIRLLKKLQqqfGTAcLFITHDLRLVERFCQRVMVMDNGQ 229
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
19-246 1.08e-08

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 56.78  E-value: 1.08e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYE-QDLIVARLQQDPPRNVEGSVYdfvaEGIEEQAEY 97
Cdd:PRK13636  22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDgKPIDYSRKGLMKLRESVGMVF----QDPDNQLFS 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   98 LKRYHDISRLVMNDPSEKNlnelaKVQEQLDHhnlwqlenrineVLAQLGLDP--NVALSSLSGGWLRKAALGRALVSNP 175
Cdd:PRK13636  98 ASVYQDVSFGAVNLKLPED-----EVRKRVDN------------ALKRTGIEHlkDKPTHCLSFGQKKRVAIAGVLVMEP 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15830287  176 RVLLLDEPTNHLD----IETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKLVtYPGNYDQYLLEKE 246
Cdd:PRK13636 161 KVLVLDEPTAGLDpmgvSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVI-LQGNPKEVFAEKE 234
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
19-234 1.17e-08

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


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 56.24  E-value: 1.17e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNreqGL---DDGRIIyeqdlivarlqqdpprnVEGSV-----------Y 84
Cdd:COG1134  42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIA---GIlepTSGRVE-----------------VNGRVsallelgagfhP 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  85 DF-VAEGIeeqaeYLK-RYHDISRlvmndpseknlnelakvqeqldhhnlWQLENRINEVL--AQLG--LD-PnvaLSSL 157
Cdd:COG1134 102 ELtGRENI-----YLNgRLLGLSR--------------------------KEIDEKFDEIVefAELGdfIDqP---VKTY 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 158 SGGwlRKAALGRALVS--NPRVLLLDEPTNHLDIE----TIDWLEGFLKTfNGTIIFISHDRSFIRNMATRIVDLDRGKL 231
Cdd:COG1134 148 SSG--MRARLAFAVATavDPDILLVDEVLAVGDAAfqkkCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKGRL 224

                ...
gi 15830287 232 VTY 234
Cdd:COG1134 225 VMD 227
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
328-504 1.22e-08

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 57.98  E-value: 1.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  328 QVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIH--VGTKLEVAYFDQHRAEldpDKTVMD--- 402
Cdd:PRK15064  10 QFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSldPNERLGKLRQDQFAFE---EFTVLDtvi 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  403 ----NLAEGKQEV--------MVNGKPRHV-------------------------LGYLQDFLFHPKRAMTPvralsgGE 445
Cdd:PRK15064  87 mghtELWEVKQERdriyalpeMSEEDGMKVadlevkfaemdgytaearagelllgVGIPEEQHYGLMSEVAP------GW 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  446 RNRLLLAR-LFLKPsNLLILDEPTNDLDVETLELLEELIDSYQGTVLLVSHDRQFVdNTV 504
Cdd:PRK15064 161 KLRVLLAQaLFSNP-DILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFL-NSV 218
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
19-239 1.23e-08

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 56.33  E-value: 1.23e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGL-----DDGRIIYEQDLIVARlQQDP-------------PRNVE 80
Cdd:PRK14243  26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLipgfrVEGKVTFHGKNLYAP-DVDPvevrrrigmvfqkPNPFP 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   81 GSVYDFVAEGIEeqaeyLKRYhdisrlvmndpsEKNLNELakVQEQLDHHNLWqleNRINEVLAQLGLdpnvalsSLSGG 160
Cdd:PRK14243 105 KSIYDNIAYGAR-----INGY------------KGDMDEL--VERSLRQAALW---DEVKDKLKQSGL-------SLSGG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  161 WLRKAALGRALVSNPRVLLLDEPTNHLD-IETIDwLEGFLKTFNG--TIIFISHdrsfirNM--ATRIVDL--------- 226
Cdd:PRK14243 156 QQQRLCIARAIAVQPEVILMDEPCSALDpISTLR-IEELMHELKEqyTIIIVTH------NMqqAARVSDMtaffnvelt 228
                        250
                 ....*....|...
gi 15830287  227 DRGKLVTYPGNYD 239
Cdd:PRK14243 229 EGGGRYGYLVEFD 241
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
316-495 1.39e-08

ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.


Pssm-ID: 213269 [Multi-domain]  Cd Length: 207  Bit Score: 55.50  E-value: 1.39e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 316 GKIVFEMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVgtklevayfDQHRAELD 395
Cdd:cd03369   5 GEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEI---------DGIDISTI 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 396 PDKTVMDNLAEGKQE-VMVNGKPRHVLG----YLQDFLFHPKRAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTND 470
Cdd:cd03369  76 PLEDLRSSLTIIPQDpTLFSGTIRSNLDpfdeYSDEEIYGALRVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATAS 155
                       170       180
                ....*....|....*....|....*..
gi 15830287 471 LDVETLELLEELI-DSYQG-TVLLVSH 495
Cdd:cd03369 156 IDYATDALIQKTIrEEFTNsTILTIAH 182
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
310-472 1.49e-08

ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 56.20  E-value: 1.49e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 310 EEASRSGKIVFEMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMlgqlqadsGRIH---VGTKLE--V 384
Cdd:COG1117   2 TAPASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCL--------NRMNdliPGARVEgeI 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 385 AYFDQ--HRAELDPD-----------------KTVMDNLAEGkqeVMVNG-KPRHVLGYL-QDFLfhpKRAM-------- 435
Cdd:COG1117  74 LLDGEdiYDPDVDVVelrrrvgmvfqkpnpfpKSIYDNVAYG---LRLHGiKSKSELDEIvEESL---RKAAlwdevkdr 147
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 15830287 436 --TPVRALSGGERNRLLLAR-LFLKPSNLLiLDEPTNDLD 472
Cdd:COG1117 148 lkKSALGLSGGQQQRLCIARaLAVEPEVLL-MDEPTSALD 186
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
18-231 1.52e-08

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 56.13  E-value: 1.52e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   18 LLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLIvaRLQQDppRNVEGSVYDfvaegiEEQAEY 97
Cdd:PRK10619  20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTI--NLVRD--KDGQLKVAD------KNQLRL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   98 LKryhdiSRLVMndpseknlnelakvqeQLDHHNLWQ----LENRINEVLAQLGLDPNVAL------------------- 154
Cdd:PRK10619  90 LR-----TRLTM----------------VFQHFNLWShmtvLENVMEAPIQVLGLSKQEAReravkylakvgideraqgk 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  155 --SSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTF---NGTIIFISHDRSFIRNMATRIVDLDRG 229
Cdd:PRK10619 149 ypVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLaeeGKTMVVVTHEMGFARHVSSHVIFLHQG 228

                 ..
gi 15830287  230 KL 231
Cdd:PRK10619 229 KI 230
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
19-255 1.55e-08

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 56.63  E-value: 1.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYeqdLIVARLQQDPPRNVEGSVYDFV----------- 87
Cdd:PRK13651  23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEW---IFKDEKNKKKTKEKEKVLEKLViqktrfkkikk 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   88 AEGIEEQ-------AEYLKRYHDISRLVMNDP-----SEKNLNELAKvqeqldhhnlwqlenrinEVLAQLGLDPNVALS 155
Cdd:PRK13651 100 IKEIRRRvgvvfqfAEYQLFEQTIEKDIIFGPvsmgvSKEEAKKRAA------------------KYIELVGLDESYLQR 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  156 S---LSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIE-TIDWLEGF--LKTFNGTIIFISHDRSFIRNMATRIVDLDRG 229
Cdd:PRK13651 162 SpfeLSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQgVKEILEIFdnLNKQGKTIILVTHDLDNVLEWTKRTIFFKDG 241
                        250       260
                 ....*....|....*....|....*.
gi 15830287  230 KLVTYPGNYDqyLLEKEEALRVEELQ 255
Cdd:PRK13651 242 KIIKDGDTYD--ILSDNKFLIENNME 265
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
19-229 1.63e-08

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: 55.55  E-value: 1.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287    19 LDNAELHIEDNERVCLVGRNGAGKSTLmkiLNREQGLD---DGRIIYEQDLIVArlqQDPPRNVEGSVYDFVAegieeqa 95
Cdd:TIGR01184   1 LKGVNLTIQQGEFISLIGHSGCGKSTL---LNLISGLAqptSGGVILEGKQITE---PGPDRMVVFQNYSLLP------- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287    96 eYLKRYHDISrlvmndpseknlneLAkVQEQLDHHNLWQLENRINEVLAQLGLD--PNVALSSLSGGWLRKAALGRALVS 173
Cdd:TIGR01184  68 -WLTVRENIA--------------LA-VDRVLPDLSKSERRAIVEEHIALVGLTeaADKRPGQLSGGMKQRVAIARALSI 131
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   174 NPRVLLLDEPTNHLDIETIDWL-EGFLKTFNG---TIIFISHDRSFIRNMATRIVDLDRG 229
Cdd:TIGR01184 132 RPKVLLLDEPFGALDALTRGNLqEELMQIWEEhrvTVLMVTHDVDEALLLSDRVVMLTNG 191
cbiO PRK13650
energy-coupling factor transporter ATPase;
319-496 1.66e-08

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 56.28  E-value: 1.66e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  319 VFEMEDVCYQVDGKQ---LVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV-GTKLEVAYFDQHRAEL 394
Cdd:PRK13650   4 IIEVKNLTFKYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIdGDLLTEENVWDIRHKI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  395 -----DPDK-----TVMDNLAEGKQ------EVMVNgKPRHVLGY--LQDFlfhpkRAMTPVRaLSGGERNRLLLARLFL 456
Cdd:PRK13650  84 gmvfqNPDNqfvgaTVEDDVAFGLEnkgiphEEMKE-RVNEALELvgMQDF-----KEREPAR-LSGGQKQRVAIAGAVA 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 15830287  457 KPSNLLILDEPTNDLDVETLELLEELI----DSYQGTVLLVSHD 496
Cdd:PRK13650 157 MRPKIIILDEATSMLDPEGRLELIKTIkgirDDYQMTVISITHD 200
BtuD COG4138
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ...
26-232 2.12e-08

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


Pssm-ID: 443313 [Multi-domain]  Cd Length: 248  Bit Score: 55.62  E-value: 2.12e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  26 IEDNERVCLVGRNGAGKSTLmkiLNREQGLDD--GRIIYEQDLI-------VARL------QQDPPRNVegSVYdfvaeg 90
Cdd:COG4138  19 VNAGELIHLIGPNGAGKSTL---LARMAGLLPgqGEILLNGRPLsdwsaaeLARHraylsqQQSPPFAM--PVF------ 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  91 ieeqaEYLKRYhdisrlvmndpseknlnelakvqeQLDHHNLWQLENRINEVLAQLGLDPNVA--LSSLSGG-W--LRKA 165
Cdd:COG4138  88 -----QYLALH------------------------QPAGASSEAVEQLLAQLAEALGLEDKLSrpLTQLSGGeWqrVRLA 138
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15830287 166 A----LGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTF---NGTIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:COG4138 139 AvllqVWPTINPEGQLLLLDEPMNSLDVAQQAALDRLLRELcqqGITVVMSSHDLNHTLRHADRVWLLKQGKLV 212
cbiO PRK13641
energy-coupling factor transporter ATPase;
19-232 2.34e-08

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 55.99  E-value: 2.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLIVARLQQDPPRNVE---GSVYDFVAEGIEEQA 95
Cdd:PRK13641  23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNLKKLRkkvSLVFQFPEAQLFENT 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   96 eylkryhdisrlVMNDPSEKNLNELAKVQEQLDHHNLWqlenrinevLAQLGLDPNVALSS---LSGGWLRKAALGRALV 172
Cdd:PRK13641 103 ------------VLKDVEFGPKNFGFSEDEAKEKALKW---------LKKVGLSEDLISKSpfeLSGGQMRRVAIAGVMA 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15830287  173 SNPRVLLLDEPTNHLDIETIDWLEGFLKTFNG---TIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:PRK13641 162 YEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKaghTVILVTHNMDDVAEYADDVLVLEHGKLI 224
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
137-228 2.36e-08

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


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 54.80  E-value: 2.36e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 137 NRINEVLAQLGL------DPNvalsSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGF----LKTFNGTI 206
Cdd:COG4136 112 ARVEQALEEAGLagfadrDPA----TLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQFREFvfeqIRQRGIPA 187
                        90       100
                ....*....|....*....|..
gi 15830287 207 IFISHDRSFIRNmATRIVDLDR 228
Cdd:COG4136 188 LLVTHDEEDAPA-AGRVLDLGN 208
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
335-496 2.50e-08

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: 55.16  E-value: 2.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   335 VKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV-GTKLEVAYFDQ----HRAELDPDKTVMDNLAEGKQ 409
Cdd:TIGR01184   1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILeGKQITEPGPDRmvvfQNYSLLPWLTVRENIALAVD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   410 EVMVN---GKPRHVLGYLQDFLFHPKRAMTPVRALSGGERNRLLLAR-LFLKPSnLLILDEPTNDLDVETLELLEELI-- 483
Cdd:TIGR01184  81 RVLPDlskSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARaLSIRPK-VLLLDEPFGALDALTRGNLQEELmq 159
                         170
                  ....*....|....*
gi 15830287   484 --DSYQGTVLLVSHD 496
Cdd:TIGR01184 160 iwEEHRVTVLMVTHD 174
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
304-495 2.70e-08

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 56.95  E-value: 2.70e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  304 TAKMQVEEASrsGKIVFEMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV-GTKL 382
Cdd:PRK11176 330 EGKRVIERAK--GDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLdGHDL 407
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  383 E----------VAYFDQHrAELDPDkTVMDNLAEGKQEVMVNGKPRHV--LGYLQDFLFHPKRAMTPV-----RALSGGE 445
Cdd:PRK11176 408 RdytlaslrnqVALVSQN-VHLFND-TIANNIAYARTEQYSREQIEEAarMAYAMDFINKMDNGLDTVigengVLLSGGQ 485
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15830287  446 RNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELIDSYQG--TVLLVSH 495
Cdd:PRK11176 486 RQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKnrTSLVIAH 537
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
330-472 2.75e-08

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


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 55.89  E-value: 2.75e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 330 DGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV-GTKLEVAyfDQHR-----AE--LDPDKTVM 401
Cdd:COG4152  12 GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWdGEPLDPE--DRRRigylpEErgLYPKMKVG 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 402 DNL-----------AEGKQEVMVngkprhvlgYLQDF-LfhPKRAMTPVRALSGGERNRL-LLARLFLKPSnLLILDEPT 468
Cdd:COG4152  90 EQLvylarlkglskAEAKRRADE---------WLERLgL--GDRANKKVEELSKGNQQKVqLIAALLHDPE-LLILDEPF 157

                ....
gi 15830287 469 NDLD 472
Cdd:COG4152 158 SGLD 161
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
316-495 3.03e-08

ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.


Pssm-ID: 213211 [Multi-domain]  Cd Length: 221  Bit Score: 54.42  E-value: 3.03e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 316 GKIVFEMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTkLEVAYFDQH----- 390
Cdd:cd03244   1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDG-VDISKIGLHdlrsr 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 391 ---------------RAELDP-----DKTVMDNLAEGKQEVMVNGKPrhvlGYLQdflfhpkramTPVRA----LSGGER 446
Cdd:cd03244  80 isiipqdpvlfsgtiRSNLDPfgeysDEELWQALERVGLKEFVESLP----GGLD----------TVVEEggenLSVGQR 145
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 15830287 447 NRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELIDSY--QGTVLLVSH 495
Cdd:cd03244 146 QLLCLARALLRKSKILVLDEATASVDPETDALIQKTIREAfkDCTVLTIAH 196
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
344-497 3.38e-08

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 55.88  E-value: 3.38e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  344 RGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVG----TKLEVAYFD-----QHRAeLDPDKTVMDNLAEG------- 407
Cdd:PRK11432  31 QGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDgedvTHRSIQQRDicmvfQSYA-LFPHMSLGENVGYGlkmlgvp 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  408 KQEVMVNGKPRHVLGYLQDFlfhPKRAmtpVRALSGGERNRLLLAR-LFLKPSNLLiLDEPTNDLDVETLELLEELIDSY 486
Cdd:PRK11432 110 KEERKQRVKEALELVDLAGF---EDRY---VDQISGGQQQRVALARaLILKPKVLL-FDEPLSNLDANLRRSMREKIREL 182
                        170
                 ....*....|....*
gi 15830287  487 QG----TVLLVSHDR 497
Cdd:PRK11432 183 QQqfniTSLYVTHDQ 197
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
11-232 3.43e-08

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 55.10  E-value: 3.43e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   11 LSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQG-----------LDDGRIIYE-QDLIVAR----LQQD 74
Cdd:PRK14271  29 LGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDkvsgyrysgdvLLGGRSIFNyRDVLEFRrrvgMLFQ 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   75 PPRNVEGSVYDFVAEGIeeqaeylkRYHdisRLVmndpSEKNLNELAkvQEQLDHHNLWQ-LENRINEvlaqlgldpnvA 153
Cdd:PRK14271 109 RPNPFPMSIMDNVLAGV--------RAH---KLV----PRKEFRGVA--QARLTEVGLWDaVKDRLSD-----------S 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  154 LSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFNG--TIIFISHDRSFIRNMATRIVDLDRGKL 231
Cdd:PRK14271 161 PFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADrlTVIIVTHNLAQAARISDRAALFFDGRL 240

                 .
gi 15830287  232 V 232
Cdd:PRK14271 241 V 241
cbiO PRK13643
energy-coupling factor transporter ATPase;
318-513 3.58e-08

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 55.12  E-value: 3.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  318 IVFEMEDVCYQVD---GKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKLEVAYFDQHraEL 394
Cdd:PRK13643   2 IKFEKVNYTYQPNspfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQK--EI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  395 DP-----------------DKTVMDNLAEGKQEVMVN--------GKPRHVLGYLQDFLfhpkrAMTPVRaLSGGERNRL 449
Cdd:PRK13643  80 KPvrkkvgvvfqfpesqlfEETVLKDVAFGPQNFGIPkekaekiaAEKLEMVGLADEFW-----EKSPFE-LSGGQMRRV 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15830287  450 LLARLFLKPSNLLILDEPTNDLDVETLELLEELIDSYQ---GTVLLVSHDRQFVDNTVTECWIFEGG 513
Cdd:PRK13643 154 AIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHqsgQTVVLVTHLMDDVADYADYVYLLEKG 220
cbiO PRK13637
energy-coupling factor transporter ATPase;
332-495 3.78e-08

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 55.05  E-value: 3.78e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  332 KQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGtklevayfdqhraELDP-DKTVmdNLAEGKQE 410
Cdd:PRK13637  20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIID-------------GVDItDKKV--KLSDIRKK 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  411 V-MVNGKPRHVL---GYLQDFLFHP--------------KRAMTPVR------------ALSGGERNRLLLARLF-LKPS 459
Cdd:PRK13637  85 VgLVFQYPEYQLfeeTIEKDIAFGPinlglseeeienrvKRAMNIVGldyedykdkspfELSGGQKRRVAIAGVVaMEPK 164
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 15830287  460 nLLILDEPTNDLDVETLELLEELI----DSYQGTVLLVSH 495
Cdd:PRK13637 165 -ILILDEPTAGLDPKGRDEILNKIkelhKEYNMTIILVSH 203
cbiO PRK13650
energy-coupling factor transporter ATPase;
14-212 4.06e-08

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 55.12  E-value: 4.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   14 SDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLI-----------VARLQQDPPRN-VEG 81
Cdd:PRK13650  18 QEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLteenvwdirhkIGMVFQNPDNQfVGA 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   82 SVYDFVAEGIEEQAeylkryhdisrlvmndpseknlnelakvqeqLDHHnlwQLENRINEVLAQLGL------DPnvalS 155
Cdd:PRK13650  98 TVEDDVAFGLENKG-------------------------------IPHE---EMKERVNEALELVGMqdfkerEP----A 139
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15830287  156 SLSGGWLRKAALGRALVSNPRVLLLDEPTNHLD----IETIDWLEGFLKTFNGTIIFISHD 212
Cdd:PRK13650 140 RLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDpegrLELIKTIKGIRDDYQMTVISITHD 200
TauB COG4525
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
1-224 4.58e-08

ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 443596 [Multi-domain]  Cd Length: 262  Bit Score: 54.48  E-value: 4.58e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   1 MSLISMHGAWLSF----SDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIiyeqdlivaRLQQDPp 76
Cdd:COG4525   1 MSMLTVRHVSVRYpgggQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEI---------TLDGVP- 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  77 rnVEG------------------SVYDFVAEGieeqaeyLKryhdisrlvmndpseknlneLAKVQEQldhhnlwQLENR 138
Cdd:COG4525  71 --VTGpgadrgvvfqkdallpwlNVLDNVAFG-------LR--------------------LRGVPKA-------ERRAR 114
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 139 INEVLAQLGLD--PNVALSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFL----KTFNGTIIFISHD 212
Cdd:COG4525 115 AEELLALVGLAdfARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLldvwQRTGKGVFLITHS 194
                       250
                ....*....|..
gi 15830287 213 RSFIRNMATRIV 224
Cdd:COG4525 195 VEEALFLATRLV 206
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
18-188 4.75e-08

The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 56.21  E-value: 4.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287    18 LLDNAELHIEDNERVCLVGRNGAGKSTLMKIL-NReqglddgriiyeqdlIVARLQQDPPRNVEGSVYDfvaegieeqae 96
Cdd:TIGR00955  40 LLKNVSGVAKPGELLAVMGSSGAGKTTLMNALaFR---------------SPKGVKGSGSVLLNGMPID----------- 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287    97 yLKRYHDISRLVMNDpsEKNLNELAkVQEQL---------DHHNLWQLENRINEVLAQLGL---------DPNvALSSLS 158
Cdd:TIGR00955  94 -AKEMRAISAYVQQD--DLFIPTLT-VREHLmfqahlrmpRRVTKKEKRERVDEVLQALGLrkcantrigVPG-RVKGLS 168
                         170       180       190
                  ....*....|....*....|....*....|
gi 15830287   159 GGWLRKAALGRALVSNPRVLLLDEPTNHLD 188
Cdd:TIGR00955 169 GGERKRLAFASELLTDPPLLFCDEPTSGLD 198
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
331-473 5.89e-08

ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.


Pssm-ID: 213258 [Multi-domain]  Cd Length: 282  Bit Score: 54.48  E-value: 5.89e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 331 GKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI-HVGtklEVAYFDQHrAELDPDkTVMDNLAEGKQ 409
Cdd:cd03291  49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIkHSG---RISFSSQF-SWIMPG-TIKENIIFGVS 123
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15830287 410 evMVNGKPRHVLGYLQ---DFLFHPKRAMTPVR----ALSGGERNRLLLARLFLKPSNLLILDEPTNDLDV 473
Cdd:cd03291 124 --YDEYRYKSVVKACQleeDITKFPEKDNTVLGeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 192
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
10-242 6.67e-08

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 56.19  E-value: 6.67e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287    10 WLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRII-----YEQDLIVARLQQDPPRNVEG--S 82
Cdd:PTZ00265 1175 YISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNDHHIvfkneHTNDMTNEQDYQGDEEQNVGmkN 1254
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287    83 VYDFVAEGIEEQAEYLKRYHDISRLVMN--DPSEKNLNEL----AKVQEQLDHHNLWQLEN------------------- 137
Cdd:PTZ00265 1255 VNEFSLTKEGGSGEDSTVFKNSGKILLDgvDICDYNLKDLrnlfSIVSQEPMLFNMSIYENikfgkedatredvkrackf 1334
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   138 -RINEVLAQL--GLDPNVAL--SSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEgflKTF-------NGT 205
Cdd:PTZ00265 1335 aAIDEFIESLpnKYDTNVGPygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIE---KTIvdikdkaDKT 1411
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 15830287   206 IIFISHDRSFIRNMATRIV--DLDR-GKLVTYPGNYDQYL 242
Cdd:PTZ00265 1412 IITIAHRIASIKRSDKIVVfnNPDRtGSFVQAHGTHEELL 1451
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
327-498 6.92e-08

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 53.67  E-value: 6.92e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  327 YQvDGK---QLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGR-IHVGTKL--------------EVAYFD 388
Cdd:PRK11629  15 YQ-EGSvqtDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDvIFNGQPMsklssaakaelrnqKLGFIY 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  389 QHRaELDPDKTVMDNLAE-----GKQEVMVNGKPRHVLGYLQdflfHPKRAMTPVRALSGGERNRLLLARLFLKPSNLLI 463
Cdd:PRK11629  94 QFH-HLLPDFTALENVAMplligKKKPAEINSRALEMLAAVG----LEHRANHRPSELSGGERQRVAIARALVNNPRLVL 168
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 15830287  464 LDEPTNDLDVETLE---LLEELIDSYQGTV-LLVSHDRQ 498
Cdd:PRK11629 169 ADEPTGNLDARNADsifQLLGELNRLQGTAfLVVTHDLQ 207
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
312-472 6.95e-08

ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444078 [Multi-domain]  Cd Length: 605  Bit Score: 55.60  E-value: 6.95e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 312 ASRSGKIVFEmeDVCYQVDGK-QLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV-GTKL-EVAyfd 388
Cdd:COG5265 352 VVGGGEVRFE--NVSFGYDPErPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIdGQDIrDVT--- 426
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 389 QH--RAELD--PDKTVM------DNLAEGK-----QEVmvngkpRHV--LGYLQDFLFH-PKRAMTPV--RA--LSGGER 446
Cdd:COG5265 427 QAslRAAIGivPQDTVLfndtiaYNIAYGRpdaseEEV------EAAarAAQIHDFIESlPDGYDTRVgeRGlkLSGGEK 500
                       170       180
                ....*....|....*....|....*.
gi 15830287 447 NRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:COG5265 501 QRVAIARTLLKNPPILIFDEATSALD 526
cbiO PRK13640
energy-coupling factor transporter ATPase;
14-232 7.21e-08

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 54.42  E-value: 7.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   14 SDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNreqGLddgriiyeqdlivaRLQQDPPRNVegsvydFVAEGIEE 93
Cdd:PRK13640  18 SKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLIN---GL--------------LLPDDNPNSK------ITVDGITL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   94 QAEYLKRYHDISRLVMNDPSEKNLNelAKVQEQLdhhnLWQLENR----------INEVLAQLG-LD-PNVALSSLSGGW 161
Cdd:PRK13640  75 TAKTVWDIREKVGIVFQNPDNQFVG--ATVGDDV----AFGLENRavprpemikiVRDVLADVGmLDyIDSEPANLSGGQ 148
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15830287  162 LRKAALGRALVSNPRVLLLDEPTNHLDIE----TIDWLEGFLKTFNGTIIFISHDRSFIrNMATRIVDLDRGKLV 232
Cdd:PRK13640 149 KQRVAIAGILAVEPKIIILDESTSMLDPAgkeqILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLL 222
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
318-500 7.57e-08

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 53.34  E-value: 7.57e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  318 IVFEMEDVCYqVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI----HVGTKL---EVAY---- 386
Cdd:PRK10908   2 IRFEHVSKAY-LGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIwfsgHDITRLknrEVPFlrrq 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  387 ----FDQHraELDPDKTVMDNLAegkQEVMVNGKP-----RHVLGYLQDFLFHPKRAMTPVRaLSGGERNRLLLARLFLK 457
Cdd:PRK10908  81 igmiFQDH--HLLMDRTVYDNVA---IPLIIAGASgddirRRVSAALDKVGLLDKAKNFPIQ-LSGGEQQRVGIARAVVN 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 15830287  458 PSNLLILDEPTNDLDVETLELLEELIDSYQG---TVLLVSHDRQFV 500
Cdd:PRK10908 155 KPAVLLADEPTGNLDDALSEGILRLFEEFNRvgvTVLMATHDIGLI 200
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
1-183 7.82e-08

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


Pssm-ID: 440752 [Multi-domain]  Cd Length: 240  Bit Score: 53.49  E-value: 7.82e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   1 MSLISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTL--MKIlnreqGL---DDGRI-IYEQDL------IV 68
Cdd:COG1137   1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTfyMIV-----GLvkpDSGRIfLDGEDIthlpmhKR 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  69 AR-----LQQDPprnvegSVydF----VAEGIeeqaeylkryhdisRLVMndpseknlnELAKVQEQldhhnlwQLENRI 139
Cdd:COG1137  76 ARlgigyLPQEA------SI--FrkltVEDNI--------------LAVL---------ELRKLSKK-------EREERL 117
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 15830287 140 NEVLAQLGLDP--NVALSSLSGGWLRKAALGRALVSNPRVLLLDEP 183
Cdd:COG1137 118 EELLEEFGITHlrKSKAYSLSGGERRRVEIARALATNPKFILLDEP 163
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
331-520 8.23e-08

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 55.30  E-value: 8.23e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  331 GKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKlEVAyFDQHRAELD-------------PD 397
Cdd:PRK11288  16 GVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQ-EMR-FASTTAALAagvaiiyqelhlvPE 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  398 KTVMDNLAEGK---QEVMVNGKP--RHVLGYLQ--DFLFHPKramTPVRALSGGERNRLLLARLFLKPSNLLILDEPTND 470
Cdd:PRK11288  94 MTVAENLYLGQlphKGGIVNRRLlnYEAREQLEhlGVDIDPD---TPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSS 170
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 15830287  471 LDVETLELLEELIDSY--QGTVLL-VSHDRQFVDNTVTECWIFegggKIGRYV 520
Cdd:PRK11288 171 LSAREIEQLFRVIRELraEGRVILyVSHRMEEIFALCDAITVF----KDGRYV 219
nickel_nikE TIGR02769
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ...
332-513 8.37e-08

nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 131816 [Multi-domain]  Cd Length: 265  Bit Score: 54.04  E-value: 8.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   332 KQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVG----TKLEVAYFDQHRAEL-----------DP 396
Cdd:TIGR02769  24 APVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRgqdlYQLDRKQRRAFRRDVqlvfqdspsavNP 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   397 DKTVMDNLAEGKQEVM---VNGKPRHVLGYLQDFLFHPKRAMTPVRALSGGERNRLLLAR-LFLKPsNLLILDEPTNDLD 472
Cdd:TIGR02769 104 RMTVRQIIGEPLRHLTsldESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARaLAVKP-KLIVLDEAVSNLD 182
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 15830287   473 VETLELLEELIDSYQ---GTV-LLVSHDRQFVDNTVTECWIFEGG 513
Cdd:TIGR02769 183 MVLQAVILELLRKLQqafGTAyLFITHDLRLVQSFCQRVAVMDKG 227
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
318-472 8.67e-08

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 53.99  E-value: 8.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  318 IVFEMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIhvgtklevaYFDQHRAELD-- 395
Cdd:PRK13648   8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEI---------FYNNQAITDDnf 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  396 -------------PDK-----TVMDNLAEGKQEVMVNGKPRH--VLGYLQDFLFHPKRAMTPvRALSGGERNRLLLAR-L 454
Cdd:PRK13648  79 eklrkhigivfqnPDNqfvgsIVKYDVAFGLENHAVPYDEMHrrVSEALKQVDMLERADYEP-NALSGGQKQRVAIAGvL 157
                        170
                 ....*....|....*...
gi 15830287  455 FLKPSnLLILDEPTNDLD 472
Cdd:PRK13648 158 ALNPS-VIILDEATSMLD 174
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
331-473 8.94e-08

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 53.84  E-value: 8.94e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  331 GKQLV-KDFSAQVLRGDKIALIGPNGCGKTTLLK----LML---GQLQADSGRIHVGTKLEVAY---FDQHRAELDPDKT 399
Cdd:PRK10253  18 GKYTVaENLTVEIPDGHFTAIIGPNGCGKSTLLRtlsrLMTpahGHVWLDGEHIQHYASKEVARrigLLAQNATTPGDIT 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  400 VMDNLAEGK-------------QEVMVNGKPRHV-LGYLqdflfhpkrAMTPVRALSGGERNRLLLARLFLKPSNLLILD 465
Cdd:PRK10253  98 VQELVARGRyphqplftrwrkeDEEAVTKAMQATgITHL---------ADQSVDTLSGGQRQRAWIAMVLAQETAIMLLD 168

                 ....*...
gi 15830287  466 EPTNDLDV 473
Cdd:PRK10253 169 EPTTWLDI 176
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
321-376 1.02e-07

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 53.62  E-value: 1.02e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15830287  321 EMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI 376
Cdd:PRK11831   9 DMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEI 64
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
337-473 1.04e-07

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 53.39  E-value: 1.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  337 DFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV----GTKLEVA----------------YFDQHRAE-LD 395
Cdd:PRK11701  24 DVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrdGQLRDLYalseaerrrllrtewgFVHQHPRDgLR 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  396 PDKTVMDNLAEgkqEVMVNGKpRH-------VLGYLQDFLFHPKRAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPT 468
Cdd:PRK11701 104 MQVSAGGNIGE---RLMAVGA-RHygdiratAGDWLERVEIDAARIDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPT 179

                 ....*
gi 15830287  469 NDLDV 473
Cdd:PRK11701 180 GGLDV 184
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
30-232 1.26e-07

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 54.86  E-value: 1.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   30 ERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQ---DLIVARLQQDPPRNVEGSVYDFVAEgieeqaeyLKRYHDISR 106
Cdd:PRK10261 351 ETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGqriDTLSPGKLQALRRDIQFIFQDPYAS--------LDPRQTVGD 422
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  107 LVMndpseknlnelakvqEQLDHHNLWQLE---NRINEVLAQLGLDPNVALS---SLSGGWLRKAALGRALVSNPRVLLL 180
Cdd:PRK10261 423 SIM---------------EPLRVHGLLPGKaaaARVAWLLERVGLLPEHAWRyphEFSGGQRQRICIARALALNPKVIIA 487
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15830287  181 DEPTNHLDI----ETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:PRK10261 488 DEAVSALDVsirgQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIV 543
cbiO PRK13649
energy-coupling factor transporter ATPase;
15-232 1.26e-07

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 53.59  E-value: 1.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   15 DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLIVARLQQDPPRNVE---GSVYDFVAEGI 91
Cdd:PRK13649  19 EGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQIRkkvGLVFQFPESQL 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   92 EEQAeylkryhdisrlVMNDPSEKNLNELAKVQEQldhhnlwqlENRINEVLAQLGLDPNVALSS---LSGGWLRKAALG 168
Cdd:PRK13649  99 FEET------------VLKDVAFGPQNFGVSQEEA---------EALAREKLALVGISESLFEKNpfeLSGGQMRRVAIA 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15830287  169 RALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFNG---TIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:PRK13649 158 GILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQsgmTIVLVTHLMDDVANYADFVYVLEKGKLV 224
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
34-473 1.31e-07

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 54.53  E-value: 1.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   34 LVGRNGAGKSTLMKILNREQGLDDGRIiyeqdLIVARLQQdpprnvEGSVYDFVAEGIE--EQaeylkryhdisrlvmnd 111
Cdd:PRK11288  35 LMGENGAGKSTLLKILSGNYQPDAGSI-----LIDGQEMR------FASTTAALAAGVAiiYQ----------------- 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  112 pseknlnELAKVQEQLDHHNLW--QLENR---------INEVLAQLG-----LDPNVALSSLSGGWLRKAALGRALVSNP 175
Cdd:PRK11288  87 -------ELHLVPEMTVAENLYlgQLPHKggivnrrllNYEAREQLEhlgvdIDPDTPLKYLSIGQRQMVEIAKALARNA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  176 RVLLLDEPTNHLDIETIDWLegF-----LKTFNGTIIFISHDRSFIRNMATRIVDLDRGKLV-TYPgnydqylleKEEAL 249
Cdd:PRK11288 160 RVIAFDEPTSSLSAREIEQL--FrvireLRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVaTFD---------DMAQV 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  250 RVEELQNAEFDRKLaqeevwirQGIKARRTRNEGRVRalkamrrergerrevmgtakMQVEEasrsgkivfemedvcyqV 329
Cdd:PRK11288 229 DRDQLVQAMVGREI--------GDIYGYRPRPLGEVR--------------------LRLDG-----------------L 263
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  330 DGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIhvgtklevaYFDQHRAELdpdKTVMDNLAEG-- 407
Cdd:PRK11288 264 KGPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQV---------YLDGKPIDI---RSPRDAIRAGim 331
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  408 ------KQEVMVNGKP----------RHVLGYlqDFLFHPKR------------------AMTPVRALSGGERNRLLLAR 453
Cdd:PRK11288 332 lcpedrKAEGIIPVHSvadninisarRHHLRA--GCLINNRWeaenadrfirslniktpsREQLIMNLSGGNQQKAILGR 409
                        490       500
                 ....*....|....*....|
gi 15830287  454 LFLKPSNLLILDEPTNDLDV 473
Cdd:PRK11288 410 WLSEDMKVILLDEPTRGIDV 429
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
18-234 1.49e-07

multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]


Pssm-ID: 188098 [Multi-domain]  Cd Length: 1522  Bit Score: 54.95  E-value: 1.49e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287     18 LLDNAELHIEDNERVCLVGRNGAGKST----LMKILNREQG--LDDGRIIYEQDLIVARLQ-----QDPPRnVEGSvydf 86
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSltlgLFRINESAEGeiIIDGLNIAKIGLHDLRFKitiipQDPVL-FSGS---- 1375
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287     87 vaegieeqaeylkryhdisrLVMN-DPSEKNLNELAKVQEQLDHhnlwqLENRINEVLAQLGLDPNVALSSLSGGWLRKA 165
Cdd:TIGR00957 1376 --------------------LRMNlDPFSQYSDEEVWWALELAH-----LKTFVSALPDKLDHECAEGGENLSVGQRQLV 1430
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15830287    166 ALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKT-FNG-TIIFISHDRSFIRNMaTRIVDLDRGKLVTY 234
Cdd:TIGR00957 1431 CLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTqFEDcTVLTIAHRLNTIMDY-TRVIVLDKGEVAEF 1500
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
333-472 1.50e-07

ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 443326 [Multi-domain]  Cd Length: 242  Bit Score: 52.71  E-value: 1.50e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 333 QLVKDFSAQVLRGDKIALIGPNGCGKTTLLKlMLGQLQ-ADSGRIHVGTklevAYFD--QHRAE---------------- 393
Cdd:COG4161  16 QALFDINLECPSGETLVLLGPSGAGKSSLLR-VLNLLEtPDSGQLNIAG----HQFDfsQKPSEkairllrqkvgmvfqq 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 394 --LDPDKTVMDNLAEG--------KQEVMvnGKPRHVLGYLQdflFHPKRAMTPVRaLSGGERNRLLLAR-LFLKPSNLL 462
Cdd:COG4161  91 ynLWPHLTVMENLIEApckvlglsKEQAR--EKAMKLLARLR---LTDKADRFPLH-LSGGQQQRVAIARaLMMEPQVLL 164
                       170
                ....*....|
gi 15830287 463 iLDEPTNDLD 472
Cdd:COG4161 165 -FDEPTAALD 173
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
19-224 1.64e-07

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 54.43  E-value: 1.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   19 LDNAELHIE-----DNERVCLVGRNGAGKSTLMKILNREQGLDDGRIiyEQDLIVARLQQDPPRNVEGSVYDFvaegiee 93
Cdd:PRK13409 350 LGDFSLEVEggeiyEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV--DPELKISYKPQYIKPDYDGTVEDL------- 420
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   94 qaeylkryhdisrlvmndpseknlneLAKVQEQLDHHNLWqlenriNEVLAQLGLDP--NVALSSLSGGWLRKAALGRAL 171
Cdd:PRK13409 421 --------------------------LRSITDDLGSSYYK------SEIIKPLQLERllDKNVKDLSGGELQRVAIAACL 468
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  172 VSNPRVLLLDEPTNHLDIE-------TIdwlEGFLKTFNGTIIFISHDRSFIRNMATRIV 224
Cdd:PRK13409 469 SRDADLYLLDEPSAHLDVEqrlavakAI---RRIAEEREATALVVDHDIYMIDYISDRLM 525
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
342-498 1.79e-07

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 52.47  E-value: 1.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  342 VLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKLEVAYFDQHRAELD--------------PDKTVMDN---- 403
Cdd:PRK10584  33 VKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRakhvgfvfqsfmliPTLNALENvelp 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  404 -LAEGKQEVMVNGKPRHVLGY--LQDFLFHpkramTPVRaLSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLE 480
Cdd:PRK10584 113 aLLRGESSRQSRNGAKALLEQlgLGKRLDH-----LPAQ-LSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIA 186
                        170       180
                 ....*....|....*....|..
gi 15830287  481 ELIDS----YQGTVLLVSHDRQ 498
Cdd:PRK10584 187 DLLFSlnreHGTTLILVTHDLQ 208
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
330-473 1.82e-07

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 52.96  E-value: 1.82e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  330 DGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV-GTKLE-------VAYFDQHRaELDPDKTVM 401
Cdd:PRK15056  18 NGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISIlGQPTRqalqknlVAYVPQSE-EVDWSFPVL 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  402 dnlaegKQEVMVNGKPRHvLGYLQDFLFHPKRAMTPVRA--------------LSGGERNRLLLARLFLKPSNLLILDEP 467
Cdd:PRK15056  97 ------VEDVVMMGRYGH-MGWLRRAKKRDRQIVTAALArvdmvefrhrqigeLSGGQKKRVFLARAIAQQGQVILLDEP 169

                 ....*.
gi 15830287  468 TNDLDV 473
Cdd:PRK15056 170 FTGVDV 175
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
21-232 1.94e-07

proline/glycine betaine ABC transporter ATP-binding protein ProV;


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 53.88  E-value: 1.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   21 NAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEqDLIVARLQQDPPRNVEGsvydfvaegiEEQAEYLKR 100
Cdd:PRK10070  46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLID-GVDIAKISDAELREVRR----------KKIAMVFQS 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  101 YHDISRLVMNDPSEKNLnELAKVQEQldhhnlwQLENRINEVLAQLGLDpNVAL---SSLSGGWLRKAALGRALVSNPRV 177
Cdd:PRK10070 115 FALMPHMTVLDNTAFGM-ELAGINAE-------ERREKALDALRQVGLE-NYAHsypDELSGGMRQRVGLARALAINPDI 185
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 15830287  178 LLLDEPTNHLD----IETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:PRK10070 186 LLMDEAFSALDplirTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVV 244
COG4674 COG4674
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
321-468 1.99e-07

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


Pssm-ID: 443710 [Multi-domain]  Cd Length: 250  Bit Score: 52.43  E-value: 1.99e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 321 EMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKlEVAYFDQHR-AELD---- 395
Cdd:COG4674  12 YVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGT-DLTGLDEHEiARLGigrk 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 396 -------PDKTVMDNLaegkqEVMVNGK--PRHVLGY------------------LQDflfhpkRAMTPVRALSGGERNR 448
Cdd:COG4674  91 fqkptvfEELTVFENL-----ELALKGDrgVFASLFArltaeerdrieevletigLTD------KADRLAGLLSHGQKQW 159
                       170       180
                ....*....|....*....|
gi 15830287 449 LLLARLFLKPSNLLILDEPT 468
Cdd:COG4674 160 LEIGMLLAQDPKLLLLDEPV 179
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
4-188 2.01e-07

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 53.30  E-value: 2.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287    4 ISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRI--IYEQDLIVARLQqdppRNVEG 81
Cdd:PRK13536  42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKItvLGVPVPARARLA----RARIG 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   82 SVYDFvaegieeqaeylkryhdisrlvmndpseKNLNELAKVQEQLDHHNLW------QLENRINEVL--AQLGLDPNVA 153
Cdd:PRK13536 118 VVPQF----------------------------DNLDLEFTVRENLLVFGRYfgmstrEIEAVIPSLLefARLESKADAR 169
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 15830287  154 LSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLD 188
Cdd:PRK13536 170 VSDLSGGMKRRLTLARALINDPQLLILDEPTTGLD 204
cbiO PRK13643
energy-coupling factor transporter ATPase;
13-233 2.08e-07

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 52.81  E-value: 2.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   13 FSDAPLLDnAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLIVARLQQD---PPRNVEGSVYDFVAE 89
Cdd:PRK13643  17 FASRALFD-IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeikPVRKKVGVVFQFPES 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   90 GIEEQAeylkryhdisrlVMNDPSEKNLNELAKVQEQldhhnlwqlENRINEVLAQLGLDPNVALSS---LSGGWLRKAA 166
Cdd:PRK13643  96 QLFEET------------VLKDVAFGPQNFGIPKEKA---------EKIAAEKLEMVGLADEFWEKSpfeLSGGQMRRVA 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15830287  167 LGRALVSNPRVLLLDEPTNHLD----IETIDWLEGFLKTfNGTIIFISHDRSFIRNMATRIVDLDRGKLVT 233
Cdd:PRK13643 155 IAGILAMEPEVLVLDEPTAGLDpkarIEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIIS 224
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
309-472 2.31e-07

Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 54.34  E-value: 2.31e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287    309 VEEASRSGKIVFEMEDVCYQV----DGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLqaDSGRIHVGTKL-- 382
Cdd:TIGR00956  749 KDMEKESGEDIFHWRNLTYEVkikkEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERV--TTGVITGGDRLvn 826
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287    383 ----------EVAYFDQHRAELdPDKTVMDNL---AEGKQ--EVMVNGKPRHVlGYLQDFLFHPKRA----MTPVRALSG 443
Cdd:TIGR00956  827 grpldssfqrSIGYVQQQDLHL-PTSTVRESLrfsAYLRQpkSVSKSEKMEYV-EEVIKLLEMESYAdavvGVPGEGLNV 904
                          170       180       190
                   ....*....|....*....|....*....|
gi 15830287    444 GERNRLLLA-RLFLKPSNLLILDEPTNDLD 472
Cdd:TIGR00956  905 EQRKRLTIGvELVAKPKLLLFLDEPTSGLD 934
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
344-512 2.43e-07

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


Pssm-ID: 213189 [Multi-domain]  Cd Length: 177  Bit Score: 51.03  E-value: 2.43e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 344 RGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIhvgtklevayfdqhraELDpdktvmdnlaegkqEVMVNGKPRHVlgy 423
Cdd:cd03222  24 EGEVIGIVGPNGTGKTTAVKILAGQLIPNGDND----------------EWD--------------GITPVYKPQYI--- 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 424 lqdflfhpkramtpvrALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELIDSY----QGTVLLVSHDRQF 499
Cdd:cd03222  71 ----------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLseegKKTALVVEHDLAV 134
                       170
                ....*....|...
gi 15830287 500 VDNTVTECWIFEG 512
Cdd:cd03222 135 LDYLSDRIHVFEG 147
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
18-193 2.65e-07

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 52.20  E-value: 2.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   18 LLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRI-IYEQDLIVARLQQDPPRNVEgsvydfvaegieeqae 96
Cdd:PRK10895  18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIiIDDEDISLLPLHARARRGIG---------------- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   97 YLKRYHDI-SRLVMNDpsekNLNELAKVQEQLDHHnlwQLENRINEVLAQLGLD--PNVALSSLSGGWLRKAALGRALVS 173
Cdd:PRK10895  82 YLPQEASIfRRLSVYD----NLMAVLQIRDDLSAE---QREDRANELMEEFHIEhlRDSMGQSLSGGERRRVEIARALAA 154
                        170       180
                 ....*....|....*....|.
gi 15830287  174 NPRVLLLDEPTNHLD-IETID 193
Cdd:PRK10895 155 NPKFILLDEPFAGVDpISVID 175
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
19-245 2.69e-07

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 52.93  E-value: 2.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNreqglddGRIIYEQDLIVARlqqdppRNVEGSVYDFVAEGIEEQAEYL 98
Cdd:PRK13631  42 LNNISYTFEKNKIYFIIGNSGSGKSTLVTHFN-------GLIKSKYGTIQVG------DIYIGDKKNNHELITNPYSKKI 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   99 KRYHDISRLV-----------MNDPSEKNL--NELAKVQEQLDHHNLWQLEnrinevLAQLGLDPNVALSS---LSGGWL 162
Cdd:PRK13631 109 KNFKELRRRVsmvfqfpeyqlFKDTIEKDImfGPVALGVKKSEAKKLAKFY------LNKMGLDDSYLERSpfgLSGGQK 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  163 RKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTF---NGTIIFISHDRSFIRNMATRIVDLDRGKLVTYPGNY- 238
Cdd:PRK13631 183 RRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAkanNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYe 262
                        250
                 ....*....|
gi 15830287  239 ---DQYLLEK 245
Cdd:PRK13631 263 iftDQHIINS 272
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
317-472 2.96e-07

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 52.30  E-value: 2.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  317 KIVFEMEDVC--YQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV-GTKLEVAYFDQHRAE 393
Cdd:PRK13632   5 SVMIKVENVSfsYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIdGITISKENLKEIRKK 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  394 L-----DPDK-----TVMDNLAEGKQEVMVNGK--PRHVLGYLQ-----DFL-FHPKRamtpvraLSGGERNRLLLAR-L 454
Cdd:PRK13632  85 IgiifqNPDNqfigaTVEDDIAFGLENKKVPPKkmKDIIDDLAKkvgmeDYLdKEPQN-------LSGGQKQRVAIASvL 157
                        170
                 ....*....|....*...
gi 15830287  455 FLKPSnLLILDEPTNDLD 472
Cdd:PRK13632 158 ALNPE-IIIFDESTSMLD 174
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
11-232 2.98e-07

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 52.30  E-value: 2.98e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   11 LSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNReqglddgriiyeqdLIVArlqqdpprnVEGSVYdFVAEG 90
Cdd:PRK10253  15 LGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSR--------------LMTP---------AHGHVW-LDGEH 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   91 IEEQA--EYLKRyhdISRLVMN--DPSEKNLNELAkVQEQLDHHNL---WQLENR--INEVLAQLGLD--PNVALSSLSG 159
Cdd:PRK10253  71 IQHYAskEVARR---IGLLAQNatTPGDITVQELV-ARGRYPHQPLftrWRKEDEeaVTKAMQATGIThlADQSVDTLSG 146
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15830287  160 GWLRKAALGRALVSNPRVLLLDEPTNHLDI-ETIDWLEgFLKTFNG----TIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:PRK10253 147 GQRQRAWIAMVLAQETAIMLLDEPTTWLDIsHQIDLLE-LLSELNRekgyTLAAVLHDLNQACRYASHLIALREGKIV 223
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
3-236 3.13e-07

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 52.32  E-value: 3.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287    3 LISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMK----ILNREQG--LDDGRII--YEQDLIVARLQ-- 72
Cdd:PRK13638   1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMnlsgLLRPQKGavLWQGKPLdySKRGLLALRQQva 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   73 ---QDPprnvegsvydfvaegiEEQAEYLKRYHDISRlvmndpSEKNLNelakVQEQldhhnlwQLENRINEVLAQLGLD 149
Cdd:PRK13638  81 tvfQDP----------------EQQIFYTDIDSDIAF------SLRNLG----VPEA-------EITRRVDEALTLVDAQ 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  150 --PNVALSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFNGT---IIFISHDRSFIRNMATRIV 224
Cdd:PRK13638 128 hfRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQgnhVIISSHDIDLIYEISDAVY 207
                        250
                 ....*....|....
gi 15830287  225 DLDRGKLVTY--PG 236
Cdd:PRK13638 208 VLRQGQILTHgaPG 221
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
18-276 3.73e-07

cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]


Pssm-ID: 273530 [Multi-domain]  Cd Length: 1490  Bit Score: 53.76  E-value: 3.73e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287     18 LLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGlDDGRIiyeqdlivarlqqdpprNVEGSVYDFV-------AEG 90
Cdd:TIGR01271 1234 VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEI-----------------QIDGVSWNSVtlqtwrkAFG 1295
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287     91 IEEQaeylKRYHDISRLVMN-DPSEK-NLNELAKVQEQLDHHN-LWQLENRINEVLAQLGLdpnvalsSLSGGWLRKAAL 167
Cdd:TIGR01271 1296 VIPQ----KVFIFSGTFRKNlDPYEQwSDEEIWKVAEEVGLKSvIEQFPDKLDFVLVDGGY-------VLSNGHKQLMCL 1364
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287    168 GRALVSNPRVLLLDEPTNHLDIETIDWLEGFLK-TF-NGTIIFISHdrsfirnmatRIvdldrgklvtypgnydQYLLEK 245
Cdd:TIGR01271 1365 ARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKqSFsNCTVILSEH----------RV----------------EALLEC 1418
                          250       260       270
                   ....*....|....*....|....*....|...
gi 15830287    246 EEALRVEELQNAEFD--RKLAQEEVWIRQGIKA 276
Cdd:TIGR01271 1419 QQFLVIEGSSVKQYDsiQKLLNETSLFKQAMSA 1451
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
21-231 3.80e-07

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 53.13  E-value: 3.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   21 NAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLIVARlqqdpprnvegSVYDFVAEGIEeqaeYLKR 100
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINAL-----------STAQRLARGLV----YLPE 345
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  101 YHDISRLVMNDPSEKNLNELAkvqeqldHHN--LWQLENRINEVL----AQLGL---DPNVALSSLSGGWLRKAALGRAL 171
Cdd:PRK15439 346 DRQSSGLYLDAPLAWNVCALT-------HNRrgFWIKPARENAVLeryrRALNIkfnHAEQAARTLSGGNQQKVLIAKCL 418
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15830287  172 VSNPRVLLLDEPTNHLDIETIDWLEGFLKTF---NGTIIFISHDRSFIRNMATRIVDLDRGKL 231
Cdd:PRK15439 419 EASPQLLIVDEPTRGVDVSARNDIYQLIRSIaaqNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
319-472 3.91e-07

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 52.00  E-value: 3.91e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  319 VFEMEDVCYQV-DGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKlevayfdqhraELDPD 397
Cdd:PRK13639   1 ILETRDLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGE-----------PIKYD 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  398 KTvmdNLAEGKQEV-MVNGKPRHVL---GYLQDFLFHP-----------KRAMTPVRA-------------LSGGERNRL 449
Cdd:PRK13639  70 KK---SLLEVRKTVgIVFQNPDDQLfapTVEEDVAFGPlnlglskeeveKRVKEALKAvgmegfenkpphhLSGGQKKRV 146
                        170       180
                 ....*....|....*....|...
gi 15830287  450 LLARLFLKPSNLLILDEPTNDLD 472
Cdd:PRK13639 147 AIAGILAMKPEIIVLDEPTSGLD 169
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
3-229 4.01e-07

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 51.62  E-value: 4.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287    3 LISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLIVAR-------LQQD- 74
Cdd:PRK11248   1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPgaergvvFQNEg 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   75 --PPRNVEgsvyDFVAEGIE----EQAEYLKRYHDIsrlvmndpseknlneLAKVQ-EQLDHHNLWQLenrinevlaqlg 147
Cdd:PRK11248  81 llPWRNVQ----DNVAFGLQlagvEKMQRLEIAHQM---------------LKKVGlEGAEKRYIWQL------------ 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  148 ldpnvalsslSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWL-EGFLKTFNGT---IIFISHDRSFIRNMATRI 223
Cdd:PRK11248 130 ----------SGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMqTLLLKLWQETgkqVLLITHDIEEAVFMATEL 199

                 ....*.
gi 15830287  224 VDLDRG 229
Cdd:PRK11248 200 VLLSPG 205
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
321-500 4.60e-07

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 51.66  E-value: 4.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  321 EMEDVCYQV-DGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV-GTKLEVAYFDQHRAEL---- 394
Cdd:PRK13647   6 EVEDLHFRYkDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVmGREVNAENEKWVRSKVglvf 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  395 -DPD-----KTVMDNLAEGKQEV-----MVNGKPRHVLGYLQDFLFHPKramtPVRALSGGERNRLLLARLFLKPSNLLI 463
Cdd:PRK13647  86 qDPDdqvfsSTVWDDVAFGPVNMgldkdEVERRVEEALKAVRMWDFRDK----PPYHLSYGQKKRVAIAGVLAMDPDVIV 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 15830287  464 LDEPTNDLDVETLELLEELID--SYQG-TVLLVSHDRQFV 500
Cdd:PRK13647 162 LDEPMAYLDPRGQETLMEILDrlHNQGkTVIVATHDVDLA 201
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
325-473 4.73e-07

ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];


Pssm-ID: 440213 [Multi-domain]  Cd Length: 320  Bit Score: 51.98  E-value: 4.73e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 325 VCYQVDGKQL--VKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQA---DSGRIHVG----TKLEVAYFDQHRAE-- 393
Cdd:COG0444   9 VYFPTRRGVVkaVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDgedlLKLSEKELRKIRGRei 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 394 ----------LDPDKTVMDNLAE--------GKQEVMvngkpRHVLGYLQDF-LFHPKRAMtpvRA----LSGGERNRLL 450
Cdd:COG0444  89 qmifqdpmtsLNPVMTVGDQIAEplrihgglSKAEAR-----ERAIELLERVgLPDPERRL---DRypheLSGGMRQRVM 160
                       170       180
                ....*....|....*....|....
gi 15830287 451 LAR-LFLKPSnLLILDEPTNDLDV 473
Cdd:COG0444 161 IARaLALEPK-LLIADEPTTALDV 183
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
344-496 5.34e-07

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 52.50  E-value: 5.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  344 RGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI-HVGTKLEVayFDQHR-AELdpdKTVMDNLAEGKQEV-----MVNGK 416
Cdd:PRK13409  98 EGKVTGILGPNGIGKTTAVKILSGELIPNLGDYeEEPSWDEV--LKRFRgTEL---QNYFKKLYNGEIKVvhkpqYVDLI 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  417 PRHVLGYLQDFLfhpKRA--------------MTPV-----RALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLE 477
Cdd:PRK13409 173 PKVFKGKVRELL---KKVdergkldevverlgLENIldrdiSELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRL 249
                        170       180
                 ....*....|....*....|.
gi 15830287  478 LLEELIDSYQG--TVLLVSHD 496
Cdd:PRK13409 250 NVARLIRELAEgkYVLVVEHD 270
hmuV PRK13547
heme ABC transporter ATP-binding protein;
18-232 5.84e-07

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 51.37  E-value: 5.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   18 LLDNAELHIEDNERVCLVGRNGAGKSTLMKILNRE-------QGLD-------DGRIIYEQD-LIVARLQQDPPRNVEGS 82
Cdd:PRK13547  16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDltgggapRGARvtgdvtlNGEPLAAIDaPRLARLRAVLPQAAQPA 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   83 vYDFVAEGIEeqaeYLKRYhdisrlvmndPSEKNLNELAkvqeqldHHNlwqlENRINEVLAQLGLDPNVA--LSSLSGG 160
Cdd:PRK13547  96 -FAFSAREIV----LLGRY----------PHARRAGALT-------HRD----GEIAWQALALAGATALVGrdVTTLSGG 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  161 WLRKAALGRAL---------VSNPRVLLLDEPTNHLDI----ETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLD 227
Cdd:PRK13547 150 ELARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDLahqhRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLA 229

                 ....*
gi 15830287  228 RGKLV 232
Cdd:PRK13547 230 DGAIV 234
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
26-224 6.41e-07

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


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 52.48  E-value: 6.41e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  26 IEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIiyEQDLIVARLQQDPPRNVEGSVYDFVAEGIEEQAEylkryhdis 105
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV--DEDLKISYKPQYISPDYDGTVEEFLRSANTDDFG--------- 431
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 106 rlvmndpseknlnelakvqeqldhHNLWQlenriNEVLAQLGLDP--NVALSSLSGGWLRKAALGRALVSNPRVLLLDEP 183
Cdd:COG1245 432 ------------------------SSYYK-----TEIIKPLGLEKllDKNVKDLSGGELQRVAIAACLSRDADLYLLDEP 482
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 15830287 184 TNHLDIE-------TIdwlEGFLKTFNGTIIFISHDRSFIRNMATRIV 224
Cdd:COG1245 483 SAHLDVEqrlavakAI---RRFAENRGKTAMVVDHDIYLIDYISDRLM 527
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
4-188 7.03e-07

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 51.34  E-value: 7.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287    4 ISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLIVARLQQdpPRNVEGSV 83
Cdd:PRK13537   8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARH--ARQRVGVV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   84 Y-------DFVaegIEEQAEYLKRY-----HDISRLVmndpseKNLNELAKvqeqldhhnlwqLENRINevlAQLGldpn 151
Cdd:PRK13537  86 PqfdnldpDFT---VRENLLVFGRYfglsaAAARALV------PPLLEFAK------------LENKAD---AKVG---- 137
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 15830287  152 valsSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLD 188
Cdd:PRK13537 138 ----ELSGGMKRRLTLARALVNDPDVLVLDEPTTGLD 170
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
344-496 8.45e-07

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


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 52.09  E-value: 8.45e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 344 RGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV-GTKLEVayFDQHR-AELdpdKTVMDNLAEGKQEV-----MVNGK 416
Cdd:COG1245  98 KGKVTGILGPNGIGKSTALKILSGELKPNLGDYDEePSWDEV--LKRFRgTEL---QDYFKKLANGEIKVahkpqYVDLI 172
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 417 PRHVLGYLQDFLfhpKRA--------------MTP-----VRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLE 477
Cdd:COG1245 173 PKVFKGTVRELL---EKVdergkldelaeklgLENildrdISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRL 249
                       170       180
                ....*....|....*....|..
gi 15830287 478 LLEELIDSYQG---TVLLVSHD 496
Cdd:COG1245 250 NVARLIRELAEegkYVLVVEHD 271
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
150-231 1.09e-06

D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 131681 [Multi-domain]  Cd Length: 500  Bit Score: 51.75  E-value: 1.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   150 PNVALSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIET---IDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDL 226
Cdd:TIGR02633 397 PFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAkyeIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVI 476

                  ....*
gi 15830287   227 DRGKL 231
Cdd:TIGR02633 477 GEGKL 481
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
4-230 1.17e-06

ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.


Pssm-ID: 213217 [Multi-domain]  Cd Length: 204  Bit Score: 49.78  E-value: 1.17e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   4 ISMHGAWLSFSD-----APLLDNAELHIEDNERVCLVGRNGAGKSTL-MKILNrEQGLDDGRIiyeqdlivarlqqdppr 77
Cdd:cd03250   1 ISVEDASFTWDSgeqetSFTLKDINLEVPKGELVAIVGPVGSGKSSLlSALLG-ELEKLSGSV----------------- 62
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  78 NVEGSVyDFVAegieeQAEYLkryhdisrlvMNdpseknlnelAKVQE------QLDhhnlwqlENRINEVLAQLGLDPN 151
Cdd:cd03250  63 SVPGSI-AYVS-----QEPWI----------QN----------GTIREnilfgkPFD-------EERYEKVIKACALEPD 109
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 152 VAL-------------SSLSGGwlRKA--ALGRALVSNPRVLLLDEPTNHLDIETIDWL-----EGFLKtFNGTIIFISH 211
Cdd:cd03250 110 LEIlpdgdlteigekgINLSGG--QKQriSLARAVYSDADIYLLDDPLSAVDAHVGRHIfenciLGLLL-NNKTRILVTH 186
                       250
                ....*....|....*....
gi 15830287 212 DRSFIRNmATRIVDLDRGK 230
Cdd:cd03250 187 QLQLLPH-ADQIVVLDNGR 204
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
319-472 1.23e-06

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 50.57  E-value: 1.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  319 VFEMEDVCYQVDG-KQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV-GTKLEVAYFDQHRAEL-- 394
Cdd:PRK13652   3 LIETRDLCYSYSGsKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIrGEPITKENIREVRKFVgl 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  395 ---DPDKTVMDNLAE----------GKQEVMVNGKPR---HVLGyLQDFlfhpkRAMTPvRALSGGERNRLLLARLFLKP 458
Cdd:PRK13652  83 vfqNPDDQIFSPTVEqdiafgpinlGLDEETVAHRVSsalHMLG-LEEL-----RDRVP-HHLSGGEKKRVAIAGVIAME 155
                        170
                 ....*....|....
gi 15830287  459 SNLLILDEPTNDLD 472
Cdd:PRK13652 156 PQVLVLDEPTAGLD 169
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
330-472 1.34e-06

sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 51.00  E-value: 1.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  330 DGK-QLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVG----TKLEVAYFD-----QHRAeLDPDKT 399
Cdd:PRK11650  14 DGKtQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGgrvvNELEPADRDiamvfQNYA-LYPHMS 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  400 VMDNLAEG-------KQEvmVNGKPRHVLGYL--QDFLfhpKRamTPvRALSGGERNRLLLARLFLKPSNLLILDEPTND 470
Cdd:PRK11650  93 VRENMAYGlkirgmpKAE--IEERVAEAARILelEPLL---DR--KP-RELSGGQRQRVAMGRAIVREPAVFLFDEPLSN 164

                 ..
gi 15830287  471 LD 472
Cdd:PRK11650 165 LD 166
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
1-212 1.36e-06

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 50.11  E-value: 1.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287    1 MSLISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLIVARLQQdpprnve 80
Cdd:PRK09544   2 TSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQ------- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   81 gsvydfvaegieeqaeylKRYHD------ISRLVMNDPSEKN---LNELAKVQEQldhHNLwqlenrinevlaqlgldpN 151
Cdd:PRK09544  75 ------------------KLYLDttlpltVNRFLRLRPGTKKediLPALKRVQAG---HLI------------------D 115
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15830287  152 VALSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIE----TIDWLEGFLKTFNGTIIFISHD 212
Cdd:PRK09544 116 APMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNgqvaLYDLIDQLRRELDCAVLMVSHD 180
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
12-253 1.43e-06

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 50.01  E-value: 1.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   12 SFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNreqGLDDGRIIYEQ--DLIVARLQQdpprnvEGSVYDFVAE 89
Cdd:PRK09984  13 TFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLS---GLITGDKSAGShiELLGRTVQR------EGRLARDIRK 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   90 GIEEQAEYLKRYHDISRLVM----------NDPSEKN-LNELAKVQEQldhhnlwqlenRINEVLAQLGLD--PNVALSS 156
Cdd:PRK09984  84 SRANTGYIFQQFNLVNRLSVlenvligalgSTPFWRTcFSWFTREQKQ-----------RALQALTRVGMVhfAHQRVST 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  157 LSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIET----IDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKlV 232
Cdd:PRK09984 153 LSGGQQQRVAIARALMQQAKVILADEPIASLDPESarivMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGH-V 231
                        250       260
                 ....*....|....*....|....*.
gi 15830287  233 TYPGNYDQYLLEKEEAL-----RVEE 253
Cdd:PRK09984 232 FYDGSSQQFDNERFDHLyrsinRVEE 257
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
345-472 1.56e-06

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 49.63  E-value: 1.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  345 GDKIALIGPNGCGKTTLLKLmLGQLQ-ADSGrihvgtKLEVA--YFD--------QHRA------------ELDPDKTVM 401
Cdd:PRK11124  28 GETLVLLGPSGAGKSSLLRV-LNLLEmPRSG------TLNIAgnHFDfsktpsdkAIRElrrnvgmvfqqyNLWPHLTVQ 100
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15830287  402 DNLAEGKQEVMVNGKPR---HVLGYLQDFLFHPKRAMTPVRaLSGGERNRLLLAR-LFLKPSNLLiLDEPTNDLD 472
Cdd:PRK11124 101 QNLIEAPCRVLGLSKDQalaRAEKLLERLRLKPYADRFPLH-LSGGQQQRVAIARaLMMEPQVLL-FDEPTAALD 173
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
319-496 1.74e-06

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 49.70  E-value: 1.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  319 VFEMEDVCYQVDGkQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQAD----SGRIHV-GTKLE--------VA 385
Cdd:PRK10418   4 QIELRNIALQAAQ-PLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGvrqtAGRVLLdGKPVApcalrgrkIA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  386 YFDQH-RAELDPDKTVMDNLAEGKQEVMVNGKPRHVLGYLQDF-LFHPKRA--MTPVRaLSGGERNRLLLARLFLKPSNL 461
Cdd:PRK10418  83 TIMQNpRSAFNPLHTMHTHARETCLALGKPADDATLTAALEAVgLENAARVlkLYPFE-MSGGMLQRMMIALALLCEAPF 161
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 15830287  462 LILDEPTNDLDVETLELLEELIDSYQGT----VLLVSHD 496
Cdd:PRK10418 162 IIADEPTTDLDVVAQARILDLLESIVQKralgMLLVTHD 200
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
149-232 1.80e-06

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 50.79  E-value: 1.80e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 149 DPNVALSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDI----ETIDWLEGFLKtfNGT-IIFISHDRSFIRNMATRI 223
Cdd:COG1129 387 SPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVgakaEIYRLIRELAA--EGKaVIVISSELPELLGLSDRI 464

                ....*....
gi 15830287 224 VDLDRGKLV 232
Cdd:COG1129 465 LVMREGRIV 473
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
19-232 1.99e-06

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 49.69  E-value: 1.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   19 LDNAELHIEDNERVCLVGRNGAGKSTLM----KILNREQG---LDDGRIIYE-QDLIVARLQ-----QDPPRNV-EGSVY 84
Cdd:PRK13639  18 LKGINFKAEKGEMVALLGPNGAGKSTLFlhfnGILKPTSGevlIKGEPIKYDkKSLLEVRKTvgivfQNPDDQLfAPTVE 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   85 DFVAEGieeqaeylkryhdisRLVMNDPSEknlnelakvqeqldhhnlwQLENRINEVLAQLGLD--PNVALSSLSGGWL 162
Cdd:PRK13639  98 EDVAFG---------------PLNLGLSKE-------------------EVEKRVKEALKAVGMEgfENKPPHHLSGGQK 143
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15830287  163 RKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFNG---TIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:PRK13639 144 KRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKegiTIIISTHDVDLVPVYADKVYVMSDGKII 216
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
155-232 2.02e-06

ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 443660 [Multi-domain]  Cd Length: 563  Bit Score: 50.90  E-value: 2.02e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 155 SSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLD-------IETIDwlegFLKTFNGTIIFISHDRSFIrNMATRIVDLD 227
Cdd:COG4618 466 ARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDdegeaalAAAIR----ALKARGATVVVITHRPSLL-AAVDKLLVLR 540

                ....*
gi 15830287 228 RGKLV 232
Cdd:COG4618 541 DGRVQ 545
YbjD COG3593
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ...
19-187 2.05e-06

Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];


Pssm-ID: 442812 [Multi-domain]  Cd Length: 359  Bit Score: 50.39  E-value: 2.05e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  19 LDNAELHIEDNeRVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLIVARLQQDPPRNVEgsvydfvaegieeqAEYL 98
Cdd:COG3593  14 IKDLSIELSDD-LTVLVGENNSGKSSILEALRLLLGPSSSRKFDEEDFYLGDDPDLPEIEIE--------------LTFG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  99 KRYHDISRLVMNDPSEKNLNE-LAKVQEQLDHHnLWQLENRINEVLAQLGLDPNVAL----------------------- 154
Cdd:COG3593  79 SLLSRLLRLLLKEEDKEELEEaLEELNEELKEA-LKALNELLSEYLKELLDGLDLELelsldeledllkslslriedgke 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 15830287 155 ---SSLSGG--WLRKAALGRALV-----SNPRVLLLDEPTNHL 187
Cdd:COG3593 158 lplDRLGSGfqRLILLALLSALAelkraPANPILLIEEPEAHL 200
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
15-230 2.36e-06

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 51.18  E-value: 2.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287    15 DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYE-----QDL-------IVARLQQDP------- 75
Cdd:PTZ00265  397 DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdshnlKDInlkwwrsKIGVVSQDPllfsnsi 476
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287    76 PRNVEGSVYDFV-AEGIEEQAE----------------YLKRYHDISrLVMNDPSEKNLNELAKVQEQLDHHNLWQLENR 138
Cdd:PTZ00265  477 KNNIKYSLYSLKdLEALSNYYNedgndsqenknkrnscRAKCAGDLN-DMSNTTDSNELIEMRKNYQTIKDSEVVDVSKK 555
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   139 --INEVLAQLGlDPNVAL-----SSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLD-------IETIDWLEGflkTFNG 204
Cdd:PTZ00265  556 vlIHDFVSALP-DKYETLvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDnkseylvQKTINNLKG---NENR 631
                         250       260
                  ....*....|....*....|....*.
gi 15830287   205 TIIFISHDRSFIRNMATRIVDLDRGK 230
Cdd:PTZ00265  632 ITIIIAHRLSTIRYANTIFVLSNRER 657
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
149-232 2.78e-06

ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 50.41  E-value: 2.78e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 149 DPNVALSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDW-----LEgfLKTFNGTIIFISHDRSFIRNMATRI 223
Cdd:COG3845 395 GPDTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFihqrlLE--LRDAGAAVLLISEDLDEILALSDRI 472

                ....*....
gi 15830287 224 VDLDRGKLV 232
Cdd:COG3845 473 AVMYEGRIV 481
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
349-501 2.88e-06

ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.


Pssm-ID: 213207 [Multi-domain]  Cd Length: 204  Bit Score: 48.37  E-value: 2.88e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 349 ALIGPNGCGKTTLLKlmlgqlqadsgrihvgtKLEVAYFDQHRAELDPDKTVMDNLAEGKQEVMV-------NGKPRHVL 421
Cdd:cd03240  26 LIVGQNGAGKTTIIE-----------------ALKYALTGELPPNSKGGAHDPKLIREGEVRAQVklafenaNGKKYTIT 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 422 GYL----------QDFLFHPkrAMTPVRALSGGERN------RLLLARLFLKPSNLLILDEPTNDLDVETLELLEELI-D 484
Cdd:cd03240  89 RSLailenvifchQGESNWP--LLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEESLAEIiE 166
                       170       180
                ....*....|....*....|.
gi 15830287 485 SYQGT----VLLVSHDRQFVD 501
Cdd:cd03240 167 ERKSQknfqLIVITHDEELVD 187
PLN03232 PLN03232
ABC transporter C family member; Provisional
332-472 3.11e-06

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 50.74  E-value: 3.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   332 KQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQ--ADSGRIHVGTkleVAYFDQhrAELDPDKTVMDNLAEG-K 408
Cdd:PLN03232  630 KPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELShaETSSVVIRGS---VAYVPQ--VSWIFNATVRENILFGsD 704
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15830287   409 QEVMVNGKPRHVLGYLQDFLFHPKRAMTPVRA----LSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:PLN03232  705 FESERYWRAIDVTALQHDLDLLPGRDLTEIGErgvnISGGQKQRVSMARAVYSNSDIYIFDDPLSALD 772
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
10-211 3.12e-06

ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.


Pssm-ID: 213184 [Multi-domain]  Cd Length: 200  Bit Score: 48.29  E-value: 3.12e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  10 WLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKIL--NREQGLDDGRIIYE-QDLI------VARL-----QQDP 75
Cdd:cd03217   7 HVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVTEGEILFKgEDITdlppeeRARLgiflaFQYP 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  76 PRnVEG-SVYDFVaegieeqaeylkryhdisrlvmndpseKNLNElakvqeqldhhnlwqlenrinevlaqlgldpnval 154
Cdd:cd03217  87 PE-IPGvKNADFL---------------------------RYVNE----------------------------------- 103
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 155 sSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTF---NGTIIFISH 211
Cdd:cd03217 104 -GFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLreeGKSVLIITH 162
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
29-223 3.27e-06

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 47.37  E-value: 3.27e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287     29 NERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYeqdlivarlqqdpprnvegsvydFVAEGIEEQAEYLKRYHDISRLV 108
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIY-----------------------IDGEDILEEVLDQLLLIIVGGKK 58
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287    109 MNDPSEKNLnelakvqeqldhhnlwqlenrinevlaqlgldpnvalsslsggwlrKAALGRALVSNPRVLLLDEPTNHLD 188
Cdd:smart00382  59 ASGSGELRL----------------------------------------------RLALALARKLKPDVLILDEITSLLD 92
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 15830287    189 IET---------IDWLEGFLKTFNGTIIFISHDRSFIRNMATRI 223
Cdd:smart00382  93 AEQeallllleeLRLLLLLKSEKNLTVILTTNDEKDLGPALLRR 136
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
335-521 3.66e-06

ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.


Pssm-ID: 213205 [Multi-domain]  Cd Length: 176  Bit Score: 47.70  E-value: 3.66e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 335 VKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLgqlqADSGRIHVGTKLEVAYfdqhraeldPDKTVM-DNLaegkQEVMV 413
Cdd:cd03238  11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGL----YASGKARLISFLPKFS---------RNKLIFiDQL----QFLID 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 414 NGkprhvLGYLQdflfhPKRAMTpvrALSGGERNRLLLAR-LFLKPSN-LLILDEPTNDLDVETLELLEELIDSY--QG- 488
Cdd:cd03238  74 VG-----LGYLT-----LGQKLS---TLSGGELQRVKLASeLFSEPPGtLFILDEPSTGLHQQDINQLLEVIKGLidLGn 140
                       170       180       190
                ....*....|....*....|....*....|...
gi 15830287 489 TVLLVSHDRQFVDntvTECWIFEGGGKIGRYVG 521
Cdd:cd03238 141 TVILIEHNLDVLS---SADWIIDFGPGSGKSGG 170
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
333-516 3.78e-06

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 48.81  E-value: 3.78e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  333 QLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKL---------EVAYFDQHRAELDPDK----- 398
Cdd:PRK10619  19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTinlvrdkdgQLKVADKNQLRLLRTRltmvf 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  399 ---------TVMDNLAEGKQEVM----VNGKPRHVLGYLQDFLFHPKRAMTPVRaLSGGERNRLLLARLFLKPSNLLILD 465
Cdd:PRK10619  99 qhfnlwshmTVLENVMEAPIQVLglskQEARERAVKYLAKVGIDERAQGKYPVH-LSGGQQQRVSIARALAMEPEVLLFD 177
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 15830287  466 EPTNDLD---VETLELLEELIDSYQGTVLLVSHDRQFVDNtVTECWIFEGGGKI 516
Cdd:PRK10619 178 EPTSALDpelVGEVLRIMQQLAEEGKTMVVVTHEMGFARH-VSSHVIFLHQGKI 230
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
134-226 3.88e-06

ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.


Pssm-ID: 213205 [Multi-domain]  Cd Length: 176  Bit Score: 47.70  E-value: 3.88e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 134 QLENRINEVLAQLGLDPNvaLSSLSGGWLRKAALGRALVSNPR--VLLLDEPTNHLDIETIDWLEGFLKTF---NGTIIF 208
Cdd:cd03238  67 QLQFLIDVGLGYLTLGQK--LSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLidlGNTVIL 144
                        90
                ....*....|....*...
gi 15830287 209 ISHDRSFIRNmATRIVDL 226
Cdd:cd03238 145 IEHNLDVLSS-ADWIIDF 161
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
331-473 4.50e-06

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 49.19  E-value: 4.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  331 GKQLVK---DFSAQVLRGDKIALIGPNGCGKTTLLKLML-------GQLQADSGRIHVGTKLEVA--------YFDQHRA 392
Cdd:PRK11308  24 PERLVKaldGVSFTLERGKTLAVVGESGCGKSTLARLLTmietptgGELYYQGQDLLKADPEAQKllrqkiqiVFQNPYG 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  393 ELDPDKTVMDNLAE--------GKQE-------VM--VNGKPRHVLGYLQDFlfhpkramtpvralSGGERNRLLLAR-L 454
Cdd:PRK11308 104 SLNPRKKVGQILEEpllintslSAAErrekalaMMakVGLRPEHYDRYPHMF--------------SGGQRQRIAIARaL 169
                        170
                 ....*....|....*....
gi 15830287  455 FLKPsNLLILDEPTNDLDV 473
Cdd:PRK11308 170 MLDP-DVVVADEPVSALDV 187
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
34-189 4.82e-06

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: 48.52  E-value: 4.82e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  34 LVGRNGAGKSTLMKILNREQGLDDGRiiyeqdlivarlQQDPPRnvegsvYDFVAE---GIEEQaEYLKRYHDISRLVMN 110
Cdd:cd03236  31 LVGPNGIGKSTALKILAGKLKPNLGK------------FDDPPD------WDEILDefrGSELQ-NYFTKLLEGDVKVIV 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 111 DPseKNLNELAKVQEQLDHHNLWQLENR--INEVLAQLGLDP--NVALSSLSGGWLRKAALGRALVSNPRVLLLDEPTNH 186
Cdd:cd03236  92 KP--QYVDLIPKAVKGKVGELLKKKDERgkLDELVDQLELRHvlDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSY 169

                ...
gi 15830287 187 LDI 189
Cdd:cd03236 170 LDI 172
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
39-231 5.83e-06

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 49.23  E-value: 5.83e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   39 GAGKSTLMKILNREQGLDDGRIIYEQDLIVARLQQDPPRNveGSVYdfvaegIEEQaeylkRYHDisRLVMNDPSEKN-- 116
Cdd:PRK10762 288 GAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLAN--GIVY------ISED-----RKRD--GLVLGMSVKENms 352
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  117 ---LNELAKVQEQLDHhnlwQLENRINEVLAQL------GLDPNVALssLSGGWLRKAALGRALVSNPRVLLLDEPTNHL 187
Cdd:PRK10762 353 ltaLRYFSRAGGSLKH----ADEQQAVSDFIRLfniktpSMEQAIGL--LSGGNQQKVAIARGLMTRPKVLILDEPTRGV 426
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 15830287  188 DI----ETIDWLEGFlKTFNGTIIFISHDRSFIRNMATRIVDLDRGKL 231
Cdd:PRK10762 427 DVgakkEIYQLINQF-KAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
cbiO PRK13642
energy-coupling factor transporter ATPase;
319-496 6.13e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 48.17  E-value: 6.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  319 VFEMEDVCYQVDGKQLVKDF---SAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV-GTKLEVAYFDQHRAEL 394
Cdd:PRK13642   4 ILEVENLVFKYEKESDVNQLngvSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIdGELLTAENVWNLRRKI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  395 -----DPDK-----TVMDNLAEGKQEvmvNGKPR-HVLGYLQDFLFHPK----RAMTPVRaLSGGERNRLLLARLFLKPS 459
Cdd:PRK13642  84 gmvfqNPDNqfvgaTVEDDVAFGMEN---QGIPReEMIKRVDEALLAVNmldfKTREPAR-LSGGQKQRVAVAGIIALRP 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 15830287  460 NLLILDEPTNDLDVETLELLEELI----DSYQGTVLLVSHD 496
Cdd:PRK13642 160 EIIILDESTSMLDPTGRQEIMRVIheikEKYQLTVLSITHD 200
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
35-220 6.89e-06

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 48.42  E-value: 6.89e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   35 VGRNGAGKSTLMKILNREQGLDDGRIIYE-QDLIVArlqqdpprnvegsvydfvaegiEEQAEYLKRyHDIsRLVMNDPS 113
Cdd:PRK11308  47 VGESGCGKSTLARLLTMIETPTGGELYYQgQDLLKA----------------------DPEAQKLLR-QKI-QIVFQNPY 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  114 eKNLNELAKVQEQLD-----HHNLWQLENR--INEVLAQLGLDPNVALS---SLSGGWLRKAALGRALVSNPRVLLLDEP 183
Cdd:PRK11308 103 -GSLNPRKKVGQILEeplliNTSLSAAERRekALAMMAKVGLRPEHYDRyphMFSGGQRQRIAIARALMLDPDVVVADEP 181
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 15830287  184 TNHLDI----ETIDWLEGFLKTFNGTIIFISHDRSFIRNMA 220
Cdd:PRK11308 182 VSALDVsvqaQVLNLMMDLQQELGLSYVFISHDLSVVEHIA 222
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
318-520 7.18e-06

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 47.85  E-value: 7.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  318 IVFEMED--VCYqvdGKQL-VKDFSAQVLRGDKIALIGPNGCGKTTLLKLM--LGQLqADSGRIhvgtKLEVAYFDQ--H 390
Cdd:PRK14243   9 TVLRTENlnVYY---GSFLaVKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrLNDL-IPGFRV----EGKVTFHGKnlY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  391 RAELDP-----------------DKTVMDNLAEGkqevmvngkPRhVLGYLQDFLFHPKRAM--------------TPVR 439
Cdd:PRK14243  81 APDVDPvevrrrigmvfqkpnpfPKSIYDNIAYG---------AR-INGYKGDMDELVERSLrqaalwdevkdklkQSGL 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  440 ALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELIDSY--QGTVLLVSHDRQFVDNTVTECWIF-----EG 512
Cdd:PRK14243 151 SLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELkeQYTIIIVTHNMQQAARVSDMTAFFnveltEG 230

                 ....*...
gi 15830287  513 GGKIGRYV 520
Cdd:PRK14243 231 GGRYGYLV 238
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
19-232 7.61e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 48.16  E-value: 7.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIiYEQDLIVARLQQD-PPRNVEGSVYD-----FVAEGIE 92
Cdd:PRK13633  26 LDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKV-YVDGLDTSDEENLwDIRNKAGMVFQnpdnqIVATIVE 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   93 EQAEYLKRYHDIsrlvmnDPSEKNlnelAKVQEQLDHHNLWQLENRinevlaqlgldpnvALSSLSGGWLRKAALGRALV 172
Cdd:PRK13633 105 EDVAFGPENLGI------PPEEIR----ERVDESLKKVGMYEYRRH--------------APHLLSGGQKQRVAIAGILA 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15830287  173 SNPRVLLLDEPTNHLD----IETIDWLEGFLKTFNGTIIFISHdrsFIRNM--ATRIVDLDRGKLV 232
Cdd:PRK13633 161 MRPECIIFDEPTAMLDpsgrREVVNTIKELNKKYGITIILITH---YMEEAveADRIIVMDSGKVV 223
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
326-472 8.01e-06

The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 48.89  E-value: 8.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   326 CYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLM----LGQLQADSGRIHVGTKLEV-------AYFDQHRAEL 394
Cdd:TIGR00955  32 CRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALafrsPKGVKGSGSVLLNGMPIDAkemraisAYVQQDDLFI 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   395 dPDKTVMDNL---AEGK-QEVMVNGKPRHVLGYLQDFLFHPKRAMT------PVRALSGGERNRLLLARLFLKPSNLLIL 464
Cdd:TIGR00955 112 -PTLTVREHLmfqAHLRmPRRVTKKEKRERVDEVLQALGLRKCANTrigvpgRVKGLSGGERKRLAFASELLTDPPLLFC 190

                  ....*...
gi 15830287   465 DEPTNDLD 472
Cdd:TIGR00955 191 DEPTSGLD 198
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
335-472 1.06e-05

ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213225 [Multi-domain]  Cd Length: 233  Bit Score: 47.19  E-value: 1.06e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 335 VKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV-GTKL-------------EVAYFDQHRAELDpDKTV 400
Cdd:cd03258  21 LKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVdGTDLtllsgkelrkarrRIGMIFQHFNLLS-SRTV 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 401 MDNLA-----EGKQEVMVNGKPRHVLGY--LQDflfhpKRAMTPvRALSGGERNRLLLAR-LFLKPSnLLILDEPTNDLD 472
Cdd:cd03258 100 FENVAlpleiAGVPKAEIEERVLELLELvgLED-----KADAYP-AQLSGGQKQRVGIARaLANNPK-VLLCDEATSALD 172
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
321-472 1.06e-05

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 47.39  E-value: 1.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  321 EMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLK------------LMLGQLQADSGRIHV-GTKLEVAY- 386
Cdd:PRK09493   3 EFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRcinkleeitsgdLIVDGLKVNDPKVDErLIRQEAGMv 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  387 FDQHraELDPDKTVMDNLAEGkqevmvngkPRHVLGY-----------LQDFLFHPKRAMTPVRALSGGERNRLLLAR-L 454
Cdd:PRK09493  83 FQQF--YLFPHLTALENVMFG---------PLRVRGAskeeaekqareLLAKVGLAERAHHYPSELSGGQQQRVAIARaL 151
                        170
                 ....*....|....*...
gi 15830287  455 FLKPsNLLILDEPTNDLD 472
Cdd:PRK09493 152 AVKP-KLMLFDEPTSALD 168
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
30-232 1.20e-05

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 47.23  E-value: 1.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   30 ERVCLVGRNGAGKSTLMKILNREQGLDDGRIIY----EQDLIVARLQQDPPRNVEGSVYDFV----AEGIEEQ------- 94
Cdd:PRK11701  33 EVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrdGQLRDLYALSEAERRRLLRTEWGFVhqhpRDGLRMQvsaggni 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   95 AEYL-----KRYHDISrlvmndpsEKNLNELAKVQEQLDhhnlwqlenRINEvlaqlglDPnvalSSLSGGWLRKAALGR 169
Cdd:PRK11701 113 GERLmavgaRHYGDIR--------ATAGDWLERVEIDAA---------RIDD-------LP----TTFSGGMQQRLQIAR 164
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15830287  170 ALVSNPRVLLLDEPTNHLDIET----IDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:PRK11701 165 NLVTHPRLVFMDEPTGGLDVSVqarlLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVV 231
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
333-468 2.08e-05

high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 46.41  E-value: 2.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  333 QLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVG----TKLEVAYFDQHRAELDPD-------KTVM 401
Cdd:PRK11614  19 QALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDgkdiTDWQTAKIMREAVAIVPEgrrvfsrMTVE 98
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15830287  402 DNLAEGKQEVMVNGKPRHVLGYLQDFLFHPKRAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPT 468
Cdd:PRK11614  99 ENLAMGGFFAERDQFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPS 165
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
1-232 2.27e-05

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 47.04  E-value: 2.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287    1 MSLISMHGAWLSFSD--APL--LDNAELHIEDNERVCLVGRNGAGKS-TLMKILnreqGLDD--GRIIYEQ------DLI 67
Cdd:PRK11022   1 MALLNVDKLSVHFGDesAPFraVDRISYSVKQGEVVGIVGESGSGKSvSSLAIM----GLIDypGRVMAEKlefngqDLQ 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   68 vaRLQQDPPRNVEGSvydfvaegieeqaeylkryhDISrLVMNDPSeKNLNELAKV----QEQLDHH---NLWQLENRIN 140
Cdd:PRK11022  77 --RISEKERRNLVGA--------------------EVA-MIFQDPM-TSLNPCYTVgfqiMEAIKVHqggNKKTRRQRAI 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  141 EVLAQLGL-DP----NVALSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDI----ETIDWLEGFLKTFNGTIIFISH 211
Cdd:PRK11022 133 DLLNQVGIpDPasrlDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVtiqaQIIELLLELQQKENMALVLITH 212
                        250       260
                 ....*....|....*....|.
gi 15830287  212 DRSFIRNMATRIVDLDRGKLV 232
Cdd:PRK11022 213 DLALVAEAAHKIIVMYAGQVV 233
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
315-471 2.44e-05

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 47.35  E-value: 2.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  315 SGKIVFEMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVG----TKLEVA----- 385
Cdd:PRK15439   7 TAPPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGgnpcARLTPAkahql 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  386 --YFDQHRAELDPDKTVMDNLAEGKQEVMVNGKPRHVLgyLQDFLFHPKRAMtPVRALSGGERNRLLLARLFLKPSNLLI 463
Cdd:PRK15439  87 giYLVPQEPLLFPNLSVKENILFGLPKRQASMQKMKQL--LAALGCQLDLDS-SAGSLEVADRQIVEILRGLMRDSRILI 163

                 ....*...
gi 15830287  464 LDEPTNDL 471
Cdd:PRK15439 164 LDEPTASL 171
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
14-216 2.58e-05

ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.


Pssm-ID: 213257 [Multi-domain]  Cd Length: 218  Bit Score: 45.78  E-value: 2.58e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  14 SDAPLLDNAELHIEDNERVCLVGRNGAGKSTLM-KILNREQGLDdGRIIYEQDLIVARLQQDPPRNVEGSVydfvaeGIE 92
Cdd:cd03290  12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQTLE-GKVHWSNKNESEPSFEATRSRNRYSV------AYA 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  93 EQAEYLkryhdisrlvMNDPSEKNLNELAKVQEQldhhnlwqlenRINEVLAQLGLDPNVAL-------------SSLSG 159
Cdd:cd03290  85 AQKPWL----------LNATVEENITFGSPFNKQ-----------RYKAVTDACSLQPDIDLlpfgdqteigergINLSG 143
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15830287 160 GWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWL--EGFLKTFNG---TIIFISHDRSFI 216
Cdd:cd03290 144 GQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLmqEGILKFLQDdkrTLVLVTHKLQYL 205
PTZ00243 PTZ00243
ABC transporter; Provisional
302-472 2.75e-05

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 47.47  E-value: 2.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   302 MGTAKMQVEEASRSGKIVfemEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRihVGTK 381
Cdd:PTZ00243  646 GHEATPTSERSAKTPKMK---TDDFFELEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGR--VWAE 720
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   382 LEVAYFDQHRAELdpDKTVMDNLaegkqevmvngkprhvlgylqdFLFHPKRA---MTPVRA------------------ 440
Cdd:PTZ00243  721 RSIAYVPQQAWIM--NATVRGNI----------------------LFFDEEDAarlADAVRVsqleadlaqlgggletei 776
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 15830287   441 ------LSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:PTZ00243  777 gekgvnLSGGQKARVSLARAVYANRDVYLLDDPLSALD 814
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
333-516 3.42e-05

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 46.23  E-value: 3.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  333 QLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIhvgtklEVAYFDQHraeldpDKTVMDNLAEGKQEVM 412
Cdd:PRK13651  21 KALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTI------EWIFKDEK------NKKKTKEKEKVLEKLV 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  413 VnGKPRH---------------VLGY----------LQDFLFHP-----------KRAMTPVR--------------ALS 442
Cdd:PRK13651  89 I-QKTRFkkikkikeirrrvgvVFQFaeyqlfeqtiEKDIIFGPvsmgvskeeakKRAAKYIElvgldesylqrspfELS 167
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15830287  443 GGERNRLLLARLFLKPSNLLILDEPTNDLD---VETLELLEELIDSYQGTVLLVSHDrqfVDNTV--TECWIFEGGGKI 516
Cdd:PRK13651 168 GGQKRRVALAGILAMEPDFLVFDEPTAGLDpqgVKEILEIFDNLNKQGKTIILVTHD---LDNVLewTKRTIFFKDGKI 243
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
17-191 3.67e-05

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


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 45.33  E-value: 3.67e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  17 PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNreqglddGRIIYEQDLIVARLQQDPPrNVEGSVYDFVAegieeqae 96
Cdd:COG2401  44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLA-------GALKGTPVAGCVDVPDNQF-GREASLIDAIG-------- 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  97 ylkryhdisrlvmndpseKNLNELAKVqeqldhhnlwqlenrinEVLAQLGLDPNVAL----SSLSGGWLRKAALGRALV 172
Cdd:COG2401 108 ------------------RKGDFKDAV-----------------ELLNAVGLSDAVLWlrrfKELSTGQKFRFRLALLLA 152
                       170
                ....*....|....*....
gi 15830287 173 SNPRVLLLDEPTNHLDIET 191
Cdd:COG2401 153 ERPKLLVIDEFCSHLDRQT 171
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
6-232 3.74e-05

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 46.65  E-value: 3.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287    6 MHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLI------------VARLQQ 73
Cdd:PRK10982   1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfksskealengISMVHQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   74 DPPRNVEGSVYDFVaegieeqaeYLKRYHDISRLVMNDpseKNLNELAKVQEQLDhhnlwqlenrinevlaqLGLDPNVA 153
Cdd:PRK10982  81 ELNLVLQRSVMDNM---------WLGRYPTKGMFVDQD---KMYRDTKAIFDELD-----------------IDIDPRAK 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  154 LSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGF---LKTFNGTIIFISHDRSFIRNMATRIVDLDRGK 230
Cdd:PRK10982 132 VATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHLFTIirkLKERGCGIVYISHKMEEIFQLCDEITILRDGQ 211

                 ..
gi 15830287  231 LV 232
Cdd:PRK10982 212 WI 213
PLN03211 PLN03211
ABC transporter G-25; Provisional
324-472 3.88e-05

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 46.80  E-value: 3.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  324 DVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADS--GRIHVGTK------LEVAYFDQHRAELD 395
Cdd:PLN03211  73 DETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRkptkqiLKRTGFVTQDDILY 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  396 PDKTVMDNLAEGKQEVMVNGKPRHVLGYLQDFLFhPKRAMTP----------VRALSGGERNRLLLARLFLKPSNLLILD 465
Cdd:PLN03211 153 PHLTVRETLVFCSLLRLPKSLTKQEKILVAESVI-SELGLTKcentiignsfIRGISGGERKRVSIAHEMLINPSLLILD 231

                 ....*..
gi 15830287  466 EPTNDLD 472
Cdd:PLN03211 232 EPTSGLD 238
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
335-496 4.73e-05

ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213261 [Multi-domain]  Cd Length: 269  Bit Score: 45.33  E-value: 4.73e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 335 VKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKlEVAYFD----------------QHRAeLDPDK 398
Cdd:cd03294  40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQ-DIAAMSrkelrelrrkkismvfQSFA-LLPHR 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 399 TVMDNLAEGKQEVMVNGKPRHvlgylqdflfhpKRAMTPVRA-------------LSGGERNRLLLAR-LFLKPSnLLIL 464
Cdd:cd03294 118 TVLENVAFGLEVQGVPRAERE------------ERAAEALELvglegwehkypdeLSGGMQQRVGLARaLAVDPD-ILLM 184
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 15830287 465 DEPTNDLDVETLELLEELI----DSYQGTVLLVSHD 496
Cdd:cd03294 185 DEAFSALDPLIRREMQDELlrlqAELQKTIVFITHD 220
GguA NF040905
sugar ABC transporter ATP-binding protein;
19-63 5.53e-05

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 45.94  E-value: 5.53e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 15830287   19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILN--REQGLDDGRIIYE 63
Cdd:NF040905  17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSgvYPHGSYEGEILFD 63
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
15-216 6.09e-05

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 44.70  E-value: 6.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   15 DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLIVARlqqdPPrnvegsvydfvaEGIEEQ 94
Cdd:PRK10247  19 DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTL----KP------------EIYRQQ 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   95 AEYLKRyhdiSRLVMNDPSEKNLN---ELAKVQEQldhhnlwqlENRINEVLAQLGLDPNV---ALSSLSGGWLRKAALG 168
Cdd:PRK10247  83 VSYCAQ----TPTLFGDTVYDNLIfpwQIRNQQPD---------PAIFLDDLERFALPDTIltkNIAELSGGEKQRISLI 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15830287  169 RALVSNPRVLLLDEPTNHLD----IETIDWLEGFLKTFNGTIIFISHDRSFI 216
Cdd:PRK10247 150 RNLQFMPKVLLLDEITSALDesnkHNVNEIIHRYVREQNIAVLWVTHDKDEI 201
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
333-472 7.09e-05

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 44.83  E-value: 7.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  333 QLVKDFSAQVLRGDKIALIGPNGCGKTTLLK-----LMLGQLQADSGRIH-------------VGTKLEVAYFDQHRAEL 394
Cdd:PRK14267  18 HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRtfnrlLELNEEARVEGEVRlfgrniyspdvdpIEVRREVGMVFQYPNPF 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  395 dPDKTVMDNLAEGkqeVMVNG--KPRHVLGYLQDFLFHPKRAMTPVR--------ALSGGERNRLLLAR-LFLKPsNLLI 463
Cdd:PRK14267  98 -PHLTIYDNVAIG---VKLNGlvKSKKELDERVEWALKKAALWDEVKdrlndypsNLSGGQRQRLVIARaLAMKP-KILL 172

                 ....*....
gi 15830287  464 LDEPTNDLD 472
Cdd:PRK14267 173 MDEPTANID 181
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
12-245 9.09e-05

ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444078 [Multi-domain]  Cd Length: 605  Bit Score: 45.58  E-value: 9.09e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  12 SFS---DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRI-IYEQDLivARLQQDPPRNVEGSV---- 83
Cdd:COG5265 364 SFGydpERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRIlIDGQDI--RDVTQASLRAAIGIVpqdt 441
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  84 ---YDFVAEGIeeqaeylkRYhdiSRLvmnDPSEKNLNELAKvqeqldhhnlwqlenrinevLAQL---------GLDPN 151
Cdd:COG5265 442 vlfNDTIAYNI--------AY---GRP---DASEEEVEAAAR--------------------AAQIhdfieslpdGYDTR 487
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 152 VA---LSsLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTF--NGTIIFISHDRSFIRNmATRIVDL 226
Cdd:COG5265 488 VGergLK-LSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVarGRTTLVIAHRLSTIVD-ADEILVL 565
                       250
                ....*....|....*....
gi 15830287 227 DRGKLVTYpGNYDQyLLEK 245
Cdd:COG5265 566 EAGRIVER-GTHAE-LLAQ 582
PRK13543 PRK13543
heme ABC exporter ATP-binding protein CcmA;
3-201 9.20e-05

heme ABC exporter ATP-binding protein CcmA;


Pssm-ID: 184129 [Multi-domain]  Cd Length: 214  Bit Score: 44.07  E-value: 9.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287    3 LISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIiyeqdlivaRLQQDPPRNVEGS 82
Cdd:PRK13543  11 LLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQI---------QIDGKTATRGDRS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   83 vyDFVA-----EGIEEQAEYLKRYHDISRLVMNDPSEKNLNELAKVqeqldhhnlwQLENRINEVLAQlgldpnvalssL 157
Cdd:PRK13543  82 --RFMAylghlPGLKADLSTLENLHFLCGLHGRRAKQMPGSALAIV----------GLAGYEDTLVRQ-----------L 138
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 15830287  158 SGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKT 201
Cdd:PRK13543 139 SAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISA 182
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
34-189 9.85e-05

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 44.40  E-value: 9.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   34 LVGRNGAGKSTLMKILNREQGLDDGRIIyeqdlivarlqqdpprnVEGSVYDFvaegieeqAEYLKRYHDIsRLVMNDPS 113
Cdd:PRK15112  44 IIGENGSGKSTLAKMLAGMIEPTSGELL-----------------IDDHPLHF--------GDYSYRSQRI-RMIFQDPS 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  114 eKNLNELAKVQEQLD-------HHNLWQLENRINEVLAQLGLDPNVAL---SSLSGGWLRKAALGRALVSNPRVLLLDEP 183
Cdd:PRK15112  98 -TSLNPRQRISQILDfplrlntDLEPEQREKQIIETLRQVGLLPDHASyypHMLAPGQKQRLGLARALILRPKVIIADEA 176

                 ....*.
gi 15830287  184 TNHLDI 189
Cdd:PRK15112 177 LASLDM 182
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
321-500 1.03e-04

leucine/isoleucine/valine transporter ATP-binding subunit; Provisional


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 44.21  E-value: 1.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  321 EMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI-------------HVGTKLEVAYF 387
Cdd:PRK11300   7 SVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIllrgqhieglpghQIARMGVVRTF 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  388 dQHrAELDPDKTVMDNLaegkqevMVnGKPRHV-LGYLQDFLFHP----------KRAMT-------------PVRALSG 443
Cdd:PRK11300  87 -QH-VRLFREMTVIENL-------LV-AQHQQLkTGLFSGLLKTPafrraesealDRAATwlervgllehanrQAGNLAY 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15830287  444 GERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELIDS----YQGTVLLVSHDRQFV 500
Cdd:PRK11300 157 GQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAElrneHNVTVLLIEHDMKLV 217
PvdE COG4615
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...
321-376 1.20e-04

ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];


Pssm-ID: 443659 [Multi-domain]  Cd Length: 547  Bit Score: 45.17  E-value: 1.20e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15830287 321 EMEDVCYQ---VDGKQL--VKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI 376
Cdd:COG4615 329 ELRGVTYRypgEDGDEGftLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEI 389
PRK15093 PRK15093
peptide ABC transporter ATP-binding protein SapD;
133-223 1.25e-04

peptide ABC transporter ATP-binding protein SapD;


Pssm-ID: 185049 [Multi-domain]  Cd Length: 330  Bit Score: 44.41  E-value: 1.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  133 WQLEN----RINEVLAQLGL-DPNVALSS----LSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIET----IDWLEGFL 199
Cdd:PRK15093 126 WQRFGwrkrRAIELLHRVGIkDHKDAMRSfpyeLTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTqaqiFRLLTRLN 205
                         90       100
                 ....*....|....*....|....
gi 15830287  200 KTFNGTIIFISHDRSFIRNMATRI 223
Cdd:PRK15093 206 QNNNTTILLISHDLQMLSQWADKI 229
ycf16 CHL00131
sulfate ABC transporter protein; Validated
317-473 1.32e-04

sulfate ABC transporter protein; Validated


Pssm-ID: 214372 [Multi-domain]  Cd Length: 252  Bit Score: 43.86  E-value: 1.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  317 KIVFEMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGqlqadsgriHVGTKL---EVAYFDQHRAE 393
Cdd:CHL00131   5 KPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG---------HPAYKIlegDILFKGESILD 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  394 LDPDK-------------------TVMDNL-----AEGKQEVMVNGKPRHVLGYLQDFLfhPKRAMTPV-------RALS 442
Cdd:CHL00131  76 LEPEErahlgiflafqypieipgvSNADFLrlaynSKRKFQGLPELDPLEFLEIINEKL--KLVGMDPSflsrnvnEGFS 153
                        170       180       190
                 ....*....|....*....|....*....|.
gi 15830287  443 GGERNRLLLARLFLKPSNLLILDEPTNDLDV 473
Cdd:CHL00131 154 GGEKKRNEILQMALLDSELAILDETDSGLDI 184
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
318-472 1.36e-04

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 44.24  E-value: 1.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  318 IVFEMEDVCYQVDG---KQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKLEVAYFDQhrael 394
Cdd:PRK13634   3 ITFQKVEHRYQYKTpfeRRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKN----- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  395 dpdktvmDNLAEGKQEV-MVNGKPRHVL---GYLQDFLFHP-----------KRAMTPVR--------------ALSGGE 445
Cdd:PRK13634  78 -------KKLKPLRKKVgIVFQFPEHQLfeeTVEKDICFGPmnfgvseedakQKAREMIElvglpeellarspfELSGGQ 150
                        170       180
                 ....*....|....*....|....*..
gi 15830287  446 RNRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:PRK13634 151 MRRVAIAGVLAMEPEVLVLDEPTAGLD 177
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
157-229 1.40e-04

sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 44.45  E-value: 1.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  157 LSGGWLRKAALGRALVSNPRVLLLDEPTNHLD--------IEtIDWLEGFLKTfngTIIFISHDRSFIRNMATRIVDLDR 228
Cdd:PRK11650 135 LSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDaklrvqmrLE-IQRLHRRLKT---TSLYVTHDQVEAMTLADRVVVMNG 210

                 .
gi 15830287  229 G 229
Cdd:PRK11650 211 G 211
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
4-267 1.54e-04

multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]


Pssm-ID: 188098 [Multi-domain]  Cd Length: 1522  Bit Score: 44.94  E-value: 1.54e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287      4 ISMHGAWLSF--SDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIiyeqdlivarlqqdpprNVEG 81
Cdd:TIGR00957  637 ITVHNATFTWarDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHV-----------------HMKG 699
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287     82 SV-YdfvaegIEEQAeylkryhdisrLVMNDPSEKNLnelakvqeqLDHHNLwqLENRINEVLAQLGLDPNVAL------ 154
Cdd:TIGR00957  700 SVaY------VPQQA-----------WIQNDSLRENI---------LFGKAL--NEKYYQQVLEACALLPDLEIlpsgdr 751
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287    155 -------SSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLD-------IETIDWLEGFLKtfNGTIIFISHDRSFIRNMA 220
Cdd:TIGR00957  752 teigekgVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDahvgkhiFEHVIGPEGVLK--NKTRILVTHGISYLPQVD 829
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 15830287    221 TRIVdLDRGKlVTYPGNYdQYLLEKEEALrveelqnAEFDRKLAQEE 267
Cdd:TIGR00957  830 VIIV-MSGGK-ISEMGSY-QELLQRDGAF-------AEFLRTYAPDE 866
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
18-213 1.64e-04

ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.


Pssm-ID: 213256 [Multi-domain]  Cd Length: 275  Bit Score: 44.07  E-value: 1.64e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  18 LLDNAELHIEDNERVCLVGRNGAGKSTLMKILNReqglddgrIIYEQDLIvarlqqdpprNVEGSVYDFVAegieeQAEY 97
Cdd:cd03289  19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLR--------LLNTEGDI----------QIDGVSWNSVP-----LQKW 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  98 LKRYHDISR--LVMNDPSEKNLN--------ELAKVQEQLDhhnlwqLENRINEVLAQLGLDPNVALSSLSGGWLRKAAL 167
Cdd:cd03289  76 RKAFGVIPQkvFIFSGTFRKNLDpygkwsdeEIWKVAEEVG------LKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCL 149
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 15830287 168 GRALVSNPRVLLLDEPTNHLDIETIDWLEGFLK-TFNGTIIFISHDR 213
Cdd:cd03289 150 ARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKqAFADCTVILSEHR 196
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
1-212 1.97e-04

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 43.60  E-value: 1.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287    1 MSLISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLIvarlqqdpPRNVE 80
Cdd:PRK11831   5 ANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENI--------PAMSR 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   81 GSVYdfvaegieeqaEYLKRyhdISRLVMNDPSEKNLNELAKVQEQLDHHNlwQLENRI--NEVLAQL---GLDPNVAL- 154
Cdd:PRK11831  77 SRLY-----------TVRKR---MSMLFQSGALFTDMNVFDNVAYPLREHT--QLPAPLlhSTVMMKLeavGLRGAAKLm 140
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15830287  155 -SSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFNG----TIIFISHD 212
Cdd:PRK11831 141 pSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSalgvTCVVVSHD 203
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
166-219 2.16e-04

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: 42.98  E-value: 2.16e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15830287 166 ALGRALVSNPRVLLLDEPTNHLDIETIDW-----LEGFLKTFNGTIIFISHDRSFIRNM 219
Cdd:cd03240 131 ALAETFGSNCGILALDEPTTNLDEENIEEslaeiIEERKSQKNFQLIVITHDEELVDAA 189
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
437-542 2.29e-04

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 44.43  E-value: 2.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   437 PVRALSGGERNRLLLARLFLKPS---NLLILDEPTNDLDVETLELLEELIDS--YQG-TVLLVSHDRQFVD--NTVTECW 508
Cdd:PRK00635  806 PLSSLSGGEIQRLKLAYELLAPSkkpTLYVLDEPTTGLHTHDIKALIYVLQSltHQGhTVVIIEHNMHVVKvaDYVLELG 885
                          90       100       110
                  ....*....|....*....|....*....|....
gi 15830287   509 IfEGGGKigryvGGYHDARGQQEQYVALKQPAVK 542
Cdd:PRK00635  886 P-EGGNL-----GGYLLASCSPEELIHLHTPTAK 913
3a01203 TIGR00954
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...
331-495 2.81e-04

Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 273360 [Multi-domain]  Cd Length: 659  Bit Score: 43.97  E-value: 2.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   331 GKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKLEVAYFDQH----------------RAEL 394
Cdd:TIGR00954 464 GDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVPQRpymtlgtlrdqiiypdSSED 543
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   395 DPDKTVMDNLAEgkqEVMVNGKPRHVLgylqdflfhpKRAM--TPVR----ALSGGERNRLLLARLFLKPSNLLILDEPT 468
Cdd:TIGR00954 544 MKRRGLSDKDLE---QILDNVQLTHIL----------EREGgwSAVQdwmdVLSGGEKQRIAMARLFYHKPQFAILDECT 610
                         170       180
                  ....*....|....*....|....*..
gi 15830287   469 NDLDVETLELLEELIDSYQGTVLLVSH 495
Cdd:TIGR00954 611 SAVSVDVEGYMYRLCREFGITLFSVSH 637
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
315-472 2.81e-04

SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 43.94  E-value: 2.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  315 SGKIvfEMEDVCYQV-DGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTK----LEVAYFDQ 389
Cdd:PRK10790 338 SGRI--DIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRplssLSHSVLRQ 415
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  390 HRAELDPDKTVM-----DNLAEGKQevMVNGKPRHVLGYLQdfLFHPKRAM-----TPV----RALSGGERNRLLLARLF 455
Cdd:PRK10790 416 GVAMVQQDPVVLadtflANVTLGRD--ISEEQVWQALETVQ--LAELARSLpdglyTPLgeqgNNLSVGQKQLLALARVL 491
                        170
                 ....*....|....*..
gi 15830287  456 LKPSNLLILDEPTNDLD 472
Cdd:PRK10790 492 VQTPQILILDEATANID 508
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
24-242 3.16e-04

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 42.65  E-value: 3.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   24 LHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRI-IYEQDLIVARLQQDPprnvegsvydfvaegieeqaeylkryh 102
Cdd:PRK10771  20 LTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLtLNGQDHTTTPPSRRP--------------------------- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  103 dISRLVmndpSEKNLnelakvqeqLDHHNLWQlenRINevlaqLGLDPNVALSS-------------------------L 157
Cdd:PRK10771  73 -VSMLF----QENNL---------FSHLTVAQ---NIG-----LGLNPGLKLNAaqreklhaiarqmgiedllarlpgqL 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  158 SGGWLRKAALGRALVSNPRVLLLDEPTNHLD----IETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKLVt 233
Cdd:PRK10771 131 SGGQRQRVALARCLVREQPILLLDEPFSALDpalrQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIA- 209

                 ....*....
gi 15830287  234 YPGNYDQYL 242
Cdd:PRK10771 210 WDGPTDELL 218
PRK13541 PRK13541
cytochrome c biogenesis protein CcmA; Provisional
348-495 3.84e-04

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184128 [Multi-domain]  Cd Length: 195  Bit Score: 42.17  E-value: 3.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  348 IALI-GPNGCGKTTLLKLMLGQLQADSGRIHVG----TKLEVAY--FDQHRAELDPDKTVMDNL---AEGKQEVMVNGKP 417
Cdd:PRK13541  28 ITYIkGANGCGKSSLLRMIAGIMQPSSGNIYYKncniNNIAKPYctYIGHNLGLKLEMTVFENLkfwSEIYNSAETLYAA 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  418 RHVLGyLQDFLfhpkraMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELI---DSYQGTVLLVS 494
Cdd:PRK13541 108 IHYFK-LHDLL------DEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIvmkANSGGIVLLSS 180

                 .
gi 15830287  495 H 495
Cdd:PRK13541 181 H 181
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
339-472 3.88e-04

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 42.59  E-value: 3.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  339 SAQVLRGDKI--------ALIGPNGCGKTTLLKLM--LGQLQAD---SGRIHVGT----KLEVAYFdQHRAELD------ 395
Cdd:PRK14247  15 QVEVLDGVNLeipdntitALMGPSGSGKSTLLRVFnrLIELYPEarvSGEVYLDGqdifKMDVIEL-RRRVQMVfqipnp 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  396 -PDKTVMDNLAEG-KQEVMVNGKP------RHVLGYLQDFLFHPKRAMTPVRALSGGERNRLLLARLFLKPSNLLILDEP 467
Cdd:PRK14247  94 iPNLSIFENVALGlKLNRLVKSKKelqervRWALEKAQLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEP 173

                 ....*
gi 15830287  468 TNDLD 472
Cdd:PRK14247 174 TANLD 178
hmuV PRK13547
heme ABC transporter ATP-binding protein;
330-473 3.98e-04

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 42.51  E-value: 3.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  330 DGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKLEVAYFDQHRAELDPD-----KTVMDNL 404
Cdd:PRK13547  12 RHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGAPRGARVTGDVTLNGEPLAAIDAPrlarlRAVLPQA 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  405 AE-----GKQEVMVNGKPRHVL---------GYLQDFLFHPKRAMTPVR----ALSGGERNRLLLARLFLK--------- 457
Cdd:PRK13547  92 AQpafafSAREIVLLGRYPHARragalthrdGEIAWQALALAGATALVGrdvtTLSGGELARVQFARVLAQlwpphdaaq 171
                        170
                 ....*....|....*.
gi 15830287  458 PSNLLILDEPTNDLDV 473
Cdd:PRK13547 172 PPRYLLLDEPTAALDL 187
PLN03130 PLN03130
ABC transporter C family member; Provisional
345-472 4.19e-04

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 43.57  E-value: 4.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   345 GDKIALIGPNGCGKTTLLKLMLGQLQADSGRiHVGTKLEVAYFDQhrAELDPDKTVMDNLAEGKQ-EVMVNGKPRHVLGY 423
Cdd:PLN03130  643 GSLVAIVGSTGEGKTSLISAMLGELPPRSDA-SVVIRGTVAYVPQ--VSWIFNATVRDNILFGSPfDPERYERAIDVTAL 719
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 15830287   424 LQDFLFHPKRAMTPV--RA--LSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:PLN03130  720 QHDLDLLPGGDLTEIgeRGvnISGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772
cbiO PRK13645
energy-coupling factor transporter ATPase;
350-472 4.64e-04

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 42.69  E-value: 4.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  350 LIGPNGCGKTTLLKLMLGQLQADSGRIHVGT----------------KLEVAY-FDQHRAELDPDKTVMD------NLAE 406
Cdd:PRK13645  42 VIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipanlkkikevkrlRKEIGLvFQFPEYQLFQETIEKDiafgpvNLGE 121
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15830287  407 GKQEVMvnGKPRHVLGYLQDFLFHPKRamTPVRaLSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:PRK13645 122 NKQEAY--KKVPELLKLVQLPEDYVKR--SPFE-LSGGQKRRVALAGIIAMDGNTLVLDEPTGGLD 182
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
158-212 4.75e-04

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 42.79  E-value: 4.75e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 15830287  158 SGGWLRKAALGRALVSNPRVLLLDEPTNHLDI----ETIDWLEGFLKTFNGTIIFISHD 212
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVtvqaQIMTLLNELKREFNTAIIMITHD 221
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
143-230 6.25e-04

leucine/isoleucine/valine transporter ATP-binding subunit; Provisional


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 41.90  E-value: 6.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  143 LAQLGLDP--NVALSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLD-IETID---WLEGFLKTFNGTIIFISHDRSFI 216
Cdd:PRK11300 138 LERVGLLEhaNRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNpKETKEldeLIAELRNEHNVTVLLIEHDMKLV 217
                         90
                 ....*....|....
gi 15830287  217 RNMATRIVDLDRGK 230
Cdd:PRK11300 218 MGISDRIYVVNQGT 231
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
136-232 6.43e-04

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 41.99  E-value: 6.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  136 ENRINEVLAQLGL-DPNVALSS----LSGGWLRKAALGRALVSNPRVLLLDEPTNHLDI----ETIDWLEGFLKTFNGTI 206
Cdd:PRK10418 115 DATLTAALEAVGLeNAARVLKLypfeMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVvaqaRILDLLESIVQKRALGM 194
                         90       100
                 ....*....|....*....|....*.
gi 15830287  207 IFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:PRK10418 195 LLVTHDMGVVARLADDVAVMSHGRIV 220
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
138-261 6.90e-04

oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 42.41  E-value: 6.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  138 RINEVLAQLGLDPNV--ALSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETID--WLEGFLKTFNG-TIIFISHD 212
Cdd:NF000106 124 RADELLERFSLTEAAgrAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNevWDEVRSMVRDGaTVLLTTQY 203
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 15830287  213 RSFIRNMATRIVDLDRGKLVTyPGNYDQYLLE-KEEALRVEELQNAEFDR 261
Cdd:NF000106 204 MEEAEQLAHELTVIDRGRVIA-DGKVDELKTKvGGRTLQIRPAHAAELDR 252
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
349-473 7.04e-04

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 42.17  E-value: 7.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  349 ALIGPNGCGKTTLLKLMLGQLQADSGRIHVGT---------------KLEVAY-FDQHRaeLDPDKTVMDNLAEGKQEVM 412
Cdd:PRK11144  28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlfdaekgiclppeKRRIGYvFQDAR--LFPHYKVRGNLRYGMAKSM 105
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15830287  413 VNGKPRHV--LGyLQDFLfhpKRamTPvRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDV 473
Cdd:PRK11144 106 VAQFDKIValLG-IEPLL---DR--YP-GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDL 161
AAA_21 pfam13304
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ...
93-217 8.17e-04

AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.


Pssm-ID: 433102 [Multi-domain]  Cd Length: 303  Bit Score: 41.99  E-value: 8.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287    93 EQAEYLKRYHDISRLVMNDPS--EKNLNELAKVQEQLDHHNLWQLENrinevlaqlGLDPNVALSSLSGGWLRKAALGRA 170
Cdd:pfam13304 180 DLKELLQRLVRGLKLADLNLSdlGEGIEKSLLVDDRLRERGLILLEN---------GGGGELPAFELSDGTKRLLALLAA 250
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 15830287   171 LVS---NPRVLLLDEPTNHLDIETIDWLEGFLK---TFNGTIIFISHDRSFIR 217
Cdd:pfam13304 251 LLSalpKGGLLLIDEPESGLHPKLLRRLLELLKelsRNGAQLILTTHSPLLLD 303
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
305-495 8.80e-04

multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]


Pssm-ID: 188098 [Multi-domain]  Cd Length: 1522  Bit Score: 42.63  E-value: 8.80e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287    305 AKMQVEEAS------RSGKIVFEMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV 378
Cdd:TIGR00957 1266 APWQIQETAppsgwpPRGRVEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIII 1345
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287    379 gTKLEVAYFDQH--------------------RAELDPDKTVMDnlaegkQEVMVNGKPRHVLGY---LQDFLFHpkRAM 435
Cdd:TIGR00957 1346 -DGLNIAKIGLHdlrfkitiipqdpvlfsgslRMNLDPFSQYSD------EEVWWALELAHLKTFvsaLPDKLDH--ECA 1416
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15830287    436 TPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELIDSY--QGTVLLVSH 495
Cdd:TIGR00957 1417 EGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQfeDCTVLTIAH 1478
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
14-268 1.12e-03

SmdA family multidrug ABC transporter permease/ATP-binding protein;


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 42.01  E-value: 1.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   14 SDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYeQDLIVARLQQDPPRNVEGSV-------YDF 86
Cdd:PRK10789 326 TDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRF-HDIPLTKLQLDSWRSRLAVVsqtpflfSDT 404
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   87 VAEGI--------EEQAEYLKRyhdisrlvmndpseknlneLAKVQEqlDHHNLWQlenrinevlaqlGLDPNVALSS-- 156
Cdd:PRK10789 405 VANNIalgrpdatQQEIEHVAR-------------------LASVHD--DILRLPQ------------GYDTEVGERGvm 451
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  157 LSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTF--NGTIIFISHDRSFIRNmATRIVDLDRG----- 229
Cdd:PRK10789 452 LSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWgeGRTVIISAHRLSALTE-ASEILVMQHGhiaqr 530
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 15830287  230 ----KLVTYPGNY-DQYllekeealRVEELQNAEFDRKLAQEEV 268
Cdd:PRK10789 531 gnhdQLAQQSGWYrDMY--------RYQQLEAALDDAPEIREEA 566
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
335-496 1.21e-03

proline/glycine betaine ABC transporter ATP-binding protein ProV;


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 41.56  E-value: 1.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  335 VKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVG----TKLEVAYFDQHRAE----------LDPDKTV 400
Cdd:PRK10070  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDgvdiAKISDAELREVRRKkiamvfqsfaLMPHMTV 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  401 MDNLAEGKQEVMVNGKPRH--VLGYLQDFLFHPKRAMTPvRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLEL 478
Cdd:PRK10070 124 LDNTAFGMELAGINAEERRekALDALRQVGLENYAHSYP-DELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
                        170       180
                 ....*....|....*....|..
gi 15830287  479 LEELI----DSYQGTVLLVSHD 496
Cdd:PRK10070 203 MQDELvklqAKHQRTIVFISHD 224
COG3950 COG3950
Predicted ATP-binding protein involved in virulence [General function prediction only];
19-219 1.50e-03

Predicted ATP-binding protein involved in virulence [General function prediction only];


Pssm-ID: 443150 [Multi-domain]  Cd Length: 276  Bit Score: 40.75  E-value: 1.50e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  19 LDNAELHIEDNERV-CLVGRNGAGKSTLMKILN-----REQGLDDGRIiyeQDLIVARLQQDPPRNV------EGSVYDF 86
Cdd:COG3950  14 FEDLEIDFDNPPRLtVLVGENGSGKTTLLEAIAlalsgLLSRLDDVKF---RKLLIRNGEFGDSAKLilyygtSRLLLDG 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  87 VAEGIEEQ-AEYLKRYHDISRLVMNDPSEKNLNE-LAKVQEQLDHHNLWQLENRINEV----------LAQLGLDPN--- 151
Cdd:COG3950  91 PLKKLERLkEEYFSRLDGYDSLLDEDSNLREFLEwLREYLEDLENKLSDELDEKLEAVrealnkllpdFKDIRIDRDpgr 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287 152 ----------VALSSLSGG--------------WLRKAALGRALVSNPRVLLLDEPTNHLDIEtidW----LEGFLKTF- 202
Cdd:COG3950 171 lvildkngeeLPLNQLSDGersllalvgdlarrLAELNPALENPLEGEGIVLIDEIDLHLHPK---WqrriLPDLRKIFp 247
                       250
                ....*....|....*..
gi 15830287 203 NGTIIFISHDRSFIRNM 219
Cdd:COG3950 248 NIQFIVTTHSPLILSSL 264
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
153-189 1.52e-03

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 41.64  E-value: 1.52e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 15830287  153 ALSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDI 189
Cdd:PRK10982 388 QIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDV 424
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
437-532 1.54e-03

excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273184 [Multi-domain]  Cd Length: 925  Bit Score: 41.54  E-value: 1.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   437 PVRALSGGERNRLLLARLFLKPSN---LLILDEPTNDL---DVETLELLEELIDSYQGTVLLVSHDrqfVDNTVTECWIF 510
Cdd:TIGR00630 826 PATTLSGGEAQRIKLAKELSKRSTgrtLYILDEPTTGLhfdDIKKLLEVLQRLVDKGNTVVVIEHN---LDVIKTADYII 902
                          90       100
                  ....*....|....*....|....*.
gi 15830287   511 ----EGGGKigryvGGYHDARGQQEQ 532
Cdd:TIGR00630 903 dlgpEGGDG-----GGTVVASGTPEE 923
cbiO PRK13641
energy-coupling factor transporter ATPase;
332-585 2.10e-03

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 40.58  E-value: 2.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  332 KQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKLEVAyfdqhraeldpdKTVMDNLAEGKQEV 411
Cdd:PRK13641  20 KKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITP------------ETGNKNLKKLRKKV 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  412 -MVNGKPRHVL---GYLQDFLFHPK-----------RAMTPVRA--------------LSGGERNRLLLARLFLKPSNLL 462
Cdd:PRK13641  88 sLVFQFPEAQLfenTVLKDVEFGPKnfgfsedeakeKALKWLKKvglsedliskspfeLSGGQMRRVAIAGVMAYEPEIL 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  463 ILDEPTNDLDVETLELLEELIDSYQG---TVLLVSHDRQFVDNTVTECWIFEGGGKIGryvggyHDArgqqEQYVALKQP 539
Cdd:PRK13641 168 CLDEPAAGLDPEGRKEMMQLFKDYQKaghTVILVTHNMDDVAEYADDVLVLEHGKLIK------HAS----PKEIFSDKE 237
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 15830287  540 AVKKN--EEPAAPKaetVKRSSSKLSYKLQRELEQLPQLLEDLEAKLE 585
Cdd:PRK13641 238 WLKKHylDEPATSR---FASKLEKGGFKFSEMPLTIDELVDGIKNNLK 282
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
349-496 2.70e-03

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 40.08  E-value: 2.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  349 ALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKL----------EVAYFDQHRAEL--DPDK---TVMDNLAEG------ 407
Cdd:PRK14271  51 SLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLlggrsifnyrDVLEFRRRVGMLfqRPNPfpmSIMDNVLAGvrahkl 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  408 --KQEVMVNGKPRHVLGYLQDFLfHPKRAMTPVRaLSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELIDS 485
Cdd:PRK14271 131 vpRKEFRGVAQARLTEVGLWDAV-KDRLSDSPFR-LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRS 208
                        170
                 ....*....|...
gi 15830287  486 YQG--TVLLVSHD 496
Cdd:PRK14271 209 LADrlTVIIVTHN 221
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
345-472 2.77e-03

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: 41.15  E-value: 2.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287    345 GDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHV-GTKLEVAYFDQHRAE-LDPDKTVMDNLAEGKQEVMVNGKPRHV-- 420
Cdd:TIGR01257 1965 GECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVaGKSILTNISDVHQNMgYCPQFDAIDDLLTGREHLYLYARLRGVpa 2044
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15830287    421 ----------LGYLQDFLFHPKRAMTpvraLSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:TIGR01257 2045 eeiekvanwsIQSLGLSLYADRLAGT----YSGGNKRKLSTAIALIGCPPLVLLDEPTTGMD 2102
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
322-471 2.88e-03

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 40.48  E-value: 2.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  322 MEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKlEVAYFDQHRA--------- 392
Cdd:PRK10982   1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGK-EIDFKSSKEAlengismvh 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  393 -ELD--PDKTVMDNLAEGKQevmvngkPRHVLGYLQDFLFHPKRAM-----------TPVRALSGGERNRLLLARLFLKP 458
Cdd:PRK10982  80 qELNlvLQRSVMDNMWLGRY-------PTKGMFVDQDKMYRDTKAIfdeldididprAKVATLSVSQMQMIEIAKAFSYN 152
                        170
                 ....*....|...
gi 15830287  459 SNLLILDEPTNDL 471
Cdd:PRK10982 153 AKIVIMDEPTSSL 165
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
319-498 3.35e-03

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 39.76  E-value: 3.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  319 VFEMEDVCYQVDGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLM--LGQLQAD---SGRI-HVGTKLEVAYFD--QH 390
Cdd:PRK14239   5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIvYNGHNIYSPRTDtvDL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  391 RAEL-----DPDK---TVMDNLAEGkqeVMVNG-KPRHVLGYLQDFLFHPKRAMTPVR--------ALSGGERNRLLLAR 453
Cdd:PRK14239  85 RKEIgmvfqQPNPfpmSIYENVVYG---LRLKGiKDKQVLDEAVEKSLKGASIWDEVKdrlhdsalGLSGGQQQRVCIAR 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 15830287  454 LFLKPSNLLILDEPTNDLDVETLELLEELI----DSYqgTVLLVSHDRQ 498
Cdd:PRK14239 162 VLATSPKIILLDEPTSALDPISAGKIEETLlglkDDY--TMLLVTRSMQ 208
EutP COG4917
Ethanolamine utilization protein EutP, contains a P-loop NTPase domain [Amino acid transport ...
347-368 3.92e-03

Ethanolamine utilization protein EutP, contains a P-loop NTPase domain [Amino acid transport and metabolism];


Pssm-ID: 443945 [Multi-domain]  Cd Length: 145  Bit Score: 38.24  E-value: 3.92e-03
                        10        20
                ....*....|....*....|..
gi 15830287 347 KIALIGPNGCGKTTLLKLMLGQ 368
Cdd:COG4917   3 RIMLIGRSGAGKTTLTQALNGE 24
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
439-543 4.46e-03

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 40.40  E-value: 4.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   439 RALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELI----DSYQGTVLLVSHDRQFVDNTvTECWIFEGGG 514
Cdd:PTZ00265 1357 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIvdikDKADKTIITIAHRIASIKRS-DKIVVFNNPD 1435
                          90       100
                  ....*....|....*....|....*....
gi 15830287   515 KIGRYVggyhDARGQQEQYVALKQPAVKK 543
Cdd:PTZ00265 1436 RTGSFV----QAHGTHEELLSVQDGVYKK 1460
cbiO PRK13649
energy-coupling factor transporter ATPase;
337-513 5.08e-03

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 39.34  E-value: 5.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  337 DFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKLEVAyfDQHRAELDP-----------------DKT 399
Cdd:PRK13649  25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITS--TSKNKDIKQirkkvglvfqfpesqlfEET 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287  400 VMDNLAEGKQEVMVNGKPRHVLGY-------LQDFLFHpkraMTPVRaLSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:PRK13649 103 VLKDVAFGPQNFGVSQEEAEALAReklalvgISESLFE----KNPFE-LSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 15830287  473 VETLELLEELIDS-YQG--TVLLVSHDRQFVDNTVTECWIFEGG 513
Cdd:PRK13649 178 PKGRKELMTLFKKlHQSgmTIVLVTHLMDDVANYADFVYVLEKG 221
cbiO PRK13642
energy-coupling factor transporter ATPase;
14-212 6.54e-03

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 38.92  E-value: 6.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   14 SDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILN----REQGL---DDGRIIYEQDLIVAR----LQQDPPRNVEG- 81
Cdd:PRK13642  18 SDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDglfeEFEGKvkiDGELLTAENVWNLRRkigmVFQNPDNQFVGa 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830287   82 SVYDFVAEGIEEQAeylkryhdISRLVMndpseknlneLAKVQEQLDHHNLWQLENRinevlaqlglDPnvalSSLSGGW 161
Cdd:PRK13642  98 TVEDDVAFGMENQG--------IPREEM----------IKRVDEALLAVNMLDFKTR----------EP----ARLSGGQ 145
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 15830287  162 LRKAALGRALVSNPRVLLLDEPTNHLD----IETIDWLEGFLKTFNGTIIFISHD 212
Cdd:PRK13642 146 KQRVAVAGIIALRPEIIILDESTSMLDptgrQEIMRVIHEIKEKYQLTVLSITHD 200
COG3950 COG3950
Predicted ATP-binding protein involved in virulence [General function prediction only];
350-406 7.76e-03

Predicted ATP-binding protein involved in virulence [General function prediction only];


Pssm-ID: 443150 [Multi-domain]  Cd Length: 276  Bit Score: 38.83  E-value: 7.76e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15830287 350 LIGPNGCGKTTLLKLMLGQLQADSGR----------IHVGTKLE----VAYFDQHRAELDPDKTVMDNLAE 406
Cdd:COG3950  30 LVGENGSGKTTLLEAIALALSGLLSRlddvkfrkllIRNGEFGDsaklILYYGTSRLLLDGPLKKLERLKE 100
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
156-190 8.70e-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: 37.55  E-value: 8.70e-03
                        10        20        30
                ....*....|....*....|....*....|....*
gi 15830287 156 SLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIE 190
Cdd:cd03222  71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIE 105
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
13-66 9.07e-03

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127 [Multi-domain]  Cd Length: 200  Bit Score: 38.01  E-value: 9.07e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15830287   13 FSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMK----ILNREQG--------LDDGRIIYEQDL 66
Cdd:PRK13540  11 YHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKliagLLNPEKGeilferqsIKKDLCTYQKQL 76
 
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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