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Conserved domains on  [gi|1411607396|emb|SPT67533|]
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ABC transporter ATP-binding protein [Aeromonas salmonicida]

Protein Classification

ATP-binding cassette domain-containing protein( domain architecture ID 1001393)

ATP-binding cassette domain-containing protein, similar to ATP-binding protein Uup, may contain the C-terminal domain (CTD) found in ABC transporters, which aids in DNA binding

CATH:  3.40.50.300
EC:  7.5.2.-
Gene Ontology:  GO:0005524|GO:0016887
PubMed:  11421269

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK11147 super family cl35997
ABC transporter ATPase component; Reviewed
1-633 0e+00

ABC transporter ATPase component; Reviewed


The actual alignment was detected with superfamily member PRK11147:

Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 1106.17  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   1 MALLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMVQQQDLKVTRLEQDPPASSD 80
Cdd:PRK11147    1 MSLISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQDPPRNVE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  81 LTVFDYTAEGLAGVGELLKKYHHISMELAHDPSDANIRIMSDLQEQLDYQNGWQFETRISQVLTLLNLDPDATLDSLSGG 160
Cdd:PRK11147   81 GTVYDFVAEGIEEQAEYLKRYHDISHLVETDPSEKNLNELAKLQEQLDHHNLWQLENRINEVLAQLGLDPDAALSSLSGG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 161 WLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVITSWPGNYDE 240
Cdd:PRK11147  161 WLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGNYDQ 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 241 YLQGKEEALRVEELQHAEFDRKLAQEEVWVRQGIKARRTRNEGRVRALEAMRMERSQRRELQGKAKLQMDDVNRSGKLVF 320
Cdd:PRK11147  241 YLLEKEEALRVEELQNAEFDRKLAQEEVWIRQGIKARRTRNEGRVRALKALRRERSERREVMGTAKMQVEEASRSGKIVF 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKGGTKLEVAYFDQYRDQLDPEQTV 400
Cdd:PRK11147  321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFDQHRAELDPEKTV 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 401 MDNVGEGKQEVMVRGRSRHILGYLQDFLFEPKRARTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVETLELLE 480
Cdd:PRK11147  401 MDNLAEGKQEVMVNGRPRHVLGYLQDFLFHPKRAMTPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLE 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 481 ELLADYPGTLLLVSHDRRFIDNTVTGCWLFEGDGRISDYVGGYADMMATRAqQSTQLAAKAAQVKTPEPVAVASPAASKV 560
Cdd:PRK11147  481 ELLDSYQGTVLLVSHDRQFVDNTVTECWIFEGNGKIGRYVGGYHDARQQQA-QYLALKQPAVKKKEEAAAPKAETVKRSS 559
                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1411607396 561 KKLSYKLQLELDNLPARLEQLETELNALQAEVNHPGFFALPSDQTQLKLDALNAAEAALEQAFSRWEELEALK 633
Cdd:PRK11147  560 KKLSYKLQRELEQLPQLLEDLEAEIEALQAQVADADFFSQPHEQTQKVLADLADAEQELEVAFERWEELEALK 632
 
Name Accession Description Interval E-value
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
1-633 0e+00

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 1106.17  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   1 MALLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMVQQQDLKVTRLEQDPPASSD 80
Cdd:PRK11147    1 MSLISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQDPPRNVE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  81 LTVFDYTAEGLAGVGELLKKYHHISMELAHDPSDANIRIMSDLQEQLDYQNGWQFETRISQVLTLLNLDPDATLDSLSGG 160
Cdd:PRK11147   81 GTVYDFVAEGIEEQAEYLKRYHDISHLVETDPSEKNLNELAKLQEQLDHHNLWQLENRINEVLAQLGLDPDAALSSLSGG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 161 WLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVITSWPGNYDE 240
Cdd:PRK11147  161 WLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGNYDQ 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 241 YLQGKEEALRVEELQHAEFDRKLAQEEVWVRQGIKARRTRNEGRVRALEAMRMERSQRRELQGKAKLQMDDVNRSGKLVF 320
Cdd:PRK11147  241 YLLEKEEALRVEELQNAEFDRKLAQEEVWIRQGIKARRTRNEGRVRALKALRRERSERREVMGTAKMQVEEASRSGKIVF 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKGGTKLEVAYFDQYRDQLDPEQTV 400
Cdd:PRK11147  321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFDQHRAELDPEKTV 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 401 MDNVGEGKQEVMVRGRSRHILGYLQDFLFEPKRARTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVETLELLE 480
Cdd:PRK11147  401 MDNLAEGKQEVMVNGRPRHVLGYLQDFLFHPKRAMTPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLE 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 481 ELLADYPGTLLLVSHDRRFIDNTVTGCWLFEGDGRISDYVGGYADMMATRAqQSTQLAAKAAQVKTPEPVAVASPAASKV 560
Cdd:PRK11147  481 ELLDSYQGTVLLVSHDRQFVDNTVTECWIFEGNGKIGRYVGGYHDARQQQA-QYLALKQPAVKKKEEAAAPKAETVKRSS 559
                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1411607396 561 KKLSYKLQLELDNLPARLEQLETELNALQAEVNHPGFFALPSDQTQLKLDALNAAEAALEQAFSRWEELEALK 633
Cdd:PRK11147  560 KKLSYKLQRELEQLPQLLEDLEAEIEALQAQVADADFFSQPHEQTQKVLADLADAEQELEVAFERWEELEALK 632
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
6-528 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: 687.57  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   6 LHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMVQQQDLKVTRLEQDPPASSDLTVFD 85
Cdd:COG0488     1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPLDDDLTVLD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  86 YTAEGLAGVGELLKKYHHISMELAHdpSDANIRIMSDLQEQLDYQNGWQFETRISQVLTLLNL---DPDATLDSLSGGWL 162
Cdd:COG0488    81 TVLDGDAELRALEAELEELEAKLAE--PDEDLERLAELQEEFEALGGWEAEARAEEILSGLGFpeeDLDRPVSELSGGWR 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 163 RKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVITSWPGNYDEYL 242
Cdd:COG0488   159 RRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAYL 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 243 QGKEEALRVEELQHAEFDRKLAQEEVWVRQ-GIKARR-TRNEGRVRALEAMRMERSQRRElqGKAKLQMDDVNRSGKLVF 320
Cdd:COG0488   239 EQRAERLEQEAAAYAKQQKKIAKEEEFIRRfRAKARKaKQAQSRIKALEKLEREEPPRRD--KTVEIRFPPPERLGKKVL 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKGGTKLEVAYFDQYRDQLDPEQTV 400
Cdd:COG0488   317 ELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQEELDPDKTV 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 401 MDNVGEGKQEvmvrGRSRHILGYLQDFLFEPKRARTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVETLELLE 480
Cdd:COG0488   397 LDELRDGAPG----GTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALE 472
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 1411607396 481 ELLADYPGTLLLVSHDRRFIDNTVTGCWLFEgDGRISDYVGGYADMMA 528
Cdd:COG0488   473 EALDDFPGTVLLVSHDRYFLDRVATRILEFE-DGGVREYPGGYDDYLE 519
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
17-545 2.58e-136

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: 409.71  E-value: 2.58e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  17 PLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGelpLD---DGRMVQQQDLKVTRLEQDPPASSDLTVFDYTAEGLAG 93
Cdd:TIGR03719  19 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG---VDkdfNGEARPQPGIKVGYLPQEPQLDPTKTVRENVEEGVAE 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  94 VGELLKKYHHISMELAHDPSDAN--IRIMSDLQEQLDYQNGWQFETRISQVLTLLNLDP-DATLDSLSGGWLRKVALARA 170
Cdd:TIGR03719  96 IKDALDRFNEISAKYAEPDADFDklAAEQAELQEIIDAADAWDLDSQLEIAMDALRCPPwDADVTKLSGGERRRVALCRL 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 171 LACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVITSWPGNYDEYLQGKEEALR 250
Cdd:TIGR03719 176 LLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWLEQKQKRLE 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 251 VEELQHAEFDRKLAQEEVWVRQGIKARRTRNEGRVRALEAMRMERSQRRElqGKAKLQMDDVNRSGKLVFETEGLGLDFG 330
Cdd:TIGR03719 256 QEEKEESARQKTLKRELEWVRQSPKGRQAKSKARLARYEELLSQEFQKRN--ETAEIYIPPGPRLGDKVIEAENLTKAFG 333
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 331 DRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKGGTKLEVAYFDQYRDQLDPEQTVMDNVGEGKQE 410
Cdd:TIGR03719 334 DKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQSRDALDPNKTVWEEISGGLDI 413
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 411 VMVRGRSRHILGYLQDFLFEPKRARTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVETLELLEELLADYPGTL 490
Cdd:TIGR03719 414 IKLGKREIPSRAYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCA 493
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1411607396 491 LLVSHDRRFIDNTVTGCWLFEGDGRISDYVGGYADMMATRAQqstQLAAKAAQVK 545
Cdd:TIGR03719 494 VVISHDRWFLDRIATHILAFEGDSHVEWFEGNFSEYEEDKKR---RLGEDADQPH 545
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
323-514 2.04e-50

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: 171.48  E-value: 2.04e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 323 EGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKGGTKLEVAYFDQyrdqldpeqtvmd 402
Cdd:cd03221     4 ENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ------------- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 403 nvgegkqevmvrgrsrhilgylqdflfepkrartpvkaLSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVETLELLEEL 482
Cdd:cd03221    71 --------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEA 112
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1411607396 483 LADYPGTLLLVSHDRRFIDNTVTGCWLFEGDG 514
Cdd:cd03221   113 LKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
335-469 3.21e-28

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: 110.43  E-value: 3.21e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 335 FQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-----------GGTKLEVAYFDQYrDQLDPEQTVMDN 403
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILldgqdltdderKSLRKEIGYVFQD-PQLFPRLTVREN 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1411607396 404 VGEGKQEVMVRGRSR-----HILGYLQDFLFEPKRARTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTN 469
Cdd:pfam00005  80 LRLGLLLKGLSKREKdaraeEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
329-496 4.16e-20

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 88.44  E-value: 4.16e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 329 FGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKGGTKLEVAYFDQyRDQLDPE--QTVMDNVGE 406
Cdd:NF040873    2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQ-RSEVPDSlpLTVRDLVAM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 407 GK-QEvmvRGRSRHI--------------LGyLQDFlfepkrARTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDL 471
Cdd:NF040873   81 GRwAR---RGLWRRLtrddraavddalerVG-LADL------AGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150
                         170       180
                  ....*....|....*....|....*...
gi 1411607396 472 DVETLELLEELLADYPG---TLLLVSHD 496
Cdd:NF040873  151 DAESRERIIALLAEEHArgaTVVVVTHD 178
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
17-226 1.21e-19

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 87.29  E-value: 1.21e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  17 PLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMVQQQDLKVTRLEQ--DPPASSDLTVFDYTAEGLAGV 94
Cdd:NF040873    6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQrsEVPDSLPLTVRDLVAMGRWAR 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  95 GELLKKYHHismelahdpsdANIRIMSDLQEQLDYQNgwqFETRisqvltllnldpdaTLDSLSGGWLRKVALARALACD 174
Cdd:NF040873   86 RGLWRRLTR-----------DDRAAVDDALERVGLAD---LAGR--------------QLGELSGGQRQRALLAQGLAQE 137
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1411607396 175 PDLLLLDEPTNHLDIEAINWLEDFLKDFRG---AIVFISHDREFIhKLATRIIDL 226
Cdd:NF040873  138 ADLLLLDEPTTGLDAESRERIIALLAEEHArgaTVVVVTHDLELV-RRADPCVLL 191
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
344-503 1.71e-08

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: 53.92  E-value: 1.71e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  344 RGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKggtklevaYFDqyrdqldpeqtvmdnvGEGKQEVMVRGRSRHILGy 423
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVI--------YID----------------GEDILEEVLDQLLLIIVG- 55
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  424 lqdflfepkrarTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVETLELLEELLADYPGTLLLVSHDRRFIDNT 503
Cdd:smart00382  56 ------------GKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLTVILTT 123
GguA NF040905
sugar ABC transporter ATP-binding protein;
19-223 1.21e-07

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 54.80  E-value: 1.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  19 LDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELP--------LDDGRMVQQQDLKvtrleqdppassdltvfDYTAEG 90
Cdd:NF040905   17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPhgsyegeiLFDGEVCRFKDIR-----------------DSEALG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  91 LAgvgellkkyhHISMELAHDP--SDA-NIRIMSdlqEQLdyQNG---WQfETRISQVLTL----LNLDPDATLDSLSGG 160
Cdd:NF040905   80 IV----------IIHQELALIPylSIAeNIFLGN---ERA--KRGvidWN-ETNRRARELLakvgLDESPDTLVTDIGVG 143
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1411607396 161 WLRKVALARALACDPDLLLLDEPT---NHLDIEAinwLEDFLKDFRG---AIVFISHDREFIHKLATRI 223
Cdd:NF040905  144 KQQLVEIAKALSKDVKLLILDEPTaalNEEDSAA---LLDLLLELKAqgiTSIIISHKLNEIRRVADSI 209
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
19-468 3.56e-07

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 53.59  E-value: 3.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  19 LDNAELSIERGERLCLVGRNGAGKSTLMKIIAGElplddgRMVQQqdlkvtrleqdppasSDLTVFD------------- 85
Cdd:NF033858   17 LDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGA------RKIQQ---------------GRVEVLGgdmadarhrravc 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  86 ----YTAEGLagvGELLkkYHHISMElahdpsdanirimsdlqEQLDY------QNGWQFETRISQVLTLLNLDP--DAT 153
Cdd:NF033858   76 priaYMPQGL---GKNL--YPTLSVF-----------------ENLDFfgrlfgQDAAERRRRIDELLRATGLAPfaDRP 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 154 LDSLSGGWLRKVALARALACDPDLLLLDEPTNHLD----------IEAInwledflkdfRGA------IVfishdrefih 217
Cdd:NF033858  134 AGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDplsrrqfwelIDRI----------RAErpgmsvLV---------- 193
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 218 klATriidldrgvitswpgnydEYLqgkEEALRveelqhaeFDRKLAQeevwvrqgikarrtrNEGRVRALEAMR--MER 295
Cdd:NF033858  194 --AT------------------AYM---EEAER--------FDWLVAM---------------DAGRVLATGTPAelLAR 227
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 296 SQRREL-------------QGKAKLQMD--DVNRSGKLVFETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKST 360
Cdd:NF033858  228 TGADTLeaafiallpeekrRGHQPVVIPprPADDDDEPAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKST 307
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 361 LIKLLLGQLEPSRG-------LVKGG---TKLEVAYFDQ----YRdqldpEQTVMDN---------VGEGKQEVMVRgrs 417
Cdd:NF033858  308 TMKMLTGLLPASEGeawlfgqPVDAGdiaTRRRVGYMSQafslYG-----ELTVRQNlelharlfhLPAAEIAARVA--- 379
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1411607396 418 rhilGYLQDFLFEPKRARTPvKALSGGEKNRLLLAKLFL-KPSnLLILDEPT 468
Cdd:NF033858  380 ----EMLERFDLADVADALP-DSLPLGIRQRLSLAVAVIhKPE-LLILDEPT 425
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
323-468 5.24e-06

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 49.74  E-value: 5.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 323 EGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGqlepSRGLVKGgtKLEV------------------ 384
Cdd:NF033858    5 EGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAG----ARKIQQG--RVEVlggdmadarhrravcpri 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 385 AYFDQ------YrdqldPEQTVMDNV-------GEGKQEvmvrgRSRHILGYLQDFLFEPKRARtPVKALSGGEKNRL-L 450
Cdd:NF033858   79 AYMPQglgknlY-----PTLSVFENLdffgrlfGQDAAE-----RRRRIDELLRATGLAPFADR-PAGKLSGGMKQKLgL 147
                         170
                  ....*....|....*...
gi 1411607396 451 LAKLFLKPsNLLILDEPT 468
Cdd:NF033858  148 CCALIHDP-DLLILDEPT 164
GguA NF040905
sugar ABC transporter ATP-binding protein;
19-210 5.83e-05

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 45.94  E-value: 5.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  19 LDNAELSIERGERLCLVGRNGAGKSTL-MKI--------IAGELpLDDGRMVqqqDLKvtrleqdppassdlTVFDYTAE 89
Cdd:NF040905  276 VDDVSLNVRRGEIVGIAGLMGAGRTELaMSVfgrsygrnISGTV-FKDGKEV---DVS--------------TVSDAIDA 337
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  90 GLAGVGELLKKYHHISME-LAHDPSDANIRIMS-----DLQEQLDYQNGWQFETRI--SQVltllnldpDATLDSLSGGW 161
Cdd:NF040905  338 GLAYVTEDRKGYGLNLIDdIKRNITLANLGKVSrrgviDENEEIKVAEEYRKKMNIktPSV--------FQKVGNLSGGN 409
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1411607396 162 LRKVALARALACDPDLLLLDEPTNHLDIEA-------INWLEDFLKdfrgAIVFIS 210
Cdd:NF040905  410 QQKVVLSKWLFTDPDVLILDEPTRGIDVGAkyeiytiINELAAEGK----GVIVIS 461
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
7-59 1.40e-04

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 45.12  E-value: 1.40e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1411607396   7 HGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGR 59
Cdd:NF033858  270 RGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGE 322
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
158-261 2.19e-03

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 40.87  E-value: 2.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 158 SGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDF--RGAIVFISHD-REFIHKLATRIIDLDRGVITSw 234
Cdd:NF000106  146 SGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMvrDGATVLLTTQyMEEAEQLAHELTVIDRGRVIA- 224
                          90       100
                  ....*....|....*....|....*....
gi 1411607396 235 PGNYDEyLQGK--EEALRVEELQHAEFDR 261
Cdd:NF000106  225 DGKVDE-LKTKvgGRTLQIRPAHAAELDR 252
 
Name Accession Description Interval E-value
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
1-633 0e+00

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 1106.17  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   1 MALLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMVQQQDLKVTRLEQDPPASSD 80
Cdd:PRK11147    1 MSLISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQDPPRNVE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  81 LTVFDYTAEGLAGVGELLKKYHHISMELAHDPSDANIRIMSDLQEQLDYQNGWQFETRISQVLTLLNLDPDATLDSLSGG 160
Cdd:PRK11147   81 GTVYDFVAEGIEEQAEYLKRYHDISHLVETDPSEKNLNELAKLQEQLDHHNLWQLENRINEVLAQLGLDPDAALSSLSGG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 161 WLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVITSWPGNYDE 240
Cdd:PRK11147  161 WLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGNYDQ 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 241 YLQGKEEALRVEELQHAEFDRKLAQEEVWVRQGIKARRTRNEGRVRALEAMRMERSQRRELQGKAKLQMDDVNRSGKLVF 320
Cdd:PRK11147  241 YLLEKEEALRVEELQNAEFDRKLAQEEVWIRQGIKARRTRNEGRVRALKALRRERSERREVMGTAKMQVEEASRSGKIVF 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKGGTKLEVAYFDQYRDQLDPEQTV 400
Cdd:PRK11147  321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFDQHRAELDPEKTV 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 401 MDNVGEGKQEVMVRGRSRHILGYLQDFLFEPKRARTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVETLELLE 480
Cdd:PRK11147  401 MDNLAEGKQEVMVNGRPRHVLGYLQDFLFHPKRAMTPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLE 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 481 ELLADYPGTLLLVSHDRRFIDNTVTGCWLFEGDGRISDYVGGYADMMATRAqQSTQLAAKAAQVKTPEPVAVASPAASKV 560
Cdd:PRK11147  481 ELLDSYQGTVLLVSHDRQFVDNTVTECWIFEGNGKIGRYVGGYHDARQQQA-QYLALKQPAVKKKEEAAAPKAETVKRSS 559
                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1411607396 561 KKLSYKLQLELDNLPARLEQLETELNALQAEVNHPGFFALPSDQTQLKLDALNAAEAALEQAFSRWEELEALK 633
Cdd:PRK11147  560 KKLSYKLQRELEQLPQLLEDLEAEIEALQAQVADADFFSQPHEQTQKVLADLADAEQELEVAFERWEELEALK 632
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
6-528 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: 687.57  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   6 LHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMVQQQDLKVTRLEQDPPASSDLTVFD 85
Cdd:COG0488     1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPLDDDLTVLD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  86 YTAEGLAGVGELLKKYHHISMELAHdpSDANIRIMSDLQEQLDYQNGWQFETRISQVLTLLNL---DPDATLDSLSGGWL 162
Cdd:COG0488    81 TVLDGDAELRALEAELEELEAKLAE--PDEDLERLAELQEEFEALGGWEAEARAEEILSGLGFpeeDLDRPVSELSGGWR 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 163 RKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVITSWPGNYDEYL 242
Cdd:COG0488   159 RRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAYL 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 243 QGKEEALRVEELQHAEFDRKLAQEEVWVRQ-GIKARR-TRNEGRVRALEAMRMERSQRRElqGKAKLQMDDVNRSGKLVF 320
Cdd:COG0488   239 EQRAERLEQEAAAYAKQQKKIAKEEEFIRRfRAKARKaKQAQSRIKALEKLEREEPPRRD--KTVEIRFPPPERLGKKVL 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKGGTKLEVAYFDQYRDQLDPEQTV 400
Cdd:COG0488   317 ELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQEELDPDKTV 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 401 MDNVGEGKQEvmvrGRSRHILGYLQDFLFEPKRARTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVETLELLE 480
Cdd:COG0488   397 LDELRDGAPG----GTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALE 472
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 1411607396 481 ELLADYPGTLLLVSHDRRFIDNTVTGCWLFEgDGRISDYVGGYADMMA 528
Cdd:COG0488   473 EALDDFPGTVLLVSHDRYFLDRVATRILEFE-DGGVREYPGGYDDYLE 519
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
17-545 2.58e-136

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: 409.71  E-value: 2.58e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  17 PLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGelpLD---DGRMVQQQDLKVTRLEQDPPASSDLTVFDYTAEGLAG 93
Cdd:TIGR03719  19 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG---VDkdfNGEARPQPGIKVGYLPQEPQLDPTKTVRENVEEGVAE 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  94 VGELLKKYHHISMELAHDPSDAN--IRIMSDLQEQLDYQNGWQFETRISQVLTLLNLDP-DATLDSLSGGWLRKVALARA 170
Cdd:TIGR03719  96 IKDALDRFNEISAKYAEPDADFDklAAEQAELQEIIDAADAWDLDSQLEIAMDALRCPPwDADVTKLSGGERRRVALCRL 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 171 LACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVITSWPGNYDEYLQGKEEALR 250
Cdd:TIGR03719 176 LLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWLEQKQKRLE 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 251 VEELQHAEFDRKLAQEEVWVRQGIKARRTRNEGRVRALEAMRMERSQRRElqGKAKLQMDDVNRSGKLVFETEGLGLDFG 330
Cdd:TIGR03719 256 QEEKEESARQKTLKRELEWVRQSPKGRQAKSKARLARYEELLSQEFQKRN--ETAEIYIPPGPRLGDKVIEAENLTKAFG 333
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 331 DRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKGGTKLEVAYFDQYRDQLDPEQTVMDNVGEGKQE 410
Cdd:TIGR03719 334 DKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQSRDALDPNKTVWEEISGGLDI 413
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 411 VMVRGRSRHILGYLQDFLFEPKRARTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVETLELLEELLADYPGTL 490
Cdd:TIGR03719 414 IKLGKREIPSRAYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCA 493
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1411607396 491 LLVSHDRRFIDNTVTGCWLFEGDGRISDYVGGYADMMATRAQqstQLAAKAAQVK 545
Cdd:TIGR03719 494 VVISHDRWFLDRIATHILAFEGDSHVEWFEGNFSEYEEDKKR---RLGEDADQPH 545
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
17-525 2.04e-134

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 404.89  E-value: 2.04e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  17 PLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGelpLD---DGRMVQQQDLKVTRLEQDPPASSDLTVFDYTAEGLAG 93
Cdd:PRK11819   21 QILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG---VDkefEGEARPAPGIKVGYLPQEPQLDPEKTVRENVEEGVAE 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  94 VGELLKKYHHISMELAHDP--SDANIRIMSDLQEQLDYQNGWQFETRISQVLTLLNL-DPDATLDSLSGGWLRKVALARA 170
Cdd:PRK11819   98 VKAALDRFNEIYAAYAEPDadFDALAAEQGELQEIIDAADAWDLDSQLEIAMDALRCpPWDAKVTKLSGGERRRVALCRL 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 171 LACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVITSWPGNYDEYLQGKEEALR 250
Cdd:PRK11819  178 LLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWLEQKAKRLA 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 251 VEELQHAEFDRKLAQEEVWVRQGIKARRTRNEGRVRALEAMRMERSQRRElqGKAKLQMDDVNRSGKLVFETEGLGLDFG 330
Cdd:PRK11819  258 QEEKQEAARQKALKRELEWVRQSPKARQAKSKARLARYEELLSEEYQKRN--ETNEIFIPPGPRLGDKVIEAENLSKSFG 335
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 331 DRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKGGTKLEVAYFDQYRDQLDPEQTVMDNVGEGKQE 410
Cdd:PRK11819  336 DRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYVDQSRDALDPNKTVWEEISGGLDI 415
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 411 VMVRGR---SRhilGYLQDFLFEPKRARTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVETLELLEELLADYP 487
Cdd:PRK11819  416 IKVGNReipSR---AYVGRFNFKGGDQQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFP 492
                         490       500       510
                  ....*....|....*....|....*....|....*...
gi 1411607396 488 GTLLLVSHDRRFIDNTVTGCWLFEGDGRISDYVGGYAD 525
Cdd:PRK11819  493 GCAVVISHDRWFLDRIATHILAFEGDSQVEWFEGNFQE 530
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
13-531 9.38e-91

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 291.03  E-value: 9.38e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  13 FSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMVQQQDLKVTRLEQDPPASSDLTVFDYTAEGLA 92
Cdd:PRK15064   11 FGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKLRQDQFAFEEFTVLDTVIMGHT 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  93 GVGELLKKYHHISMELahDPSDANIRIMSDLQEQLDYQNGWQFETRISQVLTLLNLDPD---ATLDSLSGGWLRKVALAR 169
Cdd:PRK15064   91 ELWEVKQERDRIYALP--EMSEEDGMKVADLEVKFAEMDGYTAEARAGELLLGVGIPEEqhyGLMSEVAPGWKLRVLLAQ 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 170 ALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVITSWPGNYDEYLQGKEEAl 249
Cdd:PRK15064  169 ALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELRVYPGNYDEYMTAATQA- 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 250 rvEELQHAEFDRKLAQ-EEVwvrQGIKARRTRNegrvrALEAmRMERSQRRELQgkaKLQMDDVNRSGK----------- 317
Cdd:PRK15064  248 --RERLLADNAKKKAQiAEL---QSFVSRFSAN-----ASKA-KQATSRAKQID---KIKLEEVKPSSRqnpfirfeqdk 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 318 ----LVFETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKGGTKLEVAYFDQ-YRD 392
Cdd:PRK15064  314 klhrNALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQdHAY 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 393 QLDPEQTVMDNVGEGKQ----EVMVRGrsrhILGYLqdfLFEPKRARTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPT 468
Cdd:PRK15064  394 DFENDLTLFDWMSQWRQegddEQAVRG----TLGRL---LFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPT 466
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1411607396 469 NDLDVETLELLEELLADYPGTLLLVSHDRRFIDNTVTGCWLFEGDGrISDYVGGYADMMATRA 531
Cdd:PRK15064  467 NHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDG-VVDFSGTYEEYLRSQG 528
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
18-592 3.95e-69

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 236.61  E-value: 3.95e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  18 LLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMVQQQDLKVTRLEQDPPASsDLTVFDYTAEGLagvgel 97
Cdd:PRK10636   16 LLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETPAL-PQPALEYVIDGD------ 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  98 lKKYHHISMELAHDPSDANIRIMSDLQEQLDYQNGWQFETRISQVLTLLNLDPDA---TLDSLSGGWLRKVALARALACD 174
Cdd:PRK10636   89 -REYRQLEAQLHDANERNDGHAIATIHGKLDAIDAWTIRSRAASLLHGLGFSNEQlerPVSDFSGGWRMRLNLAQALICR 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 175 PDLLLLDEPTNHLDIEAINWLEDFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVITSWPGNYDEYLQGKEEALRVEEL 254
Cdd:PRK10636  168 SDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSSFEVQRATRLAQQQA 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 255 QHAEFDRKLAQEEVWV-RQGIKARRTRN-EGRVRALEamRMERSQRRELQGKAKLQMDDVNRSGKLVFETEGLGLDFGDR 332
Cdd:PRK10636  248 MYESQQERVAHLQSYIdRFRAKATKAKQaQSRIKMLE--RMELIAPAHVDNPFHFSFRAPESLPNPLLKMEKVSAGYGDR 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 333 TLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKGGTKLEVAYFDQYrdqldpeQTVMDNVGEGKQEVM 412
Cdd:PRK10636  326 IILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQH-------QLEFLRADESPLQHL 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 413 VRGRSRHILGYLQDFL----FEPKRARTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVETLELLEELLADYPG 488
Cdd:PRK10636  399 ARLAPQELEQKLRDYLggfgFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEG 478
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 489 TLLLVSHDRRFIDNTVTGCWL--------FEGDgrISDYVGGYADMMATRAQQS---TQLAAKAAQVKTPEPVAVAspaa 557
Cdd:PRK10636  479 ALVVVSHDRHLLRSTTDDLYLvhdgkvepFDGD--LEDYQQWLSDVQKQENQTDeapKENNANSAQARKDQKRREA---- 552
                         570       580       590
                  ....*....|....*....|....*....|....*
gi 1411607396 558 sKVKKLSYKLQLELDNLPARLEQLETELNALQAEV 592
Cdd:PRK10636  553 -ELRTQTQPLRKEIARLEKEMEKLNAQLAQAEEKL 586
PLN03073 PLN03073
ABC transporter F family; Provisional
18-525 2.62e-59

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 211.26  E-value: 2.62e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  18 LLDNAELSIERGERLCLVGRNGAGKSTLMKIIA-----------------GELPLDDGRMVQ---QQDLKVTRLEQDP-- 75
Cdd:PLN03073  192 LIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAmhaidgipkncqilhveQEVVGDDTTALQcvlNTDIERTQLLEEEaq 271
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  76 --PASSDLTVFDYTAEGLAGVGELLKKyhhismelahdpsDANIRIMSDLQEQLDYQNGWQFETRISQVLTLLNLDPDAT 153
Cdd:PLN03073  272 lvAQQRELEFETETGKGKGANKDGVDK-------------DAVSQRLEEIYKRLELIDAYTAEARAASILAGLSFTPEMQ 338
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 154 L---DSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRGAIVFISHDREFIHKLATRIIDLDRGV 230
Cdd:PLN03073  339 VkatKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLHGQK 418
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 231 ITSWPGNYDEYLQGKEEALRVEELQHAEFDRKLAQEEVWV---RQGIKaRRTRNEGRVRALEAMRMERSQRRELQGKAKL 307
Cdd:PLN03073  419 LVTYKGDYDTFERTREEQLKNQQKAFESNERSRSHMQAFIdkfRYNAK-RASLVQSRIKALDRLGHVDAVVNDPDYKFEF 497
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 308 QMDDVNRSGKLV-FETEGLGLDfGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKGGTKLEVAY 386
Cdd:PLN03073  498 PTPDDRPGPPIIsFSDASFGYP-GGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAV 576
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 387 FDQYR-DQLDPEQT---VMDNVGEGKQEVMVRGrsrhilgYLQDFLFEPKRARTPVKALSGGEKNRLLLAKLFLKPSNLL 462
Cdd:PLN03073  577 FSQHHvDGLDLSSNpllYMMRCFPGVPEQKLRA-------HLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHIL 649
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1411607396 463 ILDEPTNDLDVETLELLEELLADYPGTLLLVSHDRRFIDNTVTGCWLFEgDGRISDYVGGYAD 525
Cdd:PLN03073  650 LLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVS-EGKVTPFHGTFHD 711
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
3-243 4.67e-55

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 195.67  E-value: 4.67e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   3 LLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMVQQQDLKVTRLEQDPPA-SSDL 81
Cdd:COG0488   315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQEElDPDK 394
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  82 TVFDYtaeglagvgellkkyhhismelahdpsdaniriMSDLQEQLDyqngwqfETRISQVLTLLNLDPDATL---DSLS 158
Cdd:COG0488   395 TVLDE---------------------------------LRDGAPGGT-------EQEVRGYLGRFLFSGDDAFkpvGVLS 434
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 159 GGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVITSWPGNY 238
Cdd:COG0488   435 GGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREYPGGY 514

                  ....*
gi 1411607396 239 DEYLQ 243
Cdd:COG0488   515 DDYLE 519
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
322-542 8.20e-54

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 192.20  E-value: 8.20e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 322 TEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKGGTKLEVAYFDQyRDQLDPEQTVM 401
Cdd:COG0488     1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQ-EPPLDDDLTVL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 402 DNVGEGKQEVM-VRGRSRHI-------------LGYLQDFL--------------------FEPKRARTPVKALSGGEKN 447
Cdd:COG0488    80 DTVLDGDAELRaLEAELEELeaklaepdedlerLAELQEEFealggweaearaeeilsglgFPEEDLDRPVSELSGGWRR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 448 RLLLAKLFLKPSNLLILDEPTNDLDVETLELLEELLADYPGTLLLVSHDRRFIDNTVTgcWLFE-GDGRISDYVGGYADM 526
Cdd:COG0488   160 RVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVAT--RILElDRGKLTLYPGNYSAY 237
                         250
                  ....*....|....*.
gi 1411607396 527 MATRAQQSTQLAAKAA 542
Cdd:COG0488   238 LEQRAERLEQEAAAYA 253
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
323-514 2.04e-50

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: 171.48  E-value: 2.04e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 323 EGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKGGTKLEVAYFDQyrdqldpeqtvmd 402
Cdd:cd03221     4 ENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ------------- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 403 nvgegkqevmvrgrsrhilgylqdflfepkrartpvkaLSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVETLELLEEL 482
Cdd:cd03221    71 --------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEA 112
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1411607396 483 LADYPGTLLLVSHDRRFIDNTVTGCWLFEGDG 514
Cdd:cd03221   113 LKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
4-229 8.90e-50

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: 169.55  E-value: 8.90e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   4 LTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMVQQQDLKVTRLEQdppassdltv 83
Cdd:cd03221     1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ---------- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  84 fdytaeglagvgellkkyhhismelahdpsdanirimsdlqeqldyqngwqfetrisqvltllnldpdatldsLSGGWLR 163
Cdd:cd03221    71 -------------------------------------------------------------------------LSGGEKM 77
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1411607396 164 KVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRGAIVFISHDREFIHKLATRIIDLDRG 229
Cdd:cd03221    78 RLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDG 143
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
2-473 1.76e-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: 166.23  E-value: 1.76e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   2 ALLTLHGACLSF--SDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELP---------LDDGRMVQQQDLKVTR 70
Cdd:COG1123     3 PLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPhggrisgevLLDGRDLLELSEALRG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  71 LE-----QDPPASSD-LTVFDYTAEGLagvgellkkyhhismeLAHDPSDANIRimsdlqeqldyqngwqfeTRISQVLT 144
Cdd:COG1123    83 RRigmvfQDPMTQLNpVTVGDQIAEAL----------------ENLGLSRAEAR------------------ARVLELLE 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 145 LLNLDP--DATLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLD----IEAINWLEDFLKDFRGAIVFISHDREFIHK 218
Cdd:COG1123   129 AVGLERrlDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDvttqAEILDLLRELQRERGTTVLLITHDLGVVAE 208
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 219 LATRIIDLDRGVItswpgnydeylqgkeealrVEELQHAEFDRklaqeevwvrqgikarrtrnegRVRALEAMRMERSQR 298
Cdd:COG1123   209 IADRVVVMDDGRI-------------------VEDGPPEEILA----------------------APQALAAVPRLGAAR 247
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 299 RELQGKAklqmddvnRSGKLVFETEGLGLDF-----GDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSR 373
Cdd:COG1123   248 GRAAPAA--------AAAEPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTS 319
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 374 G--LVKG---GTKLEVAYFDQYRD----------QLDPEQTVMDNVGEGkqeVMVRG------RSRHILGYLQDFLFEPK 432
Cdd:COG1123   320 GsiLFDGkdlTKLSRRSLRELRRRvqmvfqdpysSLNPRMTVGDIIAEP---LRLHGllsraeRRERVAELLERVGLPPD 396
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|..
gi 1411607396 433 RARTPVKALSGGEKNRLLLAK-LFLKPSnLLILDEPTNDLDV 473
Cdd:COG1123   397 LADRYPHELSGGQRQRVAIARaLALEPK-LLILDEPTSALDV 437
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
3-231 1.75e-37

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: 139.79  E-value: 1.75e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   3 LLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGR-MVQQQDL----------KVTRL 71
Cdd:COG1120     1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEvLLDGRDLaslsrrelarRIAYV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  72 EQDPPASSDLTVFDYTAEGLagvgellkkYHHISMELAHDPSDanirimsdlqeqldyqngwqfETRISQVLTLLNLDP- 150
Cdd:COG1120    81 PQEPPAPFGLTVRELVALGR---------YPHLGLFGRPSAED---------------------REAVEEALERTGLEHl 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 151 -DATLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDI----EAINWLEDFLKDFRGAIVFISHDREFIHKLATRIID 225
Cdd:COG1120   131 aDRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLahqlEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVL 210

                  ....*.
gi 1411607396 226 LDRGVI 231
Cdd:COG1120   211 LKDGRI 216
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
12-231 2.56e-37

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 138.66  E-value: 2.56e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  12 SFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRM------VQQQDLKVTR----LEQDPPASSDL 81
Cdd:COG1131     9 RYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVrvlgedVARDPAEVRRrigyVPQEPALYPDL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  82 TVFDYTaeglagvgELLKKYHHISMELAhdpsdanirimsdlqeqldyqngwqfETRISQVLTLLNLDP--DATLDSLSG 159
Cdd:COG1131    89 TVRENL--------RFFARLYGLPRKEA--------------------------RERIDELLELFGLTDaaDRKVGTLSG 134
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1411607396 160 GWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDF--RGAIVFIS-HDREFIHKLATRIIDLDRGVI 231
Cdd:COG1131   135 GMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELaaEGKTVLLStHYLEEAERLCDRVAIIDKGRI 209
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
1-257 1.19e-36

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 137.14  E-value: 1.19e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   1 MALLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRM------VQQQDLKVTRLEQD 74
Cdd:COG1121     4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVrlfgkpPRRARRRIGYVPQR 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  75 PPASSD--LTVFDYTAEGLAGVGELLKKYHHIsmelahdpsdanirimsdlqeqlDYQngwqfetRISQVLTLLNLDP-- 150
Cdd:COG1121    84 AEVDWDfpITVRDVVLMGRYGRRGLFRRPSRA-----------------------DRE-------AVDEALERVGLEDla 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 151 DATLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRG---AIVFISHDREFIHKLATRIIDLD 227
Cdd:COG1121   134 DRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRegkTILVVTHDLGAVREYFDRVLLLN 213
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1411607396 228 RGVITSwpGNYDEYLQgkEEAL------RVEELQHA 257
Cdd:COG1121   214 RGLVAH--GPPEEVLT--PENLsrayggPVALLAHG 245
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
12-231 1.82e-34

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: 128.67  E-value: 1.82e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  12 SFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRmvqqqdlkVTRLEQDPPASsdltvfdytaegl 91
Cdd:cd03230     9 RYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGE--------IKVLGKDIKKE------------- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  92 agvGELLKKyhhismelahdpsdaNIRIMSDLQEQLDYQNGWQfetrisqvltllNLDpdatldsLSGGWLRKVALARAL 171
Cdd:cd03230    68 ---PEEVKR---------------RIGYLPEEPSLYENLTVRE------------NLK-------LSGGMKQRLALAQAL 110
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1411607396 172 ACDPDLLLLDEPTNHLDIEAINWLEDFLKDFR---GAIVFISHDREFIHKLATRIIDLDRGVI 231
Cdd:cd03230   111 LHDPELLILDEPTSGLDPESRREFWELLRELKkegKTILLSSHILEEAERLCDRVAILNNGRI 173
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
11-229 6.82e-34

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: 128.35  E-value: 6.82e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  11 LSFS----DFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGR-MVQQQDLKVTRLE----------QDP 75
Cdd:cd03225     5 LSFSypdgARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEvLVDGKDLTKLSLKelrrkvglvfQNP 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  76 passD-----LTVFDYTAEGLAGVGellkkyhhismelaHDPSDAnirimsdlqeqldyqngwqfETRISQVLTLLNLDP 150
Cdd:cd03225    85 ----DdqffgPTVEEEVAFGLENLG--------------LPEEEI--------------------EERVEEALELVGLEG 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 151 --DATLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRGA---IVFISHDREFIHKLATRIID 225
Cdd:cd03225   127 lrDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEgktIIIVTHDLDLLLELADRVIV 206

                  ....
gi 1411607396 226 LDRG 229
Cdd:cd03225   207 LEDG 210
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
12-231 8.58e-34

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: 129.21  E-value: 8.58e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  12 SFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLD------DGRMVQQQDLKVTR----LEQDPPASSDL 81
Cdd:COG4555    10 KYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDsgsiliDGEDVRKEPREARRqigvLPDERGLYDRL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  82 TVFDytaeglagvgellkkyhhismelahdpsdaNIRIMSDLQEQLDYQNgwqfETRISQVLTLLNLDP--DATLDSLSG 159
Cdd:COG4555    90 TVRE------------------------------NIRYFAELYGLFDEEL----KKRIEELIELLGLEEflDRRVGELST 135
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1411607396 160 GWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRG---AIVFISHDREFIHKLATRIIDLDRGVI 231
Cdd:COG4555   136 GMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKegkTVLFSSHIMQEVEALCDRVVILHKGKV 210
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
4-246 1.27e-32

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 132.32  E-value: 1.27e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   4 LTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMVQQQDLKVTRLEQDPPA--SSDL 81
Cdd:PRK15064  320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQDHAYdfENDL 399
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  82 TVFDYtaeglagvgellkkyhhisMELAHDPSDANIRIMSDLQEQLDYQNgwqfetrisqvltllnlDPDATLDSLSGGW 161
Cdd:PRK15064  400 TLFDW-------------------MSQWRQEGDDEQAVRGTLGRLLFSQD-----------------DIKKSVKVLSGGE 443
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 162 LRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVITSWPGNYDEY 241
Cdd:PRK15064  444 KGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFSGTYEEY 523

                  ....*..
gi 1411607396 242 L--QGKE 246
Cdd:PRK15064  524 LrsQGIE 530
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
2-228 1.91e-32

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: 124.13  E-value: 1.91e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   2 ALLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMvqqqdlkvtRLEQDPPASSDL 81
Cdd:COG4133     1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEV---------LWNGEPIRDARE 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  82 TVFDYTAeglagvgellkkYhhismeLAHDPsdaniRIMSDL--QEQLDY----QNGWQFETRISQVLTLLNLDP--DAT 153
Cdd:COG4133    72 DYRRRLA------------Y------LGHAD-----GLKPELtvRENLRFwaalYGLRADREAIDEALEAVGLAGlaDLP 128
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1411607396 154 LDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFR---GAIVFISHDREFIhkLATRIIDLDR 228
Cdd:COG4133   129 VRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLargGAVLLTTHQPLEL--AAARVLDLGD 204
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
3-232 6.04e-32

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: 124.15  E-value: 6.04e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   3 LLTLHGACLSFS----DFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRM------VQQQDLKVTR-- 70
Cdd:COG1124     1 MLEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVtfdgrpVTRRRRKAFRrr 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  71 ---LEQDPPASSD--LTVFDYTAEGLAGvgellkkyHHISMElahdpsdanirimsdlqeqldyqngwqfETRISQVLTL 145
Cdd:COG1124    81 vqmVFQDPYASLHprHTVDRILAEPLRI--------HGLPDR----------------------------EERIAELLEQ 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 146 LNLDPDAtLD----SLSGGWLRKVALARALACDPDLLLLDEPTNHLDI----EAINWLEDFLKDFRGAIVFISHDREFIH 217
Cdd:COG1124   125 VGLPPSF-LDryphQLSGGQRQRVAIARALILEPELLLLDEPTSALDVsvqaEILNLLKDLREERGLTYLFVSHDLAVVA 203
                         250
                  ....*....|....*
gi 1411607396 218 KLATRIIDLDRGVIT 232
Cdd:COG1124   204 HLCDRVAVMQNGRIV 218
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
11-231 1.07e-31

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: 122.83  E-value: 1.07e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  11 LSFS---DFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRM-VQQQDLKVTRLE----------QDP- 75
Cdd:COG1122     6 LSFSypgGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVlVDGKDITKKNLRelrrkvglvfQNPd 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  76 -----PassdlTVFDYTAEGLagvgellkkyhhisMELAHDPSDAnirimsdlqeqldyqngwqfETRISQVLTLLNLDP 150
Cdd:COG1122    86 dqlfaP-----TVEEDVAFGP--------------ENLGLPREEI--------------------RERVEEALELVGLEH 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 151 --DATLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRGA---IVFISHDREFIHKLATRIID 225
Cdd:COG1122   127 laDRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEgktVIIVTHDLDLVAELADRVIV 206

                  ....*.
gi 1411607396 226 LDRGVI 231
Cdd:COG1122   207 LDDGRI 212
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
4-231 1.29e-31

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 121.85  E-value: 1.29e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   4 LTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRM----VQQQDLKVTRLEQDP---P 76
Cdd:COG4619     1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIyldgKPLSAMPPPEWRRQVayvP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  77 ASSDLtvFDYTaeglagVGELLKKYHHISmelahdpsdanirimsdlQEQLDyqngwqfETRISQVLTLLNLDP---DAT 153
Cdd:COG4619    81 QEPAL--WGGT------VRDNLPFPFQLR------------------ERKFD-------RERALELLERLGLPPdilDKP 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 154 LDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEA----INWLEDFLKDFRGAIVFISHDREFIHKLATRIIDLDRG 229
Cdd:COG4619   128 VERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENtrrvEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAG 207

                  ..
gi 1411607396 230 VI 231
Cdd:COG4619   208 RL 209
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
6-231 5.49e-31

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: 120.33  E-value: 5.49e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   6 LHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLD------DGRMVQQQDLKVTRLEQDPPASS 79
Cdd:cd03235     2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTsgsirvFGKPLEKERKRIGYVPQRRSIDR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  80 D--LTVFDYTAEGLAGVGELLKKYHHISMELAhdpsdanirimsdlQEQLDyqngwqfETRISQVLtllnldpDATLDSL 157
Cdd:cd03235    82 DfpISVRDVVLMGLYGHKGLFRRLSKADKAKV--------------DEALE-------RVGLSELA-------DRQIGEL 133
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1411607396 158 SGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRG---AIVFISHDREFIHKLATRIIDLDRGVI 231
Cdd:cd03235   134 SGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRRegmTILVVTHDLGLVLEYFDRVLLLNRTVV 210
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
4-231 3.77e-30

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: 118.01  E-value: 3.77e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   4 LTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGR-MVQQQDlkVTRLE---------- 72
Cdd:cd03259     1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEiLIDGRD--VTGVPperrnigmvf 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  73 QDPPASSDLTVFDYTAEGLagvgellkkyhhismelahdpsdaNIRIMSDLQEQldyqngwqfeTRISQVLTLLNLDPDA 152
Cdd:cd03259    79 QDYALFPHLTVAENIAFGL------------------------KLRGVPKAEIR----------ARVRELLELVGLEGLL 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 153 TL--DSLSGGWLRKVALARALACDPDLLLLDEPTNHLD----IEAINWLEDFLKDFRGAIVFISHDREFIHKLATRIIDL 226
Cdd:cd03259   125 NRypHELSGGQQQRVALARALAREPSLLLLDEPLSALDaklrEELREELKELQRELGITTIYVTHDQEEALALADRIAVM 204

                  ....*
gi 1411607396 227 DRGVI 231
Cdd:cd03259   205 NEGRI 209
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
5-233 1.07e-29

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: 115.61  E-value: 1.07e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   5 TLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRmvqqqdlkvtrleqdppassdLTVF 84
Cdd:cd03214     1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGE---------------------ILLD 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  85 dytaeglagvGELLKKYHHIsmELAhdpsdaniRIMSDLqeqldyqngwqfetriSQVLTLLNLDP--DATLDSLSGGWL 162
Cdd:cd03214    60 ----------GKDLASLSPK--ELA--------RKIAYV----------------PQALELLGLAHlaDRPFNELSGGER 103
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1411607396 163 RKVALARALACDPDLLLLDEPTNHLDI----EAINWLEDFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVITS 233
Cdd:cd03214   104 QRVLLARALAQEPPILLLDEPTSHLDIahqiELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVA 178
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
3-231 1.36e-29

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: 116.84  E-value: 1.36e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   3 LLTLHGACLSFSD----FPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRM---------VQQQDLKVT 69
Cdd:cd03257     1 LLEVKNLSVSFPTgggsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIifdgkdllkLSRRLRKIR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  70 RLE-----QDPPASSD--LTVFDYTAEGLAGVGELLKKyhhismelahdpsdanirimsdlqeqldyqngWQFETRISQV 142
Cdd:cd03257    81 RKEiqmvfQDPMSSLNprMTIGEQIAEPLRIHGKLSKK--------------------------------EARKEAVLLL 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 143 LTLLNLDPDAtLDS----LSGGWLRKVALARALACDPDLLLLDEPTNHLD----IEAINWLEDFLKDFRGAIVFISHDRE 214
Cdd:cd03257   129 LVGVGLPEEV-LNRypheLSGGQRQRVAIARALALNPKLLIADEPTSALDvsvqAQILDLLKKLQEELGLTLLFITHDLG 207
                         250
                  ....*....|....*..
gi 1411607396 215 FIHKLATRIIDLDRGVI 231
Cdd:cd03257   208 VVAKIADRVAVMYAGKI 224
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
3-231 1.56e-29

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: 122.70  E-value: 1.56e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   3 LLTLHGACLSF-----SDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRM-VQQQDLKVTRLE---- 72
Cdd:COG1123   260 LLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSIlFDGKDLTKLSRRslre 339
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  73 ---------QDPPASSD--LTVFDYTAEGLagvgellkkyhhismELAHDPSDANIRimsdlqeqldyqngwqfeTRISQ 141
Cdd:COG1123   340 lrrrvqmvfQDPYSSLNprMTVGDIIAEPL---------------RLHGLLSRAERR------------------ERVAE 386
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 142 VLTLLNLDPDAtLD----SLSGGWLRKVALARALACDPDLLLLDEPTNHLDI----EAINWLEDFLKDFRGAIVFISHDR 213
Cdd:COG1123   387 LLERVGLPPDL-ADryphELSGGQRQRVAIARALALEPKLLILDEPTSALDVsvqaQILNLLRDLQRELGLTYLFISHDL 465
                         250
                  ....*....|....*...
gi 1411607396 214 EFIHKLATRIIDLDRGVI 231
Cdd:COG1123   466 AVVRYIADRVAVMYDGRI 483
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
5-229 1.80e-29

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: 114.26  E-value: 1.80e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   5 TLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGrmvqqqdlKVTRLEQDPPASSDLTVF 84
Cdd:cd00267     1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSG--------EILIDGKDIAKLPLEELR 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  85 DytaeglagvgellkkyhHISMelahdpsdanirimsdlqeqldyqngwqfetrisqvltllnldpdatLDSLSGGWLRK 164
Cdd:cd00267    73 R-----------------RIGY-----------------------------------------------VPQLSGGQRQR 88
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1411607396 165 VALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRG---AIVFISHDREFIHKLATRIIDLDRG 229
Cdd:cd00267    89 VALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEegrTVIIVTHDPELAELAADRVIVLKDG 156
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
1-473 1.83e-29

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 122.43  E-value: 1.83e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   1 MALLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMVqqqdLKVTRLEQDPPASS- 79
Cdd:COG1129     2 EPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEIL----LDGEPVRFRSPRDAq 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  80 ---------------DLTVfdytAEGLAgVGELLKKYHHISMElahdpsdaniRIMSDLQEQLDyqngwqfetRISqvlt 144
Cdd:COG1129    78 aagiaiihqelnlvpNLSV----AENIF-LGREPRRGGLIDWR----------AMRRRARELLA---------RLG---- 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 145 lLNLDPDATLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRG---AIVFISHDREFIHKLAt 221
Cdd:COG1129   130 -LDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAqgvAIIYISHRLDEVFEIA- 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 222 riidlDRGVItswpgnydeylqgkeeaLR----VEELQHAEFDRklaqEEVwVRQ--GikarrtrnegrvRALEAMRMER 295
Cdd:COG1129   208 -----DRVTV-----------------LRdgrlVGTGPVAELTE----DEL-VRLmvG------------RELEDLFPKR 248
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 296 SQrrelqgkaklqmddvnRSGKLVFETEGLGLdfgdRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGL 375
Cdd:COG1129   249 AA----------------APGEVVLEVEGLSV----GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGE 308
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 376 VK-GGTKLE-----------VAYF--DQYRDQLDPEQTVMDNVGEGKQEVMVRGR-------SRHILGYLQDFLFEPKRA 434
Cdd:COG1129   309 IRlDGKPVRirsprdairagIAYVpeDRKGEGLVLDLSIRENITLASLDRLSRGGlldrrreRALAEEYIKRLRIKTPSP 388
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|
gi 1411607396 435 RTPVKALSGGEKNRLLLAK-LFLKPSnLLILDEPTNDLDV 473
Cdd:COG1129   389 EQPVGNLSGGNQQKVVLAKwLATDPK-VLILDEPTRGIDV 427
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
320-501 1.62e-28

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 112.99  E-value: 1.62e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 320 FETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGlvkggtklEVAYFDQYRDQLDPEQ- 398
Cdd:COG4619     1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSG--------EIYLDGKPLSAMPPPEw 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 399 ----------------TVMDNVGEGKQEVMVRGRSRHILGYLQDFLFEPKRARTPVKALSGGEKNRLLLAK-LFLKPSNL 461
Cdd:COG4619    73 rrqvayvpqepalwggTVRDNLPFPFQLRERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRaLLLQPDVL 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1411607396 462 LiLDEPTNDLDVETLELLEELLADYP----GTLLLVSHDRRFID 501
Cdd:COG4619   153 L-LDEPTSALDPENTRRVEELLREYLaeegRAVLWVSHDPEQIE 195
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
335-469 3.21e-28

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: 110.43  E-value: 3.21e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 335 FQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-----------GGTKLEVAYFDQYrDQLDPEQTVMDN 403
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILldgqdltdderKSLRKEIGYVFQD-PQLFPRLTVREN 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1411607396 404 VGEGKQEVMVRGRSR-----HILGYLQDFLFEPKRARTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTN 469
Cdd:pfam00005  80 LRLGLLLKGLSKREKdaraeEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
1-263 3.50e-28

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: 113.64  E-value: 3.50e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   1 MALLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPlddgrmvqqqdlkvtrleqdPPASSD 80
Cdd:COG1119     1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLP--------------------PTYGND 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  81 LTVFDYTAeGLAGVGELLKKYHHISMELAHD-PSDANIR--IMS------DLQEQLDYQNgwqfETRISQVLTLLNLDP- 150
Cdd:COG1119    61 VRLFGERR-GGEDVWELRKRIGLVSPALQLRfPRDETVLdvVLSgffdsiGLYREPTDEQ----RERARELLELLGLAHl 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 151 -DATLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEA----INWLEDFLKDFRGAIVFISHDREFIHKLATRIID 225
Cdd:COG1119   136 aDRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGArellLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLL 215
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1411607396 226 LDRGVITSwpgnydeylQG-KEEALRVEELQHAeFDRKL 263
Cdd:COG1119   216 LKDGRVVA---------AGpKEEVLTSENLSEA-FGLPV 244
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
4-232 7.29e-28

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: 109.83  E-value: 7.29e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   4 LTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMVqqqdlkvtrleqdppassdltv 83
Cdd:cd03216     1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEIL---------------------- 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  84 fdytaegLAGvgellKKYHHismelaHDPSDANirimsdlqeqldyQNGWQFetrISQvltllnldpdatldsLSGGWLR 163
Cdd:cd03216    59 -------VDG-----KEVSF------ASPRDAR-------------RAGIAM---VYQ---------------LSVGERQ 89
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1411607396 164 KVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRG---AIVFISHDREFIHKLATRIIDLDRGVIT 232
Cdd:cd03216    90 MVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAqgvAVIFISHRLDEVFEIADRVTVLRDGRVV 161
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...
1-248 1.04e-27

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: 112.44  E-value: 1.04e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   1 MALLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGR-MVQQQDlkVTRLeqdPPAS- 78
Cdd:COG0411     2 DPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRiLFDGRD--ITGL---PPHRi 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  79 ---------------SDLTVFDYTAeglagVGELLKKYHHISMELAHDPSDAniRIMSDLQEqldyqngwqfetRISQVL 143
Cdd:COG0411    77 arlgiartfqnprlfPELTVLENVL-----VAAHARLGRGLLAALLRLPRAR--REEREARE------------RAEELL 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 144 TLLNLDP--DATLDSLSGGWLRKVALARALACDPDLLLLDEPT---NHLDIEAINWLEDFLKDFRG-AIVFISHDREFIH 217
Cdd:COG0411   138 ERVGLADraDEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAaglNPEETEELAELIRRLRDERGiTILLIEHDMDLVM 217
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1411607396 218 KLATRIIDLDRG-VITSwpGNYDE----------YLqGKEEA 248
Cdd:COG0411   218 GLADRIVVLDFGrVIAE--GTPAEvradprvieaYL-GEEAA 256
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
319-503 1.43e-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: 110.26  E-value: 1.43e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 319 VFETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLV----KGGTKLEVAYFDQ--Y-- 390
Cdd:COG4133     2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVlwngEPIRDAREDYRRRlaYlg 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 391 -RDQLDPEQTVMDN---VGEGKQEVMVRGRSRHILGYLQdfLfePKRARTPVKALSGGEKNRLLLAKLFLKPSNLLILDE 466
Cdd:COG4133    82 hADGLKPELTVRENlrfWAALYGLRADREAIDEALEAVG--L--AGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDE 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1411607396 467 PTNDLDVETLELLEELLADYP---GTLLLVSHDRRFIDNT 503
Cdd:COG4133   158 PFTALDAAGVALLAELIAAHLargGAVLLTTHQPLELAAA 197
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
13-518 3.31e-27

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: 116.06  E-value: 3.31e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  13 FSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAG--ELPLDDGRMVQQQDL--KVTRLE-------QDPPASSDL 81
Cdd:TIGR03269  10 FDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIIYHVALceKCGYVErpskvgePCPVCGGTL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  82 TVFDYTAEGLA-GVGELLKKYHHI--------------------SMELAHDPSDANIRIMSDLQEQLdyqngwQFETRIS 140
Cdd:TIGR03269  90 EPEEVDFWNLSdKLRRRIRKRIAImlqrtfalygddtvldnvleALEEIGYEGKEAVGRAVDLIEMV------QLSHRIT 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 141 QVLTllnldpdatldSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFL----KDFRGAIVFISHDREFI 216
Cdd:TIGR03269 164 HIAR-----------DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALeeavKASGISMVLTSHWPEVI 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 217 HKLATRIIDLDRGVITSwPGNYDEYLQgkeealrveelqhaefdrklaqeevwvrqgikarrtrnegrvRALEAMRMERS 296
Cdd:TIGR03269 233 EDLSDKAIWLENGEIKE-EGTPDEVVA------------------------------------------VFMEGVSEVEK 269
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 297 QRRELQGKAKLQMDDVNRsgklvfetEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLV 376
Cdd:TIGR03269 270 ECEVEVGEPIIKVRNVSK--------RYISVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEV 341
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 377 ------------------KGGTKLEVAYFDQYRDqLDPEQTVMDNVGEG-----KQEVMVRgRSRHILGYLQdflFEPKR 433
Cdd:TIGR03269 342 nvrvgdewvdmtkpgpdgRGRAKRYIGILHQEYD-LYPHRTVLDNLTEAiglelPDELARM-KAVITLKMVG---FDEEK 416
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 434 ARTPVK----ALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLD----VETLELLEELLADYPGTLLLVSHDRRFIDNTVT 505
Cdd:TIGR03269 417 AEEILDkypdELSEGERHRVALAQVLIKEPRIVILDEPTGTMDpitkVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCD 496
                         570
                  ....*....|...
gi 1411607396 506 GCWLFEgDGRISD 518
Cdd:TIGR03269 497 RAALMR-DGKIVK 508
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
4-229 4.97e-27

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: 109.83  E-value: 4.97e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   4 LTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRmVQQQDLKVTRLE----------- 72
Cdd:cd03219     1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGS-VLFDGEDITGLPpheiarlgigr 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  73 --QDPPASSDLTVFdytaEGLAgVGELLKKYHHISMelahdpsDANIRIMSDLQEqldyqngwqfetRISQVLTLLNLDP 150
Cdd:cd03219    80 tfQIPRLFPELTVL----ENVM-VAAQARTGSGLLL-------ARARREEREARE------------RAEELLERVGLAD 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 151 --DATLDSLSGGWLRKVALARALACDPDLLLLDEPT---NHLDIEAI-NWLEDfLKDFRGAIVFISHDREFIHKLATRII 224
Cdd:cd03219   136 laDRPAGELSYGQQRRLEIARALATDPKLLLLDEPAaglNPEETEELaELIRE-LRERGITVLLVEHDMDVVMSLADRVT 214

                  ....*
gi 1411607396 225 DLDRG 229
Cdd:cd03219   215 VLDQG 219
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
330-524 5.44e-27

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: 115.42  E-value: 5.44e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 330 GDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKGGTKLEVAYFDQyRDQLDPEQTVMDNVGEGKQ 409
Cdd:TIGR03719  16 PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQ-EPQLDPTKTVRENVEEGVA 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 410 EVmvrgrsRHILGYLQ-------------DFLFEpKRAR------------------------------TPVKALSGGEK 446
Cdd:TIGR03719  95 EI------KDALDRFNeisakyaepdadfDKLAA-EQAElqeiidaadawdldsqleiamdalrcppwdADVTKLSGGER 167
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1411607396 447 NRLLLAKLFLKPSNLLILDEPTNDLDVETLELLEELLADYPGTLLLVSHDRRFIDNtVTGcWLFEGD-GRISDYVGGYA 524
Cdd:TIGR03719 168 RRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDN-VAG-WILELDrGRGIPWEGNYS 244
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
19-185 8.09e-27

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: 106.19  E-value: 8.09e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  19 LDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLD------DGRMVQQQDLKVTR-----LEQDPPASSDLTVFDyt 87
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTegtillDGQDLTDDERKSLRkeigyVFQDPQLFPRLTVRE-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  88 aeglagvgellkkyhhismelahdpsdaNIRIMSDLQEqldYQNGWqFETRISQVLTLLNLD------PDATLDSLSGGW 161
Cdd:pfam00005  79 ----------------------------NLRLGLLLKG---LSKRE-KDARAEEALEKLGLGdladrpVGERPGTLSGGQ 126
                         170       180
                  ....*....|....*....|....
gi 1411607396 162 LRKVALARALACDPDLLLLDEPTN 185
Cdd:pfam00005 127 RQRVAIARALLTKPKLLLLDEPTA 150
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
319-504 8.35e-27

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 109.41  E-value: 8.35e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 319 VFETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTKLE-----VAYFDQyRD 392
Cdd:COG1121     6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRlFGKPPRrarrrIGYVPQ-RA 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 393 QLDPEQ--TVMDNVGEG--KQEVMVRGRSRHI----------LGyLQDFlfepkrARTPVKALSGGEKNRLLLAKLFLKP 458
Cdd:COG1121    85 EVDWDFpiTVRDVVLMGryGRRGLFRRPSRADreavdealerVG-LEDL------ADRPIGELSGGQQQRVLLARALAQD 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1411607396 459 SNLLILDEPTNDLDVETLELLE---ELLADYPGTLLLVSHD----RRFIDNTV 504
Cdd:COG1121   158 PDLLLLDEPFAGVDAATEEALYellRELRREGKTILVVTHDlgavREYFDRVL 210
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
15-233 1.54e-26

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 107.83  E-value: 1.54e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  15 DFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGR-MVQQQDLkvTRLE---------------QDPPAS 78
Cdd:COG2884    14 GREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQvLVNGQDL--SRLKrreipylrrrigvvfQDFRLL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  79 SDLTVFDYTAeglagvgellkkyhhISMELA-HDPSDAnirimsdlqeqldyqngwqfETRISQVLTLLNLD------PD 151
Cdd:COG2884    92 PDRTVYENVA---------------LPLRVTgKSRKEI--------------------RRRVREVLDLVGLSdkakalPH 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 152 AtldsLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDF--RGAIVFI-SHDREFIHKLATRIIDLDR 228
Cdd:COG2884   137 E----LSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEInrRGTTVLIaTHDLELVDRMPKRVLELED 212

                  ....*
gi 1411607396 229 GVITS 233
Cdd:COG2884   213 GRLVR 217
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
330-545 1.72e-26

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 114.06  E-value: 1.72e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 330 GDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKGGTKLEVAYFDQyRDQLDPEQTVMDNVGEGKQ 409
Cdd:PRK11819   18 PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYLPQ-EPQLDPEKTVRENVEEGVA 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 410 EVM-VRGRSRHI-----------------LGYLQDFL-------FEPK--RA----RTP-----VKALSGGEKNRLLLAK 453
Cdd:PRK11819   97 EVKaALDRFNEIyaayaepdadfdalaaeQGELQEIIdaadawdLDSQleIAmdalRCPpwdakVTKLSGGERRRVALCR 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 454 LFLKPSNLLILDEPTNDLDVETLELLEELLADYPGTLLLVSHDRRFIDNtVTGcWLFEGD-GRISDYVGGYadmmatraq 532
Cdd:PRK11819  177 LLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDN-VAG-WILELDrGRGIPWEGNY--------- 245
                         250
                  ....*....|...
gi 1411607396 533 qSTQLAAKAAQVK 545
Cdd:PRK11819  246 -SSWLEQKAKRLA 257
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
1-231 3.17e-26

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 110.19  E-value: 3.17e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   1 MALLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGR-MVQQQDlkVTRLE------- 72
Cdd:COG3842     3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRiLLDGRD--VTGLPpekrnvg 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  73 ---QDPPASSDLTVFDYTAEGLagvgellkKYHHISmelahdPSDAnirimsdlqeqldyqngwqfETRISQVLTLLNLD 149
Cdd:COG3842    81 mvfQDYALFPHLTVAENVAFGL--------RMRGVP------KAEI--------------------RARVAELLELVGLE 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 150 ------PDAtldsLSGGWLRKVALARALACDPDLLLLDEPTNHLD----IEAINWLEDFLKDFRGAIVFISHDRE--FIh 217
Cdd:COG3842   127 gladryPHQ----LSGGQQQRVALARALAPEPRVLLLDEPLSALDaklrEEMREELRRLQRELGITFIYVTHDQEeaLA- 201
                         250
                  ....*....|....
gi 1411607396 218 kLATRIIDLDRGVI 231
Cdd:COG3842   202 -LADRIAVMNDGRI 214
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
2-250 4.35e-26

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: 106.99  E-value: 4.35e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   2 ALLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGR-MVQQQDL-KVTRLEQDPPAS- 78
Cdd:COG1127     4 PMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEiLVDGQDItGLSEKELYELRRr 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  79 -----------SDLTVFDytaeglaGVGELLKKYHHISMELAHDpsdanirimsdlqeqldyqngwqfetRISQVLTLLN 147
Cdd:COG1127    84 igmlfqggalfDSLTVFE-------NVAFPLREHTDLSEAEIRE--------------------------LVLEKLELVG 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 148 LDPDATL--DSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRGA----IVFISHDREFIHKLAT 221
Cdd:COG1127   131 LPGAADKmpSELSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDElgltSVVVTHDLDSAFAIAD 210
                         250       260
                  ....*....|....*....|....*....
gi 1411607396 222 RIIDLDRGVITsWPGNYDEYLQGKEEALR 250
Cdd:COG1127   211 RVAVLADGKII-AEGTPEELLASDDPWVR 238
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
34-474 6.77e-26

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 112.59  E-value: 6.77e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  34 LVGRNGAGKSTLMKIIAGELPLDDGRMvqqqdlkvtrleqDPPASSDlTVFDYTA--------EGLAGvGELlKKYHHIS 105
Cdd:PRK13409  104 ILGPNGIGKTTAVKILSGELIPNLGDY-------------EEEPSWD-EVLKRFRgtelqnyfKKLYN-GEI-KVVHKPQ 167
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 106 M-ELAHDPSDANIRimsDLQEQLDyQNGwqfetRISQVLTLLNLDP--DATLDSLSGGWLRKVALARALACDPDLLLLDE 182
Cdd:PRK13409  168 YvDLIPKVFKGKVR---ELLKKVD-ERG-----KLDEVVERLGLENilDRDISELSGGELQRVAIAAALLRDADFYFFDE 238
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 183 PTNHLDI----EAINWLEDFLKDfrGAIVFISHDrefihkLAtrIIDL--DR-----------GVITSWPGN---YDEYL 242
Cdd:PRK13409  239 PTSYLDIrqrlNVARLIRELAEG--KYVLVVEHD------LA--VLDYlaDNvhiaygepgayGVVSKPKGVrvgINEYL 308
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 243 QG--KEEALRV--EELqhaEFDrklaqeevwvrqgikarrtrnegrvraleamrmERSQRRELQGKAKLQMDDVNRS-GK 317
Cdd:PRK13409  309 KGylPEENMRIrpEPI---EFE---------------------------------ERPPRDESERETLVEYPDLTKKlGD 352
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 318 LVFETEGlGldfgdrtlfqgldlQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKggTKLEVAYFDQYRdQLDPE 397
Cdd:PRK13409  353 FSLEVEG-G--------------EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVD--PELKISYKPQYI-KPDYD 414
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 398 QTVMD---NVGEG------KQEVMVRgrsrhilgyLQ-DFLFEpkrarTPVKALSGGEKNRLLLAKLFLKPSNLLILDEP 467
Cdd:PRK13409  415 GTVEDllrSITDDlgssyyKSEIIKP---------LQlERLLD-----KNVKDLSGGELQRVAIAACLSRDADLYLLDEP 480

                  ....*..
gi 1411607396 468 TNDLDVE 474
Cdd:PRK13409  481 SAHLDVE 487
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
27-474 1.02e-25

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: 111.80  E-value: 1.02e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  27 ERGERLCLVGRNGAGKSTLMKIIAGEL-P----LDDG-------------------RMVQQQDLKVTRLEQdppassdlt 82
Cdd:COG1245    97 KKGKVTGILGPNGIGKSTALKILSGELkPnlgdYDEEpswdevlkrfrgtelqdyfKKLANGEIKVAHKPQ--------- 167
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  83 VFDYTAEGLAG-VGELLKKYhhismelahdpsdanirimsDLQEQLDYqngwqfetrisqVLTLLNLDP--DATLDSLSG 159
Cdd:COG1245   168 YVDLIPKVFKGtVRELLEKV--------------------DERGKLDE------------LAEKLGLENilDRDISELSG 215
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 160 GWLRKVALARALACDPDLLLLDEPTNHLDI-EAIN---WLEDFLKDFRgAIVFISHDrefihkLAtrIIDL--DRGVIT- 232
Cdd:COG1245   216 GELQRVAIAAALLRDADFYFFDEPSSYLDIyQRLNvarLIRELAEEGK-YVLVVEHD------LA--ILDYlaDYVHILy 286
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 233 SWPGNY-------------DEYLQG--KEEALRV--EELqhaEFDrklaqeevwvrqgikarrtrnegrvraleamrmER 295
Cdd:COG1245   287 GEPGVYgvvskpksvrvgiNQYLDGylPEENVRIrdEPI---EFE---------------------------------VH 330
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 296 SQRRELQGKAKLQMDDVNRS-GKLVFETEGlgldfgdrtlfqGldlQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRG 374
Cdd:COG1245   331 APRREKEEETLVEYPDLTKSyGGFSLEVEG------------G---EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEG 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 375 LVKggTKLEVAYFDQYRDQlDPEQTVMDnvgegkqevMVRGRSRHILG--YLQDFLFEP----KRARTPVKALSGGEKNR 448
Cdd:COG1245   396 EVD--EDLKISYKPQYISP-DYDGTVEE---------FLRSANTDDFGssYYKTEIIKPlgleKLLDKNVKDLSGGELQR 463
                         490       500
                  ....*....|....*....|....*.
gi 1411607396 449 LLLAKLFLKPSNLLILDEPTNDLDVE 474
Cdd:COG1245   464 VAIAACLSRDADLYLLDEPSAHLDVE 489
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
6-250 1.10e-25

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: 106.05  E-value: 1.10e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   6 LHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRM---------VQQQDLKVTRLE---- 72
Cdd:cd03261     3 LRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVlidgedisgLSEAELYRLRRRmgml 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  73 -QDPPASSDLTVFDYTAEGLagvgellkkyhhismelahdpsdaniRIMSDLQEqldyqngWQFETRISQVLTLLNLDPD 151
Cdd:cd03261    83 fQSGALFDSLTVFENVAFPL--------------------------REHTRLSE-------EEIREIVLEKLEAVGLRGA 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 152 ATL--DSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRGA----IVFISHDREFIHKLATRIID 225
Cdd:cd03261   130 EDLypAELSGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKElgltSIMVTHDLDTAFAIADRIAV 209
                         250       260
                  ....*....|....*....|....*
gi 1411607396 226 LDRGVITsWPGNYDEYLQGKEEALR 250
Cdd:cd03261   210 LYDGKIV-AEGTPEELRASDDPLVR 233
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
12-231 1.19e-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: 104.99  E-value: 1.19e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  12 SFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGrmvqqqdlKVTRLEQDppassdltvFDYTAEGL 91
Cdd:cd03268     9 TYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSG--------EITFDGKS---------YQKNIEAL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  92 AGVGELLkKYHHISMEL-AHDpsdaNIRImSDLQEQLDYQngwqfetRISQVLTLLNLD--PDATLDSLSGGWLRKVALA 168
Cdd:cd03268    72 RRIGALI-EAPGFYPNLtARE----NLRL-LARLLGIRKK-------RIDEVLDVVGLKdsAKKKVKGFSLGMKQRLGIA 138
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1411607396 169 RALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFR--GAIVFI-SHDREFIHKLATRIIDLDRGVI 231
Cdd:cd03268   139 LALLGNPDLLILDEPTNGLDPDGIKELRELILSLRdqGITVLIsSHLLSEIQKVADRIGIINKGKL 204
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
1-236 3.67e-25

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


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 105.17  E-value: 3.67e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   1 MALLTLHGACLSF----SDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRmVQQQDLKVTRLE---- 72
Cdd:COG1116     5 APALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGE-VLVDGKPVTGPGpdrg 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  73 ---QDP---PAssdLTVFDYTAEGLAGVGELLKKYHHISMELahdpsdanirimsdlqeqldyqngwqfetrisqvLTLL 146
Cdd:COG1116    84 vvfQEPallPW---LTVLDNVALGLELRGVPKAERRERAREL----------------------------------LELV 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 147 NLDPDATL--DSLSGGWLRKVALARALACDPDLLLLDEPTNHLDieAI------NWLEDFLKDFRGAIVFISHD-REFIH 217
Cdd:COG1116   127 GLAGFEDAypHQLSGGMRQRVAIARALANDPEVLLMDEPFGALD--ALtrerlqDELLRLWQETGKTVLFVTHDvDEAVF 204
                         250
                  ....*....|....*....
gi 1411607396 218 kLATRIIdldrgVITSWPG 236
Cdd:COG1116   205 -LADRVV-----VLSARPG 217
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
16-231 1.03e-24

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: 102.57  E-value: 1.03e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  16 FPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRM-VQQQD---LKVTRLE-----------QDPPASSD 80
Cdd:cd03255    17 VQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVrVDGTDiskLSEKELAafrrrhigfvfQSFNLLPD 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  81 LTVFDYTAeglagvgellkkyhhISMELAHDPSDANirimsdlqeqldyqngwqfETRISQVLTLLNLDPDATL--DSLS 158
Cdd:cd03255    97 LTALENVE---------------LPLLLAGVPKKER-------------------RERAEELLERVGLGDRLNHypSELS 142
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1411607396 159 GGWLRKVALARALACDPDLLLLDEPTNHLDIEA----INWLEDFLKDFRGAIVFISHDREFIhKLATRIIDLDRGVI 231
Cdd:cd03255   143 GGQQQRVAIARALANDPKIILADEPTGNLDSETgkevMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
4-229 1.13e-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: 101.11  E-value: 1.13e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   4 LTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGelplddgrmvqqqdlkvtrLEqdPPASSDLTV 83
Cdd:cd03229     1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAG-------------------LE--EPDSGSILI 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  84 FDytaEGLAGVGELLKkyhhismelahdPSDANIRIMsdlqeqldYQNGwqfetrisQVLTLLNLDPDATLdSLSGGWLR 163
Cdd:cd03229    60 DG---EDLTDLEDELP------------PLRRRIGMV--------FQDF--------ALFPHLTVLENIAL-GLSGGQQQ 107
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 164 KVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRG----AIVFISHDREFIHKLATRIIDLDRG 229
Cdd:cd03229   108 RVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAqlgiTVVLVTHDLDEAARLADRVVVLRDG 177
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
12-231 1.16e-24

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


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 105.61  E-value: 1.16e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  12 SFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAG-ELPlDDGRM----------VQQQDLKVTRLEQDPPASSD 80
Cdd:COG1118    11 RFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGlETP-DSGRIvlngrdlftnLPPRERRVGFVFQHYALFPH 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  81 LTVFDYTAEGLAgvgellkkyhhismelAHDPSDANIRimsdlqeqldyqngwqfeTRISQVLTLLNLD------PDAtl 154
Cdd:COG1118    90 MTVAENIAFGLR----------------VRPPSKAEIR------------------ARVEELLELVQLEgladryPSQ-- 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 155 dsLSGGWLRKVALARALACDPDLLLLDEPTNHLD------IEAinWLEDFLKDFRGAIVFISHDREFIHKLATRIIDLDR 228
Cdd:COG1118   134 --LSGGQRQRVALARALAVEPEVLLLDEPFGALDakvrkeLRR--WLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQ 209

                  ...
gi 1411607396 229 GVI 231
Cdd:COG1118   210 GRI 212
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
4-236 1.29e-24

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: 102.16  E-value: 1.29e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   4 LTLHGACLSFSD----FPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLD------DGRMVQQQDLKVTRLEQ 73
Cdd:cd03293     1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTsgevlvDGEPVTGPGPDRGYVFQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  74 DP---PAssdLTVFDYTAEGLAGVGellkkyhhismelaHDPSDAnirimsdlqeqldyqngwqfETRISQVLTLLNLDP 150
Cdd:cd03293    81 QDallPW---LTVLDNVALGLELQG--------------VPKAEA--------------------RERAEELLELVGLSG 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 151 --DATLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLD----IEAINWLEDFLKDFRGAIVFISHD-REFIHkLATRI 223
Cdd:cd03293   124 feNAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDaltrEQLQEELLDIWRETGKTVLLVTHDiDEAVF-LADRV 202
                         250
                  ....*....|...
gi 1411607396 224 IdldrgVITSWPG 236
Cdd:cd03293   203 V-----VLSARPG 210
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
321-515 2.39e-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: 101.39  E-value: 2.39e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 321 ETEGLGLDFGD--RTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTKLEVAYFDQYRDQL--- 394
Cdd:cd03225     1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLvDGKDLTKLSLKELRRKVglv 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 395 --DPE-QTVMDNVGEgkqEVMV----RGRSRH-----ILGYLQDFLFEPKRARtPVKALSGGEKNRLLLAK-LFLKPsNL 461
Cdd:cd03225    81 fqNPDdQFFGPTVEE---EVAFglenLGLPEEeieerVEEALELVGLEGLRDR-SPFTLSGGQKQRVAIAGvLAMDP-DI 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1411607396 462 LILDEPTNDLDVETLELLEELLADYPG---TLLLVSHDRRFIDNTVTGCWLFEgDGR 515
Cdd:cd03225   156 LLLDEPTAGLDPAGRRELLELLKKLKAegkTIIIVTHDLDLLLELADRVIVLE-DGK 211
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
321-502 3.88e-24

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: 98.86  E-value: 3.88e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVkggtklevaYFDqyrdqldpeqtv 400
Cdd:cd00267     1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEI---------LID------------ 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 401 mdnvGEGKQEVMVRGRSRHILgylqdFLFEpkrartpvkaLSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVETLELLE 480
Cdd:cd00267    60 ----GKDIAKLPLEELRRRIG-----YVPQ----------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLL 120
                         170       180
                  ....*....|....*....|....*
gi 1411607396 481 ELLADYPG---TLLLVSHDRRFIDN 502
Cdd:cd00267   121 ELLRELAEegrTVIIVTHDPELAEL 145
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
321-496 5.76e-24

ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.


Pssm-ID: 213202 [Multi-domain]  Cd Length: 213  Bit Score: 100.30  E-value: 5.76e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK------GGTKLEVAYFDQYRDqL 394
Cdd:cd03235     1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRvfgkplEKERKRIGYVPQRRS-I 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 395 DPEQ--TVMDNVGEGKqevmvRGRSRHILGYLQDflfEPKRART-------------PVKALSGGEKNRLLLAKLFLKPS 459
Cdd:cd03235    80 DRDFpiSVRDVVLMGL-----YGHKGLFRRLSKA---DKAKVDEalervglseladrQIGELSGGQQQRVLLARALVQDP 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1411607396 460 NLLILDEPTNDLDVETLELLEELLADYPG---TLLLVSHD 496
Cdd:cd03235   152 DLLLLDEPFAGVDPKTQEDIYELLRELRRegmTILVVTHD 191
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
330-495 7.25e-24

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


Pssm-ID: 213195 [Multi-domain]  Cd Length: 171  Bit Score: 98.61  E-value: 7.25e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 330 GDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTKLEVAYFDQYRDQL-----DP---EQTV 400
Cdd:cd03228    13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILiDGVDLRDLDLESLRKNIayvpqDPflfSGTI 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 401 MDNVgegkqevmvrgrsrhilgylqdflfepkrartpvkaLSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVETLELLE 480
Cdd:cd03228    93 RENI------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALIL 136
                         170
                  ....*....|....*..
gi 1411607396 481 ELLADYPG--TLLLVSH 495
Cdd:cd03228   137 EALRALAKgkTVIVIAH 153
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
330-496 8.11e-24

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: 106.00  E-value: 8.11e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 330 GDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTKLEVAYFDQYRDQL-----DP---EQTV 400
Cdd:COG4988   348 GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILiNGVDLSDLDPASWRRQIawvpqNPylfAGTI 427
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 401 MDNVGEGKQEVmvrgrSRHIL------GYLQDFLFE-PKRARTPV----KALSGGEKNRLLLAKLFLKPSNLLILDEPTN 469
Cdd:COG4988   428 RENLRLGRPDA-----SDEELeaaleaAGLDEFVAAlPDGLDTPLgeggRGLSGGQAQRLALARALLRDAPLLLLDEPTA 502
                         170       180
                  ....*....|....*....|....*....
gi 1411607396 470 DLDVETLELLEELLADYPG--TLLLVSHD 496
Cdd:COG4988   503 HLDAETEAEILQALRRLAKgrTVILITHR 531
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
321-475 1.39e-23

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: 97.85  E-value: 1.39e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGlvkggtklEVAYFDQyrdqldpeqtv 400
Cdd:cd03230     2 EVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSG--------EIKVLGK----------- 62
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1411607396 401 mdNVGEGKQEVmvrgrsRHILGYL--QDFLFEPKRARTPVKaLSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVET 475
Cdd:cd03230    63 --DIKKEPEEV------KRRIGYLpeEPSLYENLTVRENLK-LSGGMKQRLALAQALLHDPELLILDEPTSGLDPES 130
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
321-496 1.42e-23

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 99.75  E-value: 1.42e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTKLE---------VAYFDQY 390
Cdd:COG1131     2 EVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRvLGEDVArdpaevrrrIGYVPQE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 391 rDQLDPEQTVMDNV-------GEGKQEVMVRgrsrhILGYLQDFLFEPkRARTPVKALSGGEKNRLLLAKLFLKPSNLLI 463
Cdd:COG1131    82 -PALYPDLTVRENLrffarlyGLPRKEARER-----IDELLELFGLTD-AADRKVGTLSGGMKQRLGLALALLHDPELLI 154
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1411607396 464 LDEPTNDLDVETLEL---LEELLADYPGTLLLVSHD 496
Cdd:COG1131   155 LDEPTSGLDPEARRElweLLRELAAEGKTVLLSTHY 190
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
17-243 1.96e-23

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: 105.30  E-value: 1.96e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  17 PLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRM------VQQQDLKVTR-----LEQDPPASSDlTVFD 85
Cdd:COG2274   489 PVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRIlidgidLRQIDPASLRrqigvVLQDVFLFSG-TIRE 567
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  86 ytaeglagvgellkkyhHISMElAHDPSDANIR-------IMSDLQEQldyQNGwqFETRISqvltllnldPDATldSLS 158
Cdd:COG2274   568 -----------------NITLG-DPDATDEEIIeaarlagLHDFIEAL---PMG--YDTVVG---------EGGS--NLS 613
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 159 GGWLRKVALARALACDPDLLLLDEPTNHLDIE---AINwleDFLKDFRG--AIVFISHDREFIhKLATRIIDLDRGVITS 233
Cdd:COG2274   614 GGQRQRLAIARALLRNPRILILDEATSALDAEteaIIL---ENLRRLLKgrTVIIIAHRLSTI-RLADRIIVLDKGRIVE 689
                         250
                  ....*....|
gi 1411607396 234 wPGNYDEYLQ 243
Cdd:COG2274   690 -DGTHEELLA 698
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
4-243 1.98e-23

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: 104.45  E-value: 1.98e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   4 LTLHGACLSFSD-FPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGR-MVQQQDL----------KVTRL 71
Cdd:COG4988   337 IELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSiLINGVDLsdldpaswrrQIAWV 416
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  72 EQDPpassdlTVFDYT-AEGLAgvgellkkyhhismeLAH-DPSDAnirimsDLQEQLDyqngwqfETRISQVLTLLNLD 149
Cdd:COG4988   417 PQNP------YLFAGTiRENLR---------------LGRpDASDE------ELEAALE-------AAGLDEFVAALPDG 462
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 150 PDATLDS----LSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKD-FRGAIV-FISHDREFIhKLATRI 223
Cdd:COG4988   463 LDTPLGEggrgLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRlAKGRTViLITHRLALL-AQADRI 541
                         250       260
                  ....*....|....*....|
gi 1411607396 224 IDLDRGVITSwPGNYDEYLQ 243
Cdd:COG4988   542 LVLDDGRIVE-QGTHEELLA 560
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
15-231 2.75e-23

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: 98.25  E-value: 2.75e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  15 DFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAG-ELPLDDGRMVQQQDL------KVTRLE-------QDPPASSD 80
Cdd:cd03292    13 GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKeELPTSGTIRVNGQDVsdlrgrAIPYLRrkigvvfQDFRLLPD 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  81 LTVFDYTAeglagvgellkkyhhISMELA-HDPSDANirimsdlqeqldyqngwqfeTRISQVLTLLNLD--PDATLDSL 157
Cdd:cd03292    93 RNVYENVA---------------FALEVTgVPPREIR--------------------KRVPAALELVGLShkHRALPAEL 137
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1411607396 158 SGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDF--RGAIVFIS-HDREFIHKLATRIIDLDRGVI 231
Cdd:cd03292   138 SGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKInkAGTTVVVAtHAKELVDTTRHRVIALERGKL 214
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
280-497 5.42e-23

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: 103.14  E-value: 5.42e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 280 RNEGRVRALEAMRMERSQRRELQGKAKLQMDDvnrSGKLVFEteGLGLDFGDRT-LFQGLDLQVLRGDKIALVGPNGCGK 358
Cdd:TIGR02857 287 RADGVAAAEALFAVLDAAPRPLAGKAPVTAAP---ASSLEFS--GVSVAYPGRRpALRPVSFTVPPGERVALVGPSGAGK 361
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 359 STLIKLLLGQLEPSRGLVK-GGTKLEVAYFDQYRDQLD--------PEQTVMDNVGEGKQEV---MVRGRSRhiLGYLQD 426
Cdd:TIGR02857 362 STLLNLLLGFVDPTEGSIAvNGVPLADADADSWRDQIAwvpqhpflFAGTIAENIRLARPDAsdaEIREALE--RAGLDE 439
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1411607396 427 FLFE-PKRARTPV----KALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVETLELLEELLADYPG--TLLLVSHDR 497
Cdd:TIGR02857 440 FVAAlPQGLDTPIgeggAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQgrTVLLVTHRL 517
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
321-496 9.00e-23

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


Pssm-ID: 213181 [Multi-domain]  Cd Length: 180  Bit Score: 95.97  E-value: 9.00e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTKLEvayfdqyrdQLDPEQt 399
Cdd:cd03214     1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILlDGKDLA---------SLSPKE- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 400 vmdnvgegkqevmvrgRSRHIlGYLQDFL----FEPKRARtPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLD--- 472
Cdd:cd03214    71 ----------------LARKI-AYVPQALellgLAHLADR-PFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDiah 132
                         170       180
                  ....*....|....*....|....*
gi 1411607396 473 -VETLELLEELLADYPGTLLLVSHD 496
Cdd:cd03214   133 qIELLELLRRLARERGKTVVMVLHD 157
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
14-231 1.56e-22

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: 96.88  E-value: 1.56e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  14 SDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGelplddgrmvqqqdlkvtrLEQdpPASSDLTVFDYTAEGLAG 93
Cdd:cd03258    16 GKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCING-------------------LER--PTSGSVLVDGTDLTLLSG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  94 vGELLKKYHHISMELAHdpsdANIrimsdLQEQLDYQN--------GWQFETRISQVLTLLNL-----DPDATLDSLSGG 160
Cdd:cd03258    75 -KELRKARRRIGMIFQH----FNL-----LSSRTVFENvalpleiaGVPKAEIEERVLELLELvgledKADAYPAQLSGG 144
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1411607396 161 WLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKD----FRGAIVFISHDREFIHKLATRIIDLDRGVI 231
Cdd:cd03258   145 QKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDinreLGLTIVLITHEMEVVKRICDRVAVMEKGEV 219
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
330-516 1.60e-22

Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];


Pssm-ID: 440739 [Multi-domain]  Cd Length: 230  Bit Score: 96.63  E-value: 1.60e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 330 GDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTKLEVAYFDQYRDQL-----DPEQ----- 398
Cdd:COG1122    12 GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLvDGKDITKKNLRELRRKVglvfqNPDDqlfap 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 399 TVMDNV-------GEGKQEvmVRGRSRHILGY--LQDFlfepkrARTPVKALSGGEKNRLLLAK-LFLKPSnLLILDEPT 468
Cdd:COG1122    92 TVEEDVafgpenlGLPREE--IRERVEEALELvgLEHL------ADRPPHELSGGQKQRVAIAGvLAMEPE-VLVLDEPT 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1411607396 469 NDLDVETLELLEELLADYPG---TLLLVSHDRRFIDNTVTGCWLFEgDGRI 516
Cdd:COG1122   163 AGLDPRGRRELLELLKRLNKegkTVIIVTHDLDLVAELADRVIVLD-DGRI 212
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
8-231 3.39e-22

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: 95.87  E-value: 3.39e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   8 GACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAG-ELPlDDGRMVQQ---------QDLKVTRLEQDPPA 77
Cdd:cd03296     7 NVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGlERP-DSGTILFGgedatdvpvQERNVGFVFQHYAL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  78 SSDLTVFDYTAEGLagvgELLKKyhhismelAHDPSDANIRimsdlqeqldyqngwqfeTRISQVLTLLNLD--PDATLD 155
Cdd:cd03296    86 FRHMTVFDNVAFGL----RVKPR--------SERPPEAEIR------------------AKVHELLKLVQLDwlADRYPA 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 156 SLSGGWLRKVALARALACDPDLLLLDEPTNHLDI----EAINWLEDFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVI 231
Cdd:cd03296   136 QLSGGQRQRVALARALAVEPKVLLLDEPFGALDAkvrkELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRI 215
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
2-233 3.71e-22

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 95.50  E-value: 3.71e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   2 ALLTLHGACLSF----SDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGR-MVQQQDlkVTRLeqdpp 76
Cdd:COG1136     3 PLLELRNLTKSYgtgeGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEvLIDGQD--ISSL----- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  77 ASSDLTVF--DYtaeglagVGELLKKYHHISmEL-AHDpsdaNIRIMSDLQEQLDYQNgwqfETRISQVLTLLNLDP--D 151
Cdd:COG1136    76 SERELARLrrRH-------IGFVFQFFNLLP-ELtALE----NVALPLLLAGVSRKER----RERARELLERVGLGDrlD 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 152 ATLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLD----IEAINWLEDFLKDFRGAIVFISHDREFIhKLATRIIDLD 227
Cdd:COG1136   140 HRPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDsktgEEVLELLRELNRELGTTIVMVTHDPELA-ARADRVIRLR 218

                  ....*.
gi 1411607396 228 RGVITS 233
Cdd:COG1136   219 DGRIVS 224
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
4-231 5.93e-22

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: 94.63  E-value: 5.93e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   4 LTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMVqQQDLKVTRLeqdPPASSDL-- 81
Cdd:cd03301     1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIY-IGGRDVTDL---PPKDRDIam 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  82 -----------TVFDYTAEGLagvgellkkyhhismELAHDPSDANIRIMSDLQEQLdyqngwqfetRISQvltLLNLDP 150
Cdd:cd03301    77 vfqnyalyphmTVYDNIAFGL---------------KLRKVPKDEIDERVREVAELL----------QIEH---LLDRKP 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 151 DAtldsLSGGWLRKVALARALACDPDLLLLDEPTNHLD----IEAINWLEDFLKDFRGAIVFISHDREFIHKLATRIIDL 226
Cdd:cd03301   129 KQ----LSGGQRQRVALGRAIVREPKVFLMDEPLSNLDaklrVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVM 204

                  ....*
gi 1411607396 227 DRGVI 231
Cdd:cd03301   205 NDGQI 209
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
330-532 7.07e-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: 99.84  E-value: 7.07e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 330 GDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTKLE----------VAYFDQ--Y------ 390
Cdd:COG4987   346 AGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITlGGVDLRdldeddlrrrIAVVPQrpHlfdttl 425
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 391 -------RDQLDPEQ--TVMDNVGegkqevmvrgrsrhilgyLQDFLFE-PKRARTPV----KALSGGEKNRLLLAKLFL 456
Cdd:COG4987   426 renlrlaRPDATDEElwAALERVG------------------LGDWLAAlPDGLDTWLgeggRRLSGGERRRLALARALL 487
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1411607396 457 KPSNLLILDEPTNDLDVETLELLEELLADYPG--TLLLVSHDRRFIDNTVTGCWLfeGDGRISDyVGGYADMMATRAQ 532
Cdd:COG4987   488 RDAPILLLDEPTEGLDAATEQALLADLLEALAgrTVLLITHRLAGLERMDRILVL--EDGRIVE-QGTHEELLAQNGR 562
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
1-473 1.15e-21

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: 98.99  E-value: 1.15e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   1 MALLTLHGACLSF----SDFPLLDNAELSIERGERLCLVGRNGAGKS----TLMKIIAGELPLDDGRMV-QQQDL----- 66
Cdd:COG4172     4 MPLLSVEDLSVAFgqggGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILfDGQDLlglse 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  67 ---------KVTRLEQDPPASSD--LTVFDYTAEGLAgvgellkkyHHISMelahdpSDANIRimsdlqeqldyqngwqf 135
Cdd:COG4172    84 relrrirgnRIAMIFQEPMTSLNplHTIGKQIAEVLR---------LHRGL------SGAAAR----------------- 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 136 etriSQVLTLLNL----DPDATLDS----LSGGWLRKVALARALACDPDLLLLDEPTNHLD--IEA--INWLEDFLKDFR 203
Cdd:COG4172   132 ----ARALELLERvgipDPERRLDAyphqLSGGQRQRVMIAMALANEPDLLIADEPTTALDvtVQAqiLDLLKDLQRELG 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 204 GAIVFISHDREFIHKLATRIIDLDRGVITswpgnydeylqgkeEALRVEEL----QHAeFDRKLaqeevwvrqgIKArrt 279
Cdd:COG4172   208 MALLLITHDLGVVRRFADRVAVMRQGEIV--------------EQGPTAELfaapQHP-YTRKL----------LAA--- 259
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 280 RNEGRVRALEAmrmersqrrelqgkaklqmddvnrSGKLVFETEGLGLDF-GDRTLFQ----------GLDLQVLRGDKI 348
Cdd:COG4172   260 EPRGDPRPVPP------------------------DAPPLLEARDLKVWFpIKRGLFRrtvghvkavdGVSLTLRRGETL 315
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 349 ALVGPNGCGKSTLIKLLLGqLEPSRGLVK-GGTKLEVAYFDQ---YRDQ-----------LDPEQTVMDNVGEG----KQ 409
Cdd:COG4172   316 GLVGESGSGKSTLGLALLR-LIPSEGEIRfDGQDLDGLSRRAlrpLRRRmqvvfqdpfgsLSPRMTVGQIIAEGlrvhGP 394
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1411607396 410 EVMVRGRSRHILGYLQDFLFEPK-RARTPvKALSGGEKNRLLLAK-LFLKPSnLLILDEPTNDLDV 473
Cdd:COG4172   395 GLSAAERRARVAEALEEVGLDPAaRHRYP-HEFSGGQRQRIAIARaLILEPK-LLVLDEPTSALDV 458
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
2-243 1.20e-21

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: 99.07  E-value: 1.20e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   2 ALLTLHGACLSF--SDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRM---------VQQQDL--KV 68
Cdd:COG4987   332 PSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSItlggvdlrdLDEDDLrrRI 411
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  69 TRLEQDPPassdltVFDYTaeglagVGELLKkyhhismeLA-HDPSDANIRimsdlqeqldyqngwqfetrisQVLTLLN 147
Cdd:COG4987   412 AVVPQRPH------LFDTT------LRENLR--------LArPDATDEELW----------------------AALERVG 449
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 148 LDPDAT-----LDS--------LSGGWLRKVALARALACDPDLLLLDEPTNHLDIE-AINWLEDFLKDFRG-AIVFISHD 212
Cdd:COG4987   450 LGDWLAalpdgLDTwlgeggrrLSGGERRRLALARALLRDAPILLLDEPTEGLDAAtEQALLADLLEALAGrTVLLITHR 529
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1411607396 213 REFIHKlATRIIDLDRGVITSwPGNYDEYLQ 243
Cdd:COG4987   530 LAGLER-MDRILVLEDGRIVE-QGTHEELLA 558
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
319-496 1.27e-21

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: 94.73  E-value: 1.27e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 319 VFETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTKLE----------VAYF 387
Cdd:COG1120     1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLlDGRDLAslsrrelarrIAYV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 388 DQyrDQLDPEQ-TVMDNVGegkqevmvRGRSRHilgylQDFLFEPKR------------------ARTPVKALSGGEKNR 448
Cdd:COG1120    81 PQ--EPPAPFGlTVRELVA--------LGRYPH-----LGLFGRPSAedreaveealertglehlADRPVDELSGGERQR 145
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1411607396 449 LLLAKLFLKPSNLLILDEPTNDLD----VETLELLEELLADYPGTLLLVSHD 496
Cdd:COG1120   146 VLIARALAQEPPLLLLDEPTSHLDlahqLEVLELLRRLARERGRTVVMVLHD 197
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
7-256 1.39e-21

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: 98.85  E-value: 1.39e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   7 HGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMVQQQDLKVTRLEQ-----DPpassDL 81
Cdd:TIGR03719 326 ENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQsrdalDP----NK 401
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  82 TVFDYTAEGLagvgellkkyHHISMELAHDPSDANIrimsdlqEQLDYQNGWQfETRISQvltllnldpdatldsLSGGW 161
Cdd:TIGR03719 402 TVWEEISGGL----------DIIKLGKREIPSRAYV-------GRFNFKGSDQ-QKKVGQ---------------LSGGE 448
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 162 LRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRGAIVFISHDREFIHKLATRIIDLD-RGVITSWPGNYDE 240
Cdd:TIGR03719 449 RNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIATHILAFEgDSHVEWFEGNFSE 528
                         250       260
                  ....*....|....*....|.
gi 1411607396 241 YLQGK-----EEALRVEELQH 256
Cdd:TIGR03719 529 YEEDKkrrlgEDADQPHRIKY 549
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
3-473 1.71e-21

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 98.18  E-value: 1.71e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   3 LLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMV---QQQDLKvtrleqDPPASS 79
Cdd:COG3845     5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILidgKPVRIR------SPRDAI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  80 D---------------LTVfdytAEGLAgvgellkkyhhismeLAHDPSDANIRIMSDLQEQLdyqngwqfeTRISQVLT 144
Cdd:COG3845    79 AlgigmvhqhfmlvpnLTV----AENIV---------------LGLEPTKGGRLDRKAARARI---------RELSERYG 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 145 lLNLDPDATLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRG---AIVFISHD-REfIHKLA 220
Cdd:COG3845   131 -LDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAegkSIIFITHKlRE-VMAIA 208
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 221 TRIIDLDRG-VITSwpgnydeylqgkeeaLRVEELQHAEfdrkLAQEEVwvrqgikarrtrneGRVRALEAMRMERsqrr 299
Cdd:COG3845   209 DRVTVLRRGkVVGT---------------VDTAETSEEE----LAELMV--------------GREVLLRVEKAPA---- 251
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 300 elqgkaklqmddvnRSGKLVFETEGLGL--DFGDRTLfQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK 377
Cdd:COG3845   252 --------------EPGEVVLEVENLSVrdDRGVPAL-KDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIR 316
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 378 -GGTKLE-----------VAYF--DQYRDQLDPEQTVMDNV--GEGKQEVMVRG---RSRHILGYLQDfLFE-----PKR 433
Cdd:COG3845   317 lDGEDITglsprerrrlgVAYIpeDRLGRGLVPDMSVAENLilGRYRRPPFSRGgflDRKAIRAFAEE-LIEefdvrTPG 395
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|
gi 1411607396 434 ARTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDV 473
Cdd:COG3845   396 PDTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDV 435
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
1-231 2.95e-21

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


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 95.53  E-value: 2.95e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   1 MALLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRM-VQQQDlkVTRLeqdPPASS 79
Cdd:COG3839     1 MASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEIlIGGRD--VTDL---PPKDR 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  80 D-------------LTVFDYTAEGL--AGVgellkkyhhismelahdpSDANIRimsdlqeqldyqngwqfeTRISQVLT 144
Cdd:COG3839    76 NiamvfqsyalyphMTVYENIAFPLklRKV------------------PKAEID------------------RRVREAAE 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 145 LLNLDPdaTLD----SLSGGWLRKVALARALACDPDLLLLDEPTNHLD----IEAINWLEDFLKDFRGAIVFISHDREFI 216
Cdd:COG3839   120 LLGLED--LLDrkpkQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDaklrVEMRAEIKRLHRRLGTTTIYVTHDQVEA 197
                         250
                  ....*....|....*
gi 1411607396 217 HKLATRIIDLDRGVI 231
Cdd:COG3839   198 MTLADRIAVMNDGRI 212
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
16-231 5.11e-21

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: 92.75  E-value: 5.11e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  16 FPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRM-VQQQDLKvtrlEQDPPassdltvfdytaeglagv 94
Cdd:cd03295    14 KKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIfIDGEDIR----EQDPV------------------ 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  95 gELLKKYHHISME---LAHDPSDANIRIMSDLQeqldyqnGW---QFETRISQVLTLLNLDPDATLD----SLSGGWLRK 164
Cdd:cd03295    72 -ELRRKIGYVIQQiglFPHMTVEENIALVPKLL-------KWpkeKIRERADELLALVGLDPAEFADryphELSGGQQQR 143
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1411607396 165 VALARALACDPDLLLLDEPTNHLD-IEAINWLEDFLK---DFRGAIVFISHDREFIHKLATRIIDLDRGVI 231
Cdd:cd03295   144 VGVARALAADPPLLLMDEPFGALDpITRDQLQEEFKRlqqELGKTIVFVTHDIDEAFRLADRIAIMKNGEI 214
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
5-232 1.17e-20

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: 90.39  E-value: 1.17e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   5 TLHGACLSFSDFP-LLDNAELSIERGERLCLVGRNGAGKSTLMKIIAG-------ELPLDDGRMVQQQDLKVTRL-EQDP 75
Cdd:cd03226     1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGlikessgSILLNGKPIKAKERRKSIGYvMQDV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  76 passDLTVFDYTAEGlagvgELLkkyhhISMELAHDPsdanirimsdlqeqldyqngwqfETRISQVLTLLNLD--PDAT 153
Cdd:cd03226    81 ----DYQLFTDSVRE-----ELL-----LGLKELDAG-----------------------NEQAETVLKDLDLYalKERH 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 154 LDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRG---AIVFISHDREFIHKLATRIIDLDRGV 230
Cdd:cd03226   124 PLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAqgkAVIVITHDYEFLAKVCDRVLLLANGA 203

                  ..
gi 1411607396 231 IT 232
Cdd:cd03226   204 IV 205
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
11-229 1.21e-20

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: 89.36  E-value: 1.21e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  11 LSFS----DFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRM-VQQQDLKvtrleqdppassDLTVFD 85
Cdd:cd03228     6 VSFSypgrPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEIlIDGVDLR------------DLDLES 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  86 YtaeglagvgellkkYHHISMELahdpsdanirimsdlqeqldyQNGWQFETRISQvltllNLdpdatldsLSGGWLRKV 165
Cdd:cd03228    74 L--------------RKNIAYVP---------------------QDPFLFSGTIRE-----NI--------LSGGQRQRI 105
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1411607396 166 ALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRG--AIVFISHDREFIhKLATRIIDLDRG 229
Cdd:cd03228   106 AIARALLRDPPILILDEATSALDPETEALILEALRALAKgkTVIVIAHRLSTI-RDADRIIVLDDG 170
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
19-224 1.36e-20

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: 93.19  E-value: 1.36e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  19 LDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELP---LDDGRMV-QQQDL-KVTRLE-------------QDPPASSD 80
Cdd:COG0444    21 VDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILfDGEDLlKLSEKElrkirgreiqmifQDPMTSLN 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  81 --LTVFDYTAEGLagvgellkKYHHIsmelaHDPSDAnirimsdlqeqldyqngwqfETRISQVLTLLNL-DPDATLDS- 156
Cdd:COG0444   101 pvMTVGDQIAEPL--------RIHGG-----LSKAEA--------------------RERAIELLERVGLpDPERRLDRy 147
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1411607396 157 ---LSGGWLRKVALARALACDPDLLLLDEPTNHLD--IEA--INWLEDFLKDFRGAIVFISHDREFIHKLATRII 224
Cdd:COG0444   148 pheLSGGMRQRVMIARALALEPKLLIADEPTTALDvtIQAqiLNLLKDLQRELGLAILFITHDLGVVAEIADRVA 222
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
329-496 4.16e-20

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 88.44  E-value: 4.16e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 329 FGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKGGTKLEVAYFDQyRDQLDPE--QTVMDNVGE 406
Cdd:NF040873    2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQ-RSEVPDSlpLTVRDLVAM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 407 GK-QEvmvRGRSRHI--------------LGyLQDFlfepkrARTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDL 471
Cdd:NF040873   81 GRwAR---RGLWRRLtrddraavddalerVG-LADL------AGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150
                         170       180
                  ....*....|....*....|....*...
gi 1411607396 472 DVETLELLEELLADYPG---TLLLVSHD 496
Cdd:NF040873  151 DAESRERIIALLAEEHArgaTVVVVTHD 178
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
4-229 8.23e-20

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: 88.02  E-value: 8.23e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   4 LTLHGACLSFSDFPLLDNAELSIERGeRLCLVGRNGAGKSTLMKIIAGELPLDDGrmvqqqdlKVTRLEQDPPASSDltv 83
Cdd:cd03264     1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSG--------TIRIDGQDVLKQPQ--- 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  84 fdytaeglagvgellKKYHHISMeLAHDPS-DANIRImsdlQEQLDYQnGW-------QFETRISQVLTLLNLDPDAT-- 153
Cdd:cd03264    69 ---------------KLRRRIGY-LPQEFGvYPNFTV----REFLDYI-AWlkgipskEVKARVDEVLELVNLGDRAKkk 127
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1411607396 154 LDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDF-RGAIVFIS-HDREFIHKLATRIIDLDRG 229
Cdd:cd03264   128 IGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELgEDRIVILStHIVEDVESLCNQVAVLNKG 205
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
330-542 1.11e-19

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 93.31  E-value: 1.11e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 330 GDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKGGTKLEVAYFDQ-------------------Y 390
Cdd:PRK10636   12 GVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQetpalpqpaleyvidgdreY 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 391 RdQLDPEQTVMDNVGEGKQEVMVRG----------RSR-----HILGYLQDFLFEPkrartpVKALSGGEKNRLLLAKLF 455
Cdd:PRK10636   92 R-QLEAQLHDANERNDGHAIATIHGkldaidawtiRSRaasllHGLGFSNEQLERP------VSDFSGGWRMRLNLAQAL 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 456 LKPSNLLILDEPTNDLDVETLELLEELLADYPGTLLLVSHDRRFIDNTVTGCWLFEGDgRISDYVGGYAdmmATRAQQST 535
Cdd:PRK10636  165 ICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQ-SLFEYTGNYS---SFEVQRAT 240

                  ....*..
gi 1411607396 536 QLAAKAA 542
Cdd:PRK10636  241 RLAQQQA 247
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
17-226 1.21e-19

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 87.29  E-value: 1.21e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  17 PLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMVQQQDLKVTRLEQ--DPPASSDLTVFDYTAEGLAGV 94
Cdd:NF040873    6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQrsEVPDSLPLTVRDLVAMGRWAR 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  95 GELLKKYHHismelahdpsdANIRIMSDLQEQLDYQNgwqFETRisqvltllnldpdaTLDSLSGGWLRKVALARALACD 174
Cdd:NF040873   86 RGLWRRLTR-----------DDRAAVDDALERVGLAD---LAGR--------------QLGELSGGQRQRALLAQGLAQE 137
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1411607396 175 PDLLLLDEPTNHLDIEAINWLEDFLKDFRG---AIVFISHDREFIhKLATRIIDL 226
Cdd:NF040873  138 ADLLLLDEPTTGLDAESRERIIALLAEEHArgaTVVVVTHDLELV-RRADPCVLL 191
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
323-496 1.93e-19

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 88.20  E-value: 1.93e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 323 EGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRG-LVKGGTKLEVAYFD---QYRD-QLDPE 397
Cdd:PRK11247   16 NAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGeLLAGTAPLAEAREDtrlMFQDaRLLPW 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 398 QTVMDNVGEGkqevmVRGRSR-HILGYLQDFLFEPKRARTPVkALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLD---- 472
Cdd:PRK11247   96 KKVIDNVGLG-----LKGQWRdAALQALAAVGLADRANEWPA-ALSGGQKQRVALARALIHRPGLLLLDEPLGALDaltr 169
                         170       180
                  ....*....|....*....|....
gi 1411607396 473 VETLELLEELLADYPGTLLLVSHD 496
Cdd:PRK11247  170 IEMQDLIESLWQQHGFTVLLVTHD 193
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
330-502 2.52e-19

ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];


Pssm-ID: 441875 [Multi-domain]  Cd Length: 711  Bit Score: 92.20  E-value: 2.52e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 330 GDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVkggtklevaYFDQY-RDQLDPEQ---------- 398
Cdd:COG2274   486 DSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRI---------LIDGIdLRQIDPASlrrqigvvlq 556
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 399 -------TVMDNVGEGK-----QEVMvrgRSRHILGyLQDFLFE-PKRARTPV----KALSGGEKNRLLLAKLFLKPSNL 461
Cdd:COG2274   557 dvflfsgTIRENITLGDpdatdEEII---EAARLAG-LHDFIEAlPMGYDTVVgeggSNLSGGQRQRLAIARALLRNPRI 632
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1411607396 462 LILDEPTNDLDVETLELLEELLADYPG--TLLLVSHDRRFIDN 502
Cdd:COG2274   633 LILDEATSALDAETEAIILENLRRLLKgrTVIIIAHRLSTIRL 675
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
321-496 2.72e-19

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: 87.61  E-value: 2.72e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRG--LVKG--------GTKLEVAYFDQy 390
Cdd:COG4555     3 EVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGsiLIDGedvrkeprEARRQIGVLPD- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 391 RDQLDPEQTVMDNV-------GEGKQEVMVRgrsrhILGYLQDFLFEPKRARtPVKALSGGEKNRLLLAKLFLKPSNLLI 463
Cdd:COG4555    82 ERGLYDRLTVRENIryfaelyGLFDEELKKR-----IEELIELLGLEEFLDR-RVGELSTGMKKKVALARALVHDPKVLL 155
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1411607396 464 LDEPTNDLDVETLEL---LEELLADYPGTLLLVSHD 496
Cdd:COG4555   156 LDEPTNGLDVMARRLlreILRALKKEGKTVLFSSHI 191
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
4-235 2.93e-19

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: 86.85  E-value: 2.93e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   4 LTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLD-----------DGRMVQQQDLKVTRLE 72
Cdd:cd03260     1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIpgapdegevllDGKDIYDLDVDVLELR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  73 -------QdPPASSDLTVFDYTAEGLAGVGELLKKyhhismelahdpsdanirimsdlqeqldyqngwQFETRISQVLTL 145
Cdd:cd03260    81 rrvgmvfQ-KPNPFPGSIYDNVAYGLRLHGIKLKE---------------------------------ELDERVEEALRK 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 146 LNLDPD----ATLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRG--AIVFISHDREFIHKL 219
Cdd:cd03260   127 AALWDEvkdrLHALGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKeyTIVIVTHNMQQAARV 206
                         250
                  ....*....|....*..
gi 1411607396 220 ATRIIDLDRG-VITSWP 235
Cdd:cd03260   207 ADRTAFLLNGrLVEFGP 223
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
12-231 3.15e-19

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 89.76  E-value: 3.15e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  12 SFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRM---------VQQQDLKVTRLEQDPPASSDLT 82
Cdd:PRK10851   11 SFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIrfhgtdvsrLHARDRKVGFVFQHYALFRHMT 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  83 VFDYTAEGLAgvgeLLKKYHHismelahdPSDANIRimsdlqeqldyqngwqfeTRISQVLTLLNLDPDATL--DSLSGG 160
Cdd:PRK10851   91 VFDNIAFGLT----VLPRRER--------PNAAAIK------------------AKVTQLLEMVQLAHLADRypAQLSGG 140
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1411607396 161 WLRKVALARALACDPDLLLLDEPTNHLDI----EAINWLEDFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVI 231
Cdd:PRK10851  141 QKQRVALARALAVEPQILLLDEPFGALDAqvrkELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNI 215
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
320-495 4.75e-19

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: 84.96  E-value: 4.75e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 320 FETEGLGLDFGD--RTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTKLEVAYFDQYRDQldp 396
Cdd:cd03246     1 LEVENVSFRYPGaePPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRlDGADISQWDPNELGDH--- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 397 eqtvmdnvgegkqevmvrgrsrhiLGYL-QDF-LFEPKRARTpvkALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVE 474
Cdd:cd03246    78 ------------------------VGYLpQDDeLFSGSIAEN---ILSGGQRQRLGLARALYGNPRILVLDEPNSHLDVE 130
                         170       180
                  ....*....|....*....|....
gi 1411607396 475 TLELLEELLADYP---GTLLLVSH 495
Cdd:cd03246   131 GERALNQAIAALKaagATRIVIAH 154
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
1-225 6.76e-19

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 89.13  E-value: 6.76e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   1 MALLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLD------DGRMVQQQDLK-VTRLEQ 73
Cdd:PRK09536    1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTagtvlvAGDDVEALSARaASRRVA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  74 DPPASSDLTvFDYTAEGLAGVGellkKYHHISMELAHDPSDANIrimsdLQEQLDYQNGWQFETRisqvltllnldpdaT 153
Cdd:PRK09536   81 SVPQDTSLS-FEFDVRQVVEMG----RTPHRSRFDTWTETDRAA-----VERAMERTGVAQFADR--------------P 136
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1411607396 154 LDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDI-EAINWLE---DFLKDFRGAIVFIsHDREfihkLATRIID 225
Cdd:PRK09536  137 VTSLSGGERQRVLLARALAQATPVLLLDEPTASLDInHQVRTLElvrRLVDDGKTAVAAI-HDLD----LAARYCD 207
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
17-231 8.05e-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: 85.72  E-value: 8.05e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  17 PLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRM------VQQQDLKVTR-----LEQDP---------- 75
Cdd:cd03245    18 PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVlldgtdIRQLDPADLRrnigyVPQDVtlfygtlrdn 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  76 -----PASSDLTVFDytAEGLAGVGELLKKyHHISMELahdpsdanirimsDLQEQldyqnGwqfetrisqvltllnldp 150
Cdd:cd03245    98 itlgaPLADDERILR--AAELAGVTDFVNK-HPNGLDL-------------QIGER-----G------------------ 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 151 datlDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRG--AIVFISHdREFIHKLATRIIDLDR 228
Cdd:cd03245   139 ----RGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGdkTLIIITH-RPSLLDLVDRIIVMDS 213

                  ...
gi 1411607396 229 GVI 231
Cdd:cd03245   214 GRI 216
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
321-501 8.13e-19

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


Pssm-ID: 440741 [Multi-domain]  Cd Length: 248  Bit Score: 86.40  E-value: 8.13e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 321 ETEGLGLDFG----DRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTKLEVAY--------- 386
Cdd:COG1124     3 EVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTfDGRPVTRRRrkafrrrvq 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 387 --FDQYRDQLDPEQTVMDNVGE-----GKQEVMVR-GRSRHILGYLQDFLFepkraRTPvKALSGGEKNRLLLAK-LFLK 457
Cdd:COG1124    83 mvFQDPYASLHPRHTVDRILAEplrihGLPDREERiAELLEQVGLPPSFLD-----RYP-HQLSGGQRQRVAIARaLILE 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1411607396 458 PSnLLILDEPTNDLDV----ETLELLEELLADYPGTLLLVSHDRRFID 501
Cdd:COG1124   157 PE-LLLLDEPTSALDVsvqaEILNLLKDLREERGLTYLFVSHDLAVVA 203
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
3-473 1.11e-18

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 89.72  E-value: 1.11e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   3 LLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRM------------VQQQDLKVTR 70
Cdd:PRK15439   11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLeiggnpcarltpAKAHQLGIYL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  71 LEQDPPASSDLTVFDYTAEGLAGVGELLKKyhhismelahdpsdaniriMSDLQEQLDYQngwqfetrisqvltllnLDP 150
Cdd:PRK15439   91 VPQEPLLFPNLSVKENILFGLPKRQASMQK-------------------MKQLLAALGCQ-----------------LDL 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 151 DATLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRG---AIVFISHDREFIHKLATRIIDLD 227
Cdd:PRK15439  135 DSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLAqgvGIVFISHKLPEIRQLADRISVMR 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 228 RGVITswpgnydeyLQGKEEALRVEELQHAefdrklaqeevwVRQGIKARRTRnEGRVRALEamrMERSQRRELQGKAKL 307
Cdd:PRK15439  215 DGTIA---------LSGKTADLSTDDIIQA------------ITPAAREKSLS-ASQKLWLE---LPGNRRQQAAGAPVL 269
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 308 QMDDVnrSGklvfetEGlgldfgdrtlFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGqLEPSRGlvkGGTKLEVAYF 387
Cdd:PRK15439  270 TVEDL--TG------EG----------FRNISLEVRAGEILGLAGVVGAGRTELAETLYG-LRPARG---GRIMLNGKEI 327
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 388 DQY--RDQLD------PEQT------------------VMDNVG---EGKQEVMVRGRSRHILGylqdflFEPKRARTPV 438
Cdd:PRK15439  328 NALstAQRLArglvylPEDRqssglyldaplawnvcalTHNRRGfwiKPARENAVLERYRRALN------IKFNHAEQAA 401
                         490       500       510
                  ....*....|....*....|....*....|....*
gi 1411607396 439 KALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDV 473
Cdd:PRK15439  402 RTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDV 436
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
302-475 1.15e-18

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


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 85.91  E-value: 1.15e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 302 QGKAKLQMDDVNRSgklvFETEGlgldfGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRG--LVKG- 378
Cdd:COG1116     3 AAAPALELRGVSKR----FPTGG-----GGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGevLVDGk 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 379 ---GTKLEVAY-FDQYRdqLDPEQTVMDNV-------GEGKQEvmVRGRSRHIL---GyLQDFlfepkRARTPvKALSGG 444
Cdd:COG1116    74 pvtGPGPDRGVvFQEPA--LLPWLTVLDNValglelrGVPKAE--RRERARELLelvG-LAGF-----EDAYP-HQLSGG 142
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1411607396 445 EKNRLLLAK-LFLKPSnLLILDEPTNDLDVET 475
Cdd:COG1116   143 MRQRVAIARaLANDPE-VLLMDEPFGALDALT 173
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
12-223 1.25e-18

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: 84.86  E-value: 1.25e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  12 SFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGR-MVQQQDLKVTRLEqdppASSDLTV---FDYT 87
Cdd:cd03263    11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTaYINGYSIRTDRKA----ARQSLGYcpqFDAL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  88 AEGLAGVgELLKKYHhismELAHDPSDANIRIMSDLQEQL---DYQNgwqfeTRISQvltllnldpdatldsLSGGWLRK 164
Cdd:cd03263    87 FDELTVR-EHLRFYA----RLKGLPKSEIKEEVELLLRVLgltDKAN-----KRART---------------LSGGMKRK 141
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1411607396 165 VALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRG--AIVFISHDREFIHKLATRI 223
Cdd:cd03263   142 LSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKgrSIILTTHSMDEAEALCDRI 202
F420-0_ABC_ATP TIGR03873
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ...
4-191 1.32e-18

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: 86.02  E-value: 1.32e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   4 LTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMV-----------QQQDLKVTRLE 72
Cdd:TIGR03873   2 LRLSRVSWSAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDlagvdlhglsrRARARRVALVE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  73 QDPPASSDLTVFDYTAeglagvgelLKKYHHISMELAHDPSDANIrimsdlqeqldyqngwqfetrISQVLTLLNLD--P 150
Cdd:TIGR03873  82 QDSDTAVPLTVRDVVA---------LGRIPHRSLWAGDSPHDAAV---------------------VDRALARTELShlA 131
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1411607396 151 DATLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEA 191
Cdd:TIGR03873 132 DRDMSTLSGGERQRVHVARALAQEPKLLLLDEPTNHLDVRA 172
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
4-231 1.42e-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: 85.08  E-value: 1.42e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   4 LTLHGACLSFSDFPLlDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGR-MVQQQDlkVTRLeqdPPASSD-- 80
Cdd:cd03299     1 LKVENLSKDWKEFKL-KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKiLLNGKD--ITNL---PPEKRDis 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  81 -----------LTVFDYTAEGLAGVGELLKKYHHISMELAhdpSDANIRimsdlqeqldyqngwqfetrisqvlTLLNLD 149
Cdd:cd03299    75 yvpqnyalfphMTVYKNIAYGLKKRKVDKKEIERKVLEIA---EMLGID-------------------------HLLNRK 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 150 PDatldSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIE----AINWLEDFLKDFRGAIVFISHDREFIHKLATRIID 225
Cdd:cd03299   127 PE----TLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRtkekLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAI 202

                  ....*.
gi 1411607396 226 LDRGVI 231
Cdd:cd03299   203 MLNGKL 208
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
4-229 1.81e-18

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


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 86.32  E-value: 1.81e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   4 LTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGrmvqqqdlKVTrLEQDPPASSDLTV 83
Cdd:COG4152     2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSG--------EVL-WDGEPLDPEDRRR 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  84 FDYTAE--GL---AGVGELLKkYhhismeLAH----DPSDANIRIMSdlqeqldyqngWqfetrisqvLTLLNLDP--DA 152
Cdd:COG4152    73 IGYLPEerGLypkMKVGEQLV-Y------LARlkglSKAEAKRRADE-----------W---------LERLGLGDraNK 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 153 TLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFR--GA-IVFISHDREFIHKLATRIIDLDRG 229
Cdd:COG4152   126 KVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAakGTtVIFSSHQMELVEELCDRIVIINKG 205
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
321-500 1.91e-18

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: 84.23  E-value: 1.91e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 321 ETEGLGLDFGDRT-LFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKGGTK-------LEVAYF--DQY 390
Cdd:cd03226     1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKpikakerRKSIGYvmQDV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 391 RDQLDpEQTVMDNVGEGKQEV-MVRGRSRHIlgyLQDF-LFEPKRaRTPvKALSGGEKNRLLLAKLFLKPSNLLILDEPT 468
Cdd:cd03226    81 DYQLF-TDSVREELLLGLKELdAGNEQAETV---LKDLdLYALKE-RHP-LSLSGGQKQRLAIAAALLSGKDLLIFDEPT 154
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1411607396 469 NDLD---VETLELLEELLADYPGTLLLVSHDRRFI 500
Cdd:cd03226   155 SGLDyknMERVGELIRELAAQGKAVIVITHDYEFL 189
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
321-472 2.25e-18

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 86.40  E-value: 2.25e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK--GGTKLEVAYFDQYR------- 391
Cdd:PRK13537    9 DFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISlcGEPVPSRARHARQRvgvvpqf 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 392 DQLDPEQTVMDNVGE-GKQEVMVRGRSRHILGYLQDFLFEPKRARTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTND 470
Cdd:PRK13537   89 DNLDPDFTVRENLLVfGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTG 168

                  ..
gi 1411607396 471 LD 472
Cdd:PRK13537  169 LD 170
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
336-475 2.76e-18

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: 84.09  E-value: 2.76e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 336 QGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRG--LVKGGTKL--------EVAYFDQYrDQLDPEQTVMDNVg 405
Cdd:cd03263    19 DDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGtaYINGYSIRtdrkaarqSLGYCPQF-DALFDELTVREHL- 96
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1411607396 406 egKQEVMVRGRSRH-----ILGYLQDFLFEPKRARtPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVET 475
Cdd:cd03263    97 --RFYARLKGLPKSeikeeVELLLRVLGLTDKANK-RARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPAS 168
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
336-499 3.21e-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: 83.69  E-value: 3.21e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 336 QGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTKL--------------EVAY-FDQYrdQLDPEQT 399
Cdd:cd03255    21 KGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRvDGTDIsklsekelaafrrrHIGFvFQSF--NLLPDLT 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 400 VMDNV-------GEGKQEvmVRGRSRHILGYLQdfLfePKRARTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:cd03255    99 ALENVelplllaGVPKKE--RRERAEELLERVG--L--GDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLD 172
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1411607396 473 VETLEL----LEELLADYPGTLLLVSHDRRF 499
Cdd:cd03255   173 SETGKEvmelLRELNKEAGTTIVVVTHDPEL 203
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
329-472 3.23e-18

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 86.42  E-value: 3.23e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 329 FGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVkggTKLEVAYFDQYR------------DQLDP 396
Cdd:PRK13536   51 YGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKI---TVLGVPVPARARlararigvvpqfDNLDL 127
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1411607396 397 EQTVMDN-VGEGKQEVMVRGRSRHILGYLQDFLFEPKRARTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:PRK13536  128 EFTVRENlLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLD 204
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
321-496 4.26e-18

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


Pssm-ID: 213260 [Multi-domain]  Cd Length: 220  Bit Score: 83.29  E-value: 4.26e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 321 ETEGLGLDFGDR----TLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTKL-----EVAY-FDQ 389
Cdd:cd03293     2 EVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLvDGEPVtgpgpDRGYvFQQ 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 390 YRdqLDPEQTVMDNV-------GEGKQEvmVRGRSRHIL---GyLQDFlfepkRARTPvKALSGGEKNRLLLAKLFLKPS 459
Cdd:cd03293    82 DA--LLPWLTVLDNValglelqGVPKAE--ARERAEELLelvG-LSGF-----ENAYP-HQLSGGMRQRVALARALAVDP 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1411607396 460 NLLILDEPTNDLDVETLELLEELLAD----YPGTLLLVSHD 496
Cdd:cd03293   151 DVLLLDEPFSALDALTREQLQEELLDiwreTGKTVLLVTHD 191
COG4559 COG4559
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
3-189 4.42e-18

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


Pssm-ID: 443620 [Multi-domain]  Cd Length: 258  Bit Score: 84.40  E-value: 4.42e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   3 LLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGR-MVQQQDLKVTRLEQDP------ 75
Cdd:COG4559     1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEvRLNGRPLAAWSPWELArrravl 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  76 PASSDLTvFDYTAEGLAGVGellkkyhhismELAHDPSDAnirimsdlqeqldyqngwQFETRISQVLTLLNLDPDATLD 155
Cdd:COG4559    81 PQHSSLA-FPFTVEEVVALG-----------RAPHGSSAA------------------QDRQIVREALALVGLAHLAGRS 130
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1411607396 156 --SLSGGWLRKVALARALA-----CDPD--LLLLDEPTNHLDI 189
Cdd:COG4559   131 yqTLSGGEQQRVQLARVLAqlwepVDGGprWLFLDEPTSALDL 173
nickel_nikE TIGR02769
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ...
17-231 5.72e-18

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: 84.09  E-value: 5.72e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  17 PLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAG-ELPLDDGRMVQQQDLKVTRLEQDPPASSDLTVFDYTAEGlagvg 95
Cdd:TIGR02769  25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGlEKPAQGTVSFRGQDLYQLDRKQRRAFRRDVQLVFQDSPS----- 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  96 ellkkyhhismelAHDPSDANIRIMSDLQEQLDYQNGWQFETRISQVLTLLNLDPDaTLD----SLSGGWLRKVALARAL 171
Cdd:TIGR02769 100 -------------AVNPRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSE-DADklprQLSGGQLQRINIARAL 165
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1411607396 172 ACDPDLLLLDEPTNHLDI----EAINWLEDFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVI 231
Cdd:TIGR02769 166 AVKPKLIVLDEAVSNLDMvlqaVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
321-495 7.12e-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: 82.65  E-value: 7.12e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVkggTKLEVAYFDQYRDQ------- 393
Cdd:cd03268     2 KTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEI---TFDGKSYQKNIEALrrigali 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 394 ----LDPEQTVMDNVGEGKQEVMVRgRSRH--ILGY--LQDflfepkRARTPVKALSGGEKNRLLLAKLFLKPSNLLILD 465
Cdd:cd03268    79 eapgFYPNLTARENLRLLARLLGIR-KKRIdeVLDVvgLKD------SAKKKVKGFSLGMKQRLGIALALLGNPDLLILD 151
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1411607396 466 EPTNDLD---VETLELLEELLADYPGTLLLVSH 495
Cdd:cd03268   152 EPTNGLDpdgIKELRELILSLRDQGITVLISSH 184
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
13-232 7.89e-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: 83.15  E-value: 7.89e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  13 FSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRmvqqqdlkVTRLEQDPpassdltvFDYTAEGLA 92
Cdd:cd03267    31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGE--------VRVAGLVP--------WKRRKKFLR 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  93 GVGELLKKYHHISMELAHDPSDANIRIMSDLQEQldyqngwQFETRISQVLTLLNLDP--DATLDSLSGGWLRKVALARA 170
Cdd:cd03267    95 RIGVVFGQKTQLWWDLPVIDSFYLLAAIYDLPPA-------RFKKRLDELSELLDLEEllDTPVRQLSLGQRMRAEIAAA 167
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1411607396 171 LACDPDLLLLDEPTNHLDIEAINWLEDFLKDF---RGAIVFI-SHDREFIHKLATRIIDLDRGVIT 232
Cdd:cd03267   168 LLHEPEILFLDEPTIGLDVVAQENIRNFLKEYnreRGTTVLLtSHYMKDIEALARRVLVIDKGRLL 233
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
331-475 8.02e-18

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


Pssm-ID: 213214 [Multi-domain]  Cd Length: 178  Bit Score: 81.59  E-value: 8.02e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 331 DRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKGGTKLEVAYFDQYRDQ---LDPE-----QTVMD 402
Cdd:cd03247    14 EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLisvLNQRpylfdTTLRN 93
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1411607396 403 NVGegkqevmvrgrsrhilgylqdflfepkrartpvKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVET 475
Cdd:cd03247    94 NLG---------------------------------RRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPIT 133
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
19-231 8.23e-18

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


Pssm-ID: 213233 [Multi-domain]  Cd Length: 218  Bit Score: 82.80  E-value: 8.23e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  19 LDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMvqqqdlkvtrleqdppassdltvfdyTAEGLAGVgell 98
Cdd:cd03266    21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFA--------------------------TVDGFDVV---- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  99 kkyhhismelaHDPSDA--NIRIMSD---------LQEQLDY------QNGWQFETRISQVLTLLNLDP--DATLDSLSG 159
Cdd:cd03266    71 -----------KEPAEArrRLGFVSDstglydrltARENLEYfaglygLKGDELTARLEELADRLGMEEllDRRVGGFST 139
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1411607396 160 GWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRG---AIVFISHDREFIHKLATRIIDLDRGVI 231
Cdd:cd03266   140 GMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRAlgkCILFSTHIMQEVERLCDRVVVLHRGRV 214
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
319-495 9.15e-18

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: 83.21  E-value: 9.15e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 319 VFETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLV-------KGGT-----KLEVAY 386
Cdd:COG1119     3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDvrlfgerRGGEdvwelRKRIGL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 387 F-----DQYRDQLDPEQTVM----DNVGEGKQ--EVMvRGRSRHILGYLQdflFEPKRARtPVKALSGGEKNRLLLAKLF 455
Cdd:COG1119    83 VspalqLRFPRDETVLDVVLsgffDSIGLYREptDEQ-RERARELLELLG---LAHLADR-PFGTLSQGEQRRVLIARAL 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1411607396 456 LKPSNLLILDEPTNDLDV---ETLELLEELLADYPG-TLLLVSH 495
Cdd:COG1119   158 VKDPELLILDEPTAGLDLgarELLLALLDKLAAEGApTLVLVTH 201
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
12-231 9.62e-18

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: 82.19  E-value: 9.62e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  12 SFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMVqqqdLKVTRLEQDPPASSDL-----TVFDY 86
Cdd:cd03262     9 SFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTII----IDGLKLTDDKKNINELrqkvgMVFQQ 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  87 -------TAegLAGVGELLKKYHHISMELAhdpsdanirimsdlqeqldyqngwqfETRISQVLTLLNLDP--DATLDSL 157
Cdd:cd03262    85 fnlfphlTV--LENITLAPIKVKGMSKAEA--------------------------EERALELLEKVGLADkaDAYPAQL 136
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1411607396 158 SGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDF--RG-AIVFISHDREFIHKLATRIIDLDRGVI 231
Cdd:cd03262   137 SGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLaeEGmTMVVVTHEMGFAREVADRVIFMDDGRI 213
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
14-231 1.24e-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: 82.62  E-value: 1.24e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  14 SDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRM----VQQQDLKVTRLE----------QDPPASS 79
Cdd:cd03256    12 NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVlidgTDINKLKGKALRqlrrqigmifQQFNLIE 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  80 DLTVFDYTAEGLAGvgellkkYHHIsmelahdpsdanIRIMSDLQEQLDYQngwqfetRISQVLTLLNLDPDATL--DSL 157
Cdd:cd03256    92 RLSVLENVLSGRLG-------RRST------------WRSLFGLFPKEEKQ-------RALAALERVGLLDKAYQraDQL 145
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1411607396 158 SGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDF---RGAIVFIS-HDREFIHKLATRIIDLDRGVI 231
Cdd:cd03256   146 SGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRInreEGITVIVSlHQVDLAREYADRIVGLKDGRI 223
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
5-229 1.32e-17

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


Pssm-ID: 443809 [Multi-domain]  Cd Length: 229  Bit Score: 82.10  E-value: 1.32e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   5 TLH---GACLsfsdfPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGE-LPlDDGRMVQQQDLKVTRLEQDPP---- 76
Cdd:COG4778    15 TLHlqgGKRL-----PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNyLP-DSGSILVRHDGGWVDLAQASPreil 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  77 ---------ASSDLTV------FDYTAEGLagvgellkkyhhisMELAHDPSDAnirimsdlqeqldyqngwqfETRISQ 141
Cdd:COG4778    89 alrrrtigyVSQFLRViprvsaLDVVAEPL--------------LERGVDREEA--------------------RARARE 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 142 VLTLLNLD------PDATLdslSGGWLRKVALARALACDPDLLLLDEPTNHLD-------IEAINWLEDflkdfRG-AIV 207
Cdd:COG4778   135 LLARLNLPerlwdlPPATF---SGGEQQRVNIARGFIADPPLLLLDEPTASLDaanravvVELIEEAKA-----RGtAII 206
                         250       260
                  ....*....|....*....|..
gi 1411607396 208 FISHDREFIHKLATRIIDLDRG 229
Cdd:COG4778   207 GIFHDEEVREAVADRVVDVTPF 228
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
4-250 1.37e-17

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 82.11  E-value: 1.37e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   4 LTLHGACLSFSDFPLldNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGR-MVQQQDL--------KVTRLEQD 74
Cdd:COG3840     2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRiLWNGQDLtalppaerPVSMLFQE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  75 PPASSDLTVFDYTAEGLagvgellkkyhhismelahdpsDANIRIMSDLQEQLdyqngwqfETRISQV-LT-LLNLDPDA 152
Cdd:COG3840    80 NNLFPHLTVAQNIGLGL----------------------RPGLKLTAEQRAQV--------EQALERVgLAgLLDRLPGQ 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 153 tldsLSGGWLRKVALARALACDPDLLLLDEPTNHLDI----EAINWLEDFLKDFRGAIVFISHDREFIHKLATRIIDLDR 228
Cdd:COG3840   130 ----LSGGQRQRVALARCLVRKRPILLLDEPFSALDPalrqEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVAD 205
                         250       260
                  ....*....|....*....|...
gi 1411607396 229 GVItSWPGNYDEYLQGK-EEALR 250
Cdd:COG3840   206 GRI-AADGPTAALLDGEpPPALA 227
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
4-231 1.82e-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: 81.90  E-value: 1.82e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   4 LTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGR-MVQQQDlkVTRLeqdPPASSD-- 80
Cdd:cd03300     1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEiLLDGKD--ITNL---PPHKRPvn 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  81 -----------LTVFDYTAEGLAgvgelLKKYhhismelahDPSDANIRIMsdlqEQLDyqngwqfetrISQVLTLLNLD 149
Cdd:cd03300    76 tvfqnyalfphLTVFENIAFGLR-----LKKL---------PKAEIKERVA----EALD----------LVQLEGYANRK 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 150 PDatldSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRGAI----VFISHDREFIHKLATRIID 225
Cdd:cd03300   128 PS----QLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELgitfVFVTHDQEEALTMSDRIAV 203

                  ....*.
gi 1411607396 226 LDRGVI 231
Cdd:cd03300   204 MNKGKI 209
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
19-231 2.16e-17

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 82.43  E-value: 2.16e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  19 LDNAELSIERGERLCLVGRNGAGKSTLMKIIAG-ELPldDGRMVQQQDLKVTRLeqdppASSDLTVFDYTaeglagvgel 97
Cdd:PRK10419   28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGlESP--SQGNVSWRGEPLAKL-----NRAQRKAFRRD---------- 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  98 lkkyhhISMELAHDPSDANIR-----IMSDLQEQLDYQNGWQFETRISQVLTLLNLDP---DATLDSLSGGWLRKVALAR 169
Cdd:PRK10419   91 ------IQMVFQDSISAVNPRktvreIIREPLRHLLSLDKAERLARASEMLRAVDLDDsvlDKRPPQLSGGQLQRVCLAR 164
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1411607396 170 ALACDPDLLLLDEPTNHLDI----EAINWLEDFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVI 231
Cdd:PRK10419  165 ALAVEPKLLILDEAVSNLDLvlqaGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
315-475 2.23e-17

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 85.60  E-value: 2.23e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 315 SGKLVFEteglGLDF---GDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTKL-EVAYfDQ 389
Cdd:COG1132   337 RGEIEFE----NVSFsypGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILiDGVDIrDLTL-ES 411
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 390 YRDQL-----DP---EQTVMDNVGEGKQEVmvrgrSR----------HILGYLQDFlfePKRARTPV----KALSGGEKN 447
Cdd:COG1132   412 LRRQIgvvpqDTflfSGTIRENIRYGRPDA-----TDeeveeaakaaQAHEFIEAL---PDGYDTVVgergVNLSGGQRQ 483
                         170       180
                  ....*....|....*....|....*...
gi 1411607396 448 RLLLAKLFLKPSNLLILDEPTNDLDVET 475
Cdd:COG1132   484 RIAIARALLKDPPILILDEATSALDTET 511
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
321-497 2.82e-17

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: 81.03  E-value: 2.82e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRG-LVKGGT--------KLEVAY-FDQY 390
Cdd:cd03259     2 ELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGeILIDGRdvtgvppeRRNIGMvFQDY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 391 RdqLDPEQTVMDNVG-----EGKQEVMVRGRSRHILGYLQDFLFEPKRARTpvkaLSGGEKNRLLLAK-LFLKPSnLLIL 464
Cdd:cd03259    82 A--LFPHLTVAENIAfglklRGVPKAEIRARVRELLELVGLEGLLNRYPHE----LSGGQQQRVALARaLAREPS-LLLL 154
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1411607396 465 DEPTNDLDVETLELLEELLADYPG----TLLLVSHDR 497
Cdd:cd03259   155 DEPLSALDAKLREELREELKELQRelgiTTIYVTHDQ 191
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
1-501 3.04e-17

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 85.07  E-value: 3.04e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   1 MALLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRmVQQQDLKVTRL--EQDPPAS 78
Cdd:PRK10938    1 MSSLQISQGTFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGE-RQSQFSHITRLsfEQLQKLV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  79 SDltVFDYTAEGLAGVGEllKKYHHISMELAHDPSDANIRImsdlqEQLDYQNGwqfetrISQVLtllnldpDATLDSLS 158
Cdd:PRK10938   80 SD--EWQRNNTDMLSPGE--DDTGRTTAEIIQDEVKDPARC-----EQLAQQFG------ITALL-------DRRFKYLS 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 159 GGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRG---AIVFISHDREFIHKLATRIIDLDRGVITswp 235
Cdd:PRK10938  138 TGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQsgiTLVLVLNRFDEIPDFVQFAGVLADCTLA--- 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 236 gnydeyLQGKEEALR----VEELQHAEfdrklaqeevwvrqgikarrtrnegrvrALEAMRM----ERSQRREL-QGKAK 306
Cdd:PRK10938  215 ------ETGEREEILqqalVAQLAHSE----------------------------QLEGVQLpepdEPSARHALpANEPR 260
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 307 LQMDDVNRSgklvfeteglgldFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQlEPS------------RG 374
Cdd:PRK10938  261 IVLNNGVVS-------------YNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGD-HPQgysndltlfgrrRG 326
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 375 lvKGGT----KLEVAYFD-----QYRDQLDPEQTVM----DNVGEGKQevmVRGRSRHILGYLQDFLFEPKR-ARTPVKA 440
Cdd:PRK10938  327 --SGETiwdiKKHIGYVSsslhlDYRVSTSVRNVILsgffDSIGIYQA---VSDRQQKLAQQWLDILGIDKRtADAPFHS 401
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1411607396 441 LSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDvetlelleelladyPGTLLLVshdRRFID 501
Cdd:PRK10938  402 LSWGQQRLALIVRALVKHPTLLILDEPLQGLD--------------PLNRQLV---RRFVD 445
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
19-212 3.07e-17

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


Pssm-ID: 443658 [Multi-domain]  Cd Length: 329  Bit Score: 83.24  E-value: 3.07e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  19 LDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMV---------QQQDLKVTRLE-----QDPPASSD--LT 82
Cdd:COG4608    34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILfdgqditglSGRELRPLRRRmqmvfQDPYASLNprMT 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  83 VFDYTAEGLagvgellkkyhhismeLAHDPSDANIRimsdlqeqldyqngwqfETRISQVLTLLNLDPDAtLDS----LS 158
Cdd:COG4608   114 VGDIIAEPL----------------RIHGLASKAER-----------------RERVAELLELVGLRPEH-ADRypheFS 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1411607396 159 GGWLRKVALARALACDPDLLLLDEPTNHLD--IEA--INWLEDFLKDFRGAIVFISHD 212
Cdd:COG4608   160 GGQRQRIGIARALALNPKLIVCDEPVSALDvsIQAqvLNLLEDLQDELGLTYLFISHD 217
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
321-472 3.24e-17

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


Pssm-ID: 213228 [Multi-domain]  Cd Length: 235  Bit Score: 81.39  E-value: 3.24e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGlvkggtklEVAYFDQYRDQLDPEQ-- 398
Cdd:cd03261     2 ELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSG--------EVLIDGEDISGLSEAEly 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 399 -------------------TVMDNVG------EGKQEVMVRGRSRHILGYLQdflFEPKRARTPVKaLSGGEKNRLLLAK 453
Cdd:cd03261    74 rlrrrmgmlfqsgalfdslTVFENVAfplrehTRLSEEEIREIVLEKLEAVG---LRGAEDLYPAE-LSGGMKKRVALAR 149
                         170       180
                  ....*....|....*....|
gi 1411607396 454 -LFLKPSnLLILDEPTNDLD 472
Cdd:cd03261   150 aLALDPE-LLLYDEPTAGLD 168
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
29-229 4.31e-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: 4.31e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  29 GERLCLVGRNGAGKSTLMKIIAGELPLDDGRMV----------QQQDLKVTR-----LEQDPPASSDLTVFDYTAEGLAG 93
Cdd:cd03297    23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVlngtvlfdsrKKINLPPQQrkiglVFQQYALFPHLNVRENLAFGLKR 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  94 vgellkkyhhismelahdPSDANIRImsdlqeqldyqngwqfetRISQVLTLLNLDP--DATLDSLSGGWLRKVALARAL 171
Cdd:cd03297   103 ------------------KRNREDRI------------------SVDELLDLLGLDHllNRYPAQLSGGEKQRVALARAL 146
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1411607396 172 ACDPDLLLLDEPTNHLD----IEAINWLEDFLKDFRGAIVFISHDREFIHKLATRIIDLDRG 229
Cdd:cd03297   147 AAQPELLLLDEPFSALDralrLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDG 208
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
12-224 4.42e-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: 84.84  E-value: 4.42e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  12 SFSDFPLlDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMvqQQDLKVTRLEQDPPASSDLTVFDYTAEGL 91
Cdd:COG1245   350 SYGGFSL-EVEGGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV--DEDLKISYKPQYISPDYDGTVEEFLRSAN 426
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  92 AGvgellkkyhhismelahdpsdanirimsdlqeqlDYQNGWqFETRISQVLtllNLDP--DATLDSLSGGWLRKVALAR 169
Cdd:COG1245   427 TD----------------------------------DFGSSY-YKTEIIKPL---GLEKllDKNVKDLSGGELQRVAIAA 468
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1411607396 170 ALACDPDLLLLDEPTNHLDIEAINWLEDFLKDF---RGAIVF-ISHDREFIHKLATRII 224
Cdd:COG1245   469 CLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFaenRGKTAMvVDHDIYLIDYISDRLM 527
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
323-473 5.23e-17

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 80.93  E-value: 5.23e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 323 EGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKGGTKLEVAYFDQyRDQLDP------ 396
Cdd:PRK09544    8 ENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQ-KLYLDTtlpltv 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 397 EQTVMDNVGEGKQEVM---VRGRSRHILGYlqdflfepkrartPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDV 473
Cdd:PRK09544   87 NRFLRLRPGTKKEDILpalKRVQAGHLIDA-------------PMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDV 153
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
320-500 6.22e-17

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: 78.77  E-value: 6.22e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 320 FETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLV----KGGTKLEVAYFDQYRD--- 392
Cdd:cd03229     1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSIlidgEDLTDLEDELPPLRRRigm 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 393 -----QLDPEQTVMDNVGEGkqevmvrgrsrhilgylqdflfepkrartpvkaLSGGEKNRLLLAK-LFLKPsNLLILDE 466
Cdd:cd03229    81 vfqdfALFPHLTVLENIALG---------------------------------LSGGQQQRVALARaLAMDP-DVLLLDE 126
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1411607396 467 PTNDLDVETLELLEELLAD----YPGTLLLVSHDRRFI 500
Cdd:cd03229   127 PTSALDPITRREVRALLKSlqaqLGITVVLVTHDLDEA 164
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
321-496 6.70e-17

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: 80.11  E-value: 6.70e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGlvkggtKLEVAYFDQYRDQLD----- 395
Cdd:cd03265     2 EVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSG------RATVAGHDVVREPREvrrri 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 396 ---PEQTVMDNVGEGKQEVMVRGRsrhILGY-----------LQDFLFEPKRARTPVKALSGGEKNRLLLAKLFLKPSNL 461
Cdd:cd03265    76 givFQDLSVDDELTGWENLYIHAR---LYGVpgaerrerideLLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEV 152
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1411607396 462 LILDEPTNDLDVETLELL----EELLADYPGTLLLVSHD 496
Cdd:cd03265   153 LFLDEPTIGLDPQTRAHVweyiEKLKEEFGMTILLTTHY 191
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
319-475 7.35e-17

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 79.53  E-value: 7.35e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 319 VFETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK--GGTKLEVAYFDQ-----YR 391
Cdd:PRK13539    2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKldGGDIDDPDVAEAchylgHR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 392 DQLDPEQTVMDNVgEGKQEVMvRGRSRHILGYLQDFLFEPKrARTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDL 471
Cdd:PRK13539   82 NAMKPALTVAENL-EFWAAFL-GGEELDIAAALEAVGLAPL-AHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAAL 158

                  ....
gi 1411607396 472 DVET 475
Cdd:PRK13539  159 DAAA 162
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
321-500 7.65e-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: 80.17  E-value: 7.65e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTklEVAYFDQYR-------- 391
Cdd:cd03219     2 EVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLfDGE--DITGLPPHEiarlgigr 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 392 ----DQLDPEQTVMDNV---------------GEGKQEVMVRGRSRHILgylqDFLFEPKRARTPVKALSGGEKNRLLLA 452
Cdd:cd03219    80 tfqiPRLFPELTVLENVmvaaqartgsglllaRARREEREARERAEELL----ERVGLADLADRPAGELSYGQQRRLEIA 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1411607396 453 K-LFLKPSnLLILDEPT---NDLDVETLELLEELLADYPGTLLLVSHDRRFI 500
Cdd:cd03219   156 RaLATDPK-LLLLDEPAaglNPEETEELAELIRELRERGITVLLVEHDMDVV 206
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
12-231 7.73e-17

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: 79.72  E-value: 7.73e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  12 SFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRM------VQQQDLKVTR----LEQDPPASSDL 81
Cdd:cd03265     9 KYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRAtvaghdVVREPREVRRrigiVFQDLSVDDEL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  82 TVFD--YTAEGLAGV-GELLKKyhhismelahdpsdaniRImsdlQEQLDYQNGWQFETRIsqvltllnldpdatLDSLS 158
Cdd:cd03265    89 TGWEnlYIHARLYGVpGAERRE-----------------RI----DELLDFVGLLEAADRL--------------VKTYS 133
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1411607396 159 GGWLRKVALARALACDPDLLLLDEPTNHLDIEAIN--W--LEDFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVI 231
Cdd:cd03265   134 GGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAhvWeyIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRI 210
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
26-224 1.67e-16

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 82.93  E-value: 1.67e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  26 IERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMVQqqDLKVTRLEQDPPASSDLTVFDYtaegLAGVGEllkkyhhis 105
Cdd:PRK13409  362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDP--ELKISYKPQYIKPDYDGTVEDL----LRSITD--------- 426
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 106 melahdpsdanirimsdlqeqlDYQNGWqFETRISQVLtllNLDP--DATLDSLSGGWLRKVALARALACDPDLLLLDEP 183
Cdd:PRK13409  427 ----------------------DLGSSY-YKSEIIKPL---QLERllDKNVKDLSGGELQRVAIAACLSRDADLYLLDEP 480
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1411607396 184 TNHLDIE-------AINwleDFLKDFRGAIVFISHDREFIHKLATRII 224
Cdd:PRK13409  481 SAHLDVEqrlavakAIR---RIAEEREATALVVDHDIYMIDYISDRLM 525
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
19-231 1.91e-16

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: 82.81  E-value: 1.91e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  19 LDNAELSIERGERLCLVGRNGAGKSTLMKII------AGELPLDDGRMVQ--QQDLKVTRLE-----QDPPASSD--LTV 83
Cdd:COG4172   302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALlrlipsEGEIRFDGQDLDGlsRRALRPLRRRmqvvfQDPFGSLSprMTV 381
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  84 FDYTAEGLAgvgellkkyhhismelAHDPsdanirimsdlqeQLDYQngwQFETRISQVLTLLNLDPDaTLD----SLSG 159
Cdd:COG4172   382 GQIIAEGLR----------------VHGP-------------GLSAA---ERRARVAEALEEVGLDPA-ARHryphEFSG 428
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1411607396 160 GWLRKVALARALACDPDLLLLDEPTNHLD--IEA--INWLEDFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVI 231
Cdd:COG4172   429 GQRQRIAIARALILEPKLLVLDEPTSALDvsVQAqiLDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKV 504
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
330-496 2.07e-16

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


Pssm-ID: 274331 [Multi-domain]  Cd Length: 530  Bit Score: 82.41  E-value: 2.07e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 330 GDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRG-----------LVKGGTKLEVAYFDQyrdqlDP-- 396
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGevtldgvpvssLDQDEVRRRVSVCAQ-----DAhl 420
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 397 -EQTVMDNV----GEGKQEVMVRGRSRHILGYLQDFLfePKRARTPV----KALSGGEKNRLLLAKLFLKPSNLLILDEP 467
Cdd:TIGR02868 421 fDTTVRENLrlarPDATDEELWAALERVGLADWLRAL--PDGLDTVLgeggARLSGGERQRLALARALLADAPILLLDEP 498
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1411607396 468 TNDLDVETLEL--LEELLADYPGTLLLVSHD 496
Cdd:TIGR02868 499 TEHLDAETADEllEDLLAALSGRTVVLITHH 529
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
337-503 2.56e-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: 78.22  E-value: 2.56e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 337 GLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTKL------EVAYFDQ-----YRD-QLDPEQTVMDN 403
Cdd:cd03292    19 GINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRvNGQDVsdlrgrAIPYLRRkigvvFQDfRLLPDRNVYEN 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 404 V-------GEGKQEvmVRGRSRHILgylqDFLFEPKRARTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVETL 476
Cdd:cd03292    99 VafalevtGVPPRE--IRKRVPAAL----ELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTT 172
                         170       180       190
                  ....*....|....*....|....*....|
gi 1411607396 477 ELLEELLADY--PGTLLLVS-HDRRFIDNT 503
Cdd:cd03292   173 WEIMNLLKKInkAGTTVVVAtHAKELVDTT 202
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
329-570 2.64e-16

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 82.25  E-value: 2.64e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 329 FGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKGGTKLEVAYFDQyrDQLDPEQ-TVMDNVGEG 407
Cdd:PRK15064   11 FGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKLRQ--DQFAFEEfTVLDTVIMG 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 408 -------KQE------------------------------VMVRGRSRHIL---GYLQDFLFEPKRARTPvkalsgGEKN 447
Cdd:PRK15064   89 htelwevKQErdriyalpemseedgmkvadlevkfaemdgYTAEARAGELLlgvGIPEEQHYGLMSEVAP------GWKL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 448 RLLLAK-LFLKPsNLLILDEPTNDLDVETLELLEELLADYPGTLLLVSHDRRFIdNTVtgCW----LFEGDGRIsdYVGG 522
Cdd:PRK15064  163 RVLLAQaLFSNP-DILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFL-NSV--CThmadLDYGELRV--YPGN 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1411607396 523 YADMMATRAQQSTQLAA----KAAQVKT-PEPVAVASPAASKVK------KLSYKLQLE 570
Cdd:PRK15064  237 YDEYMTAATQARERLLAdnakKKAQIAElQSFVSRFSANASKAKqatsraKQIDKIKLE 295
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
319-496 2.81e-16

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: 81.87  E-value: 2.81e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 319 VFETEGLGLDF--GDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGqLEPSRGLVKGGTKL-------------- 382
Cdd:COG1123     4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMG-LLPHGGRISGEVLLdgrdllelsealrg 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 383 -EVAY-FDQYRDQLDPEqTVMDNVGEGKQEVMVRGRSRH--ILGYLQDFLFEpKRARTPVKALSGGEKNRLLLA-KLFLK 457
Cdd:COG1123    83 rRIGMvFQDPMTQLNPV-TVGDQIAEALENLGLSRAEARarVLELLEAVGLE-RRLDRYPHQLSGGQRQRVAIAmALALD 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1411607396 458 PSnLLILDEPTNDLDV----ETLELLEELLADYPGTLLLVSHD 496
Cdd:COG1123   161 PD-LLIADEPTTALDVttqaEILDLLRELQRERGTTVLLITHD 202
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
4-229 3.16e-16

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 82.16  E-value: 3.16e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   4 LTLHGACLSFSDF-PLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMVQQQDLKVTRLEQDP------- 75
Cdd:COG4178   363 LALEDLTLRTPDGrPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGARVLFLPQRPylplgtl 442
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  76 ------PASSDltvfDYTAEGLAgvgELLKKYHhismeLAHdpsdanirimsdLQEQLDYQNGWqfetriSQVLtllnld 149
Cdd:COG4178   443 reallyPATAE----AFSDAELR---EALEAVG-----LGH------------LAERLDEEADW------DQVL------ 486
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 150 pdatldslSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKD--FRGAIVFISHdREFIHKLATRIIDLD 227
Cdd:COG4178   487 --------SLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREelPGTTVISVGH-RSTLAAFHDRVLELT 557

                  ..
gi 1411607396 228 RG 229
Cdd:COG4178   558 GD 559
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
321-495 3.92e-16

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: 77.71  E-value: 3.92e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRG--LVKG-----GTKLEVAYFDQYRDq 393
Cdd:cd03269     2 EVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGevLFDGkpldiAARNRIGYLPEERG- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 394 LDPEQTVMDNV-------GEGKQEVmvrgrSRHILGYLQDFLFEPKRARtPVKALSGGEKNRLLLAKLFLKPSNLLILDE 466
Cdd:cd03269    81 LYPKMKVIDQLvylaqlkGLKKEEA-----RRRIDEWLERLELSEYANK-RVEELSKGNQQKVQFIAAVIHDPELLILDE 154
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1411607396 467 PTNDLD---VETLELLEELLADYPGTLLLVSH 495
Cdd:cd03269   155 PFSGLDpvnVELLKDVIRELARAGKTVILSTH 186
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
17-226 4.83e-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: 81.18  E-value: 4.83e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  17 PLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRM-VQQQDL----------KVTRLEQDPpassdlTVFD 85
Cdd:TIGR02857 336 PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIaVNGVPLadadadswrdQIAWVPQHP------FLFA 409
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  86 YT-AEGLAgvgeLLKKyhhismelahDPSDAnirimsDLQEQLDYQNGWQFETRISQVLTLLnLDPDATldSLSGGWLRK 164
Cdd:TIGR02857 410 GTiAENIR----LARP----------DASDA------EIREALERAGLDEFVAALPQGLDTP-IGEGGA--GLSGGQAQR 466
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1411607396 165 VALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDF-RGAIVF-ISHDREFIHkLATRIIDL 226
Cdd:TIGR02857 467 LALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALaQGRTVLlVTHRLALAA-LADRIVVL 529
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
321-474 5.28e-16

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


Pssm-ID: 273491 [Multi-domain]  Cd Length: 198  Bit Score: 77.01  E-value: 5.28e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKGGTKLEVAYFDQY---------R 391
Cdd:TIGR01189   2 AARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPhenilylghL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 392 DQLDPEQTVMDNVGegkqevmvrgRSRHILGYLQDFLFEP-------KRARTPVKALSGGEKNRLLLAKLFLKPSNLLIL 464
Cdd:TIGR01189  82 PGLKPELSALENLH----------FWAAIHGGAQRTIEDAlaavgltGFEDLPAAQLSAGQQRRLALARLWLSRRPLWIL 151
                         170
                  ....*....|
gi 1411607396 465 DEPTNDLDVE 474
Cdd:TIGR01189 152 DEPTTALDKA 161
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
320-475 5.33e-16

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: 77.99  E-value: 5.33e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 320 FETEGLGLDFGD-RTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK----GGTKLEVAYFDQYRDQ- 393
Cdd:cd03256     1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLidgtDINKLKGKALRQLRRQi 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 394 --------LDPEQTVMDNVGEGKQEVMVRGRS----------RHILGYLQDFLFEPKrARTPVKALSGGEKNRLLLAKLF 455
Cdd:cd03256    81 gmifqqfnLIERLSVLENVLSGRLGRRSTWRSlfglfpkeekQRALAALERVGLLDK-AYQRADQLSGGQQQRVAIARAL 159
                         170       180
                  ....*....|....*....|
gi 1411607396 456 LKPSNLLILDEPTNDLDVET 475
Cdd:cd03256   160 MQQPKLILADEPVASLDPAS 179
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
4-183 5.51e-16

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: 77.58  E-value: 5.51e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   4 LTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGR------------MVQQQDLKVTRL 71
Cdd:cd03218     1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKilldgqditklpMHKRARLGIGYL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  72 EQDPPASSDLTVfdytAEGLAGVGELLKKyhhismelahdpsdanirimsdlqeqldyqNGWQFETRISQVLTLLNLDP- 150
Cdd:cd03218    81 PQEASIFRKLTV----EENILAVLEIRGL------------------------------SKKEREEKLEELLEEFHITHl 126
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1411607396 151 -DATLDSLSGGWLRKVALARALACDPDLLLLDEP 183
Cdd:cd03218   127 rKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
17-231 6.87e-16

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: 75.72  E-value: 6.87e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  17 PLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMvqqqdlkvtRLEqdppassdltvfdytaeglagvGE 96
Cdd:cd03246    16 PVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRV---------RLD----------------------GA 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  97 LLKKYHhismelahdpsdaniriMSDLQEQLDY--QNGWQFETRISQvltllNLdpdatldsLSGGWLRKVALARALACD 174
Cdd:cd03246    65 DISQWD-----------------PNELGDHVGYlpQDDELFSGSIAE-----NI--------LSGGQRQRLGLARALYGN 114
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 175 PDLLLLDEPTNHLDIEAINWLEDFLKDFRGA---IVFISHDREFIhKLATRIIDLDRGVI 231
Cdd:cd03246   115 PRILVLDEPNSHLDVEGERALNQAIAALKAAgatRIVIAHRPETL-ASADRILVLEDGRV 173
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
320-472 7.02e-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: 77.22  E-value: 7.02e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 320 FETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLL-----LGQLEPSRGlvkggtklEVAYFDQ--YRD 392
Cdd:cd03260     1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEG--------EVLLDGKdiYDL 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 393 QLDPEQ-----------------TVMDNV-------GEGKQEVMvRGRSRHILGylQDFLFEPKRARTPVKALSGGEKNR 448
Cdd:cd03260    73 DVDVLElrrrvgmvfqkpnpfpgSIYDNVayglrlhGIKLKEEL-DERVEEALR--KAALWDEVKDRLHALGLSGGQQQR 149
                         170       180
                  ....*....|....*....|....*
gi 1411607396 449 LLLAK-LFLKPSNLLiLDEPTNDLD 472
Cdd:cd03260   150 LCLARaLANEPEVLL-LDEPTSALD 173
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
3-243 7.28e-16

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 80.98  E-value: 7.28e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   3 LLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMVQQQDLKVTRLEQdppassdlt 82
Cdd:PRK10636  312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQ--------- 382
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  83 vfdytaeglagvgellkkyHHISMELAHD-PSDANIRIM-SDLQEQL-DYQNGWQFETriSQVltllnldPDATlDSLSG 159
Cdd:PRK10636  383 -------------------HQLEFLRADEsPLQHLARLApQELEQKLrDYLGGFGFQG--DKV-------TEET-RRFSG 433
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 160 GWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVITSWPGNYD 239
Cdd:PRK10636  434 GEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVEPFDGDLE 513

                  ....
gi 1411607396 240 EYLQ 243
Cdd:PRK10636  514 DYQQ 517
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
17-227 8.21e-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: 75.27  E-value: 8.21e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  17 PLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMVQQQDLKVTRLEQDPpassdltvfdYTAEGLagvge 96
Cdd:cd03223    15 VLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLFLPQRP----------YLPLGT----- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  97 llkkyhhismelahdpsdanirimsdLQEQLDYQngWQfetrisqvltllnldpdatlDSLSGGWLRKVALARALACDPD 176
Cdd:cd03223    80 --------------------------LREQLIYP--WD--------------------DVLSGGEQQRLAFARLLLHKPK 111
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1411607396 177 LLLLDEPTNHLDIEAINWLEDFLKDFRGAIVFISHdREFIHKLATRIIDLD 227
Cdd:cd03223   112 FVFLDEATSALDEESEDRLYQLLKELGITVISVGH-RPSLWKFHDRVLDLD 161
CeuD COG4604
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ...
5-189 8.48e-16

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


Pssm-ID: 443654 [Multi-domain]  Cd Length: 252  Bit Score: 77.43  E-value: 8.48e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   5 TLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGR-MVQQQDLKVTR----------LEQ 73
Cdd:COG4604     3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEvLVDGLDVATTPsrelakrlaiLRQ 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  74 DPPASSDLTVFDytaegLAGVGellkKYHHISMEL-AHDpsdanirimsdlqeqldyqngwqfETRISQVLTLLNLDP-- 150
Cdd:COG4604    83 ENHINSRLTVRE-----LVAFG----RFPYSKGRLtAED------------------------REIIDEAIAYLDLEDla 129
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1411607396 151 DATLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDI 189
Cdd:COG4604   130 DRYLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDM 168
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...
319-500 9.25e-16

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: 77.39  E-value: 9.25e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 319 VFETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGlvkggtklEVAYFDQYRDQLDPEQ 398
Cdd:COG0411     4 LLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSG--------RILFDGRDITGLPPHR 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 399 -------------------TVMDNV--------GEG------------KQEVMVRGRSRHILGY--LQDflfepkRARTP 437
Cdd:COG0411    76 iarlgiartfqnprlfpelTVLENVlvaaharlGRGllaallrlprarREEREARERAEELLERvgLAD------RADEP 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1411607396 438 VKALSGGEKNRLLLAK-LFLKPSnLLILDEPT---NDLDVETLELLEELLADYPG-TLLLVSHDRRFI 500
Cdd:COG0411   150 AGNLSYGQQRRLEIARaLATEPK-LLLLDEPAaglNPEETEELAELIRRLRDERGiTILLIEHDMDLV 216
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
1-184 1.00e-15

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: 76.94  E-value: 1.00e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   1 MALLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMV-QQQDLkvTRLeqdPPAS- 78
Cdd:COG0410     1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRfDGEDI--TGL---PPHRi 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  79 ---------------SDLTVfdytAEGLagvgellkkyhhismELAHDPSDANIRIMSDLQEQLDYqngwqF---ETRIS 140
Cdd:COG0410    76 arlgigyvpegrrifPSLTV----EENL---------------LLGAYARRDRAEVRADLERVYEL-----FprlKERRR 131
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1411607396 141 QvltllnldpDATldSLSGGWLRKVALARALACDPDLLLLDEPT 184
Cdd:COG0410   132 Q---------RAG--TLSGGEQQMLAIGRALMSRPKLLLLDEPS 164
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
331-475 1.02e-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: 76.89  E-value: 1.02e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 331 DRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTKLEVAYFDQYRDQLD--PEQTV------M 401
Cdd:cd03253    13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILiDGQDIREVTLDSLRRAIGvvPQDTVlfndtiG 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 402 DNVGEGK-----QEVMVRGRSRHILGYLQDFlfePKRARTPVKA----LSGGEKNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:cd03253    93 YNIRYGRpdatdEEVIEAAKAAQIHDKIMRF---PDGYDTIVGErglkLSGGEKQRVAIARAILKNPPILLLDEATSALD 169

                  ...
gi 1411607396 473 VET 475
Cdd:cd03253   170 THT 172
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
321-496 1.37e-15

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: 76.39  E-value: 1.37e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 321 ETEGLGLDFGDRTLF----QGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLV----KGGTKLEVAYFDQYRD 392
Cdd:cd03257     3 EVKNLSVSFPTGGGSvkalDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIifdgKDLLKLSRRLRKIRRK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 393 Q-----------LDPEQTVMDNVGEG--KQEVMVRGRSRHILGYLQDFLFEPKRA---RTPVkALSGGEKNRLLLAK-LF 455
Cdd:cd03257    83 EiqmvfqdpmssLNPRMTIGEQIAEPlrIHGKLSKKEARKEAVLLLLVGVGLPEEvlnRYPH-ELSGGQRQRVAIARaLA 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1411607396 456 LKPSnLLILDEPTNDLDVETLELLEELLAD----YPGTLLLVSHD 496
Cdd:cd03257   162 LNPK-LLIADEPTSALDVSVQAQILDLLKKlqeeLGLTLLFITHD 205
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
2-189 1.39e-15

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 77.12  E-value: 1.39e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   2 ALLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRM-VQQQDLKVTRLEQDP----- 75
Cdd:PRK13548    1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVrLNGRPLADWSPAELArrrav 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  76 -PASSDLTvFDYTAEglagvgELlkkyhhISMELAHDPSDANirimsdlqeqldyqngwQFETRISQVLTLLNLDPDATL 154
Cdd:PRK13548   81 lPQHSSLS-FPFTVE------EV------VAMGRAPHGLSRA-----------------EDDALVAAALAQVDLAHLAGR 130
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1411607396 155 D--SLSGGWLRKVALARALA----CDPD--LLLLDEPTNHLDI 189
Cdd:PRK13548  131 DypQLSGGEQQRVQLARVLAqlwePDGPprWLLLDEPTSALDL 173
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
6-232 1.48e-15

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: 76.03  E-value: 1.48e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   6 LHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRmvqqqdlkVTRLEQDPPA-------S 78
Cdd:cd03220    25 ILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGT--------VTVRGRVSSLlglgggfN 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  79 SDLTVFDYTaeglagvgellkkyHHISMELAHDPSDANIRI-----MSDLQEQLDYqngwqfetrisQVLTllnldpdat 153
Cdd:cd03220    97 PELTGRENI--------------YLNGRLLGLSRKEIDEKIdeiieFSELGDFIDL-----------PVKT--------- 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 154 ldsLSGGWLRKVALARALACDPDLLLLDEPT----NHLDIEAINWLEDFLKDFRgAIVFISHDREFIHKLATRIIDLDRG 229
Cdd:cd03220   143 ---YSSGMKARLAFAIATALEPDILLIDEVLavgdAAFQEKCQRRLRELLKQGK-TVILVSHDPSSIKRLCDRALVLEKG 218

                  ...
gi 1411607396 230 VIT 232
Cdd:cd03220   219 KIR 221
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
336-501 1.78e-15

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: 75.70  E-value: 1.78e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 336 QGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTKLevayfdqyrDQLDPeQTVMDNVGEGKQEVM-- 412
Cdd:cd03245    21 DNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLlDGTDI---------RQLDP-ADLRRNIGYVPQDVTlf 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 413 ---VR---------GRSRHIL-----GYLQDFL-FEPKRARTPV----KALSGGEKNRLLLAKLFLKPSNLLILDEPTND 470
Cdd:cd03245    91 ygtLRdnitlgaplADDERILraaelAGVTDFVnKHPNGLDLQIgergRGLSGGQRQAVALARALLNDPPILLLDEPTSA 170
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1411607396 471 LDVETLELLEELLADYPG--TLLLVSHDRRFID 501
Cdd:cd03245   171 MDMNSEERLKERLRQLLGdkTLIIITHRPSLLD 203
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
319-475 1.81e-15

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


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 75.77  E-value: 1.81e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 319 VFETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLepSRGLVKGgtklevaYFDQYRDQLDPEQ 398
Cdd:COG2401    30 VLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGAL--KGTPVAG-------CVDVPDNQFGREA 100
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1411607396 399 TVMDNVGEgKQEVMVRGRSRHILGYLQDFLFepkraRTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVET 475
Cdd:COG2401   101 SLIDAIGR-KGDFKDAVELLNAVGLSDAVLW-----LRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQT 171
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
321-473 2.04e-15

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 76.59  E-value: 2.04e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKGGTKLEVAYFD-QYRDQLD--PE 397
Cdd:PRK11231    4 RTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSrQLARRLAllPQ 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 398 QTVmdnVGEG--KQEVMVRGRSRHI-----LGYLQDFLFEPKRART--------PVKALSGGEKNRLLLAKLFLKPSNLL 462
Cdd:PRK11231   84 HHL---TPEGitVRELVAYGRSPWLslwgrLSAEDNARVNQAMEQTrinhladrRLTDLSGGQRQRAFLAMVLAQDTPVV 160
                         170
                  ....*....|.
gi 1411607396 463 ILDEPTNDLDV 473
Cdd:PRK11231  161 LLDEPTTYLDI 171
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
1-231 2.09e-15

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 78.15  E-value: 2.09e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   1 MALLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIA-------GELPLDDGRM--VQQQDLKVTRL 71
Cdd:PRK11000    1 MASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAgleditsGDLFIGEKRMndVPPAERGVGMV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  72 EQDPPASSDLTVFDYTAEG--LAGVG--ELLKKYHHIS--MELAHdpsdanirimsdlqeqldyqngwqfetrisqvltL 145
Cdd:PRK11000   81 FQSYALYPHLSVAENMSFGlkLAGAKkeEINQRVNQVAevLQLAH----------------------------------L 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 146 LNLDPDAtldsLSGGWLRKVALARALACDPDLLLLDEPTNHLD--------IEaINWLEdflKDFRGAIVFISHDREFIH 217
Cdd:PRK11000  127 LDRKPKA----LSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDaalrvqmrIE-ISRLH---KRLGRTMIYVTHDQVEAM 198
                         250
                  ....*....|....
gi 1411607396 218 KLATRIIDLDRGVI 231
Cdd:PRK11000  199 TLADKIVVLDAGRV 212
cbiO PRK13637
energy-coupling factor transporter ATPase;
19-231 2.59e-15

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 76.62  E-value: 2.59e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  19 LDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGR-MVQQQDLKVTRLEQdppasSDL-----TVFDYTAEGLa 92
Cdd:PRK13637   23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKiIIDGVDITDKKVKL-----SDIrkkvgLVFQYPEYQL- 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  93 gVGELLKKyhhismELAHDPSDANirimsdLQEQldyqngwQFETRISQVLTLLNLDPDATLD----SLSGGWLRKVALA 168
Cdd:PRK13637   97 -FEETIEK------DIAFGPINLG------LSEE-------EIENRVKRAMNIVGLDYEDYKDkspfELSGGQKRRVAIA 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1411607396 169 RALACDPDLLLLDEPTNHLDI----EAINWLEDFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVI 231
Cdd:PRK13637  157 GVVAMEPKILILDEPTAGLDPkgrdEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKC 223
COG4559 COG4559
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
321-473 3.02e-15

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


Pssm-ID: 443620 [Multi-domain]  Cd Length: 258  Bit Score: 75.92  E-value: 3.02e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGlvkggtklEVAYFDQYRDQLDPEQ-- 398
Cdd:COG4559     3 EAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSG--------EVRLNGRPLAAWSPWEla 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 399 ----------------TVmdnvgegkQEVmVR-GRSRHILGYLQDflfePKRART-------------PVKALSGGEKNR 448
Cdd:COG4559    75 rrravlpqhsslafpfTV--------EEV-VAlGRAPHGSSAAQD----RQIVREalalvglahlagrSYQTLSGGEQQR 141
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1411607396 449 LLLAKLFL-------KPSNLLILDEPTNDLDV 473
Cdd:COG4559   142 VQLARVLAqlwepvdGGPRWLFLDEPTSALDL 173
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
321-473 3.21e-15

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 77.96  E-value: 3.21e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTKLEVAYFDQYRDQLD--PE 397
Cdd:PRK09536    5 DVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLvAGDDVEALSARAASRRVAsvPQ 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 398 QTVMDNVGEGKQEVMVrGRSRHI-----LGYLQDFLFEPKRART--------PVKALSGGEKNRLLLAKLFLKPSNLLIL 464
Cdd:PRK09536   85 DTSLSFEFDVRQVVEM-GRTPHRsrfdtWTETDRAAVERAMERTgvaqfadrPVTSLSGGERQRVLLARALAQATPVLLL 163

                  ....*....
gi 1411607396 465 DEPTNDLDV 473
Cdd:PRK09536  164 DEPTASLDI 172
PLN03073 PLN03073
ABC transporter F family; Provisional
11-241 3.31e-15

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 79.13  E-value: 3.31e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  11 LSFSD----FP----LLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMVQQQDLKVTRLEQDPPASSDLT 82
Cdd:PLN03073  509 ISFSDasfgYPggplLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAVFSQHHVDGLDLS 588
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  83 V--FDYTAEGLAGVGELLKKYHHISMELAHDpsdanirimsdlqeqldyqngwqfetrisqvltlLNLDPDATLdslSGG 160
Cdd:PLN03073  589 SnpLLYMMRCFPGVPEQKLRAHLGSFGVTGN----------------------------------LALQPMYTL---SGG 631
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 161 WLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVITSWPGNYDE 240
Cdd:PLN03073  632 QKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKVTPFHGTFHD 711

                  .
gi 1411607396 241 Y 241
Cdd:PLN03073  712 Y 712
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
10-233 3.61e-15

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: 77.46  E-value: 3.61e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  10 CLSFS----DFPLldNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMVQQQdlkvtRLEQDPPASSDLTV-- 83
Cdd:TIGR02142   2 SARFSkrlgDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNG-----RTLFDSRKGIFLPPek 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  84 --FDYtaeglagVGELLKKYHHISmelahdpsdanirIMSDLQEQLDYQNGWQFETRISQVLTLLNLDP--DATLDSLSG 159
Cdd:TIGR02142  75 rrIGY-------VFQEARLFPHLS-------------VRGNLRYGMKRARPSERRISFERVIELLGIGHllGRLPGRLSG 134
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1411607396 160 GWLRKVALARALACDPDLLLLDEPTNHLDI----EAINWLEDFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVITS 233
Cdd:TIGR02142 135 GEKQRVAIGRALLSSPRLLLMDEPLAALDDprkyEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAA 212
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
4-184 4.09e-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: 74.78  E-value: 4.09e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   4 LTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMV-QQQDlkVTRLeqdPPassdlt 82
Cdd:cd03224     1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRfDGRD--ITGL---PP------ 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  83 vFDYTAEGLAGVGELLKKYHHIS----MELAhdpsdANIRIMSDLQEQLDyqngWQFE------TRISQvltllnldPDA 152
Cdd:cd03224    70 -HERARAGIGYVPEGRRIFPELTveenLLLG-----AYARRRAKRKARLE----RVYElfprlkERRKQ--------LAG 131
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1411607396 153 TldsLSGGWLRKVALARALACDPDLLLLDEPT 184
Cdd:cd03224   132 T---LSGGEQQMLAIARALMSRPKLLLLDEPS 160
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
323-472 4.12e-15

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


Pssm-ID: 440744 [Multi-domain]  Cd Length: 241  Bit Score: 75.40  E-value: 4.12e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 323 EGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGlvkggtklEVAYFDQYRDQLDPEQ---- 398
Cdd:COG1127     9 RNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSG--------EILVDGQDITGLSEKElyel 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 399 -----------------TVMDNVG------EGKQEVMVRGRSRHIL---GyLQDFlfepkRARTPvKALSGGEKNRLLLA 452
Cdd:COG1127    81 rrrigmlfqggalfdslTVFENVAfplrehTDLSEAEIRELVLEKLelvG-LPGA-----ADKMP-SELSGGMRKRVALA 153
                         170       180
                  ....*....|....*....|.
gi 1411607396 453 K-LFLKPSnLLILDEPTNDLD 472
Cdd:COG1127   154 RaLALDPE-ILLYDEPTAGLD 173
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
24-231 4.40e-15

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 75.05  E-value: 4.40e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  24 LSIERGERLCLVGRNGAGKSTLMKIiageLPLddgrmvqqqdlkvtrLEQdpPASSDLTV----FDYTA-----EGLA-- 92
Cdd:PRK11124   23 LDCPQGETLVLLGPSGAGKSSLLRV----LNL---------------LEM--PRSGTLNIagnhFDFSKtpsdkAIRElr 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  93 -GVGELLKKYH---HisMELAHDPSDANIRIMSdLQEQldyqngwQFETRISQVLTLLNLDP--DATLDSLSGGWLRKVA 166
Cdd:PRK11124   82 rNVGMVFQQYNlwpH--LTVQQNLIEAPCRVLG-LSKD-------QALARAEKLLERLRLKPyaDRFPLHLSGGQQQRVA 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1411607396 167 LARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRG-AI--VFISHDREFIHKLATRIIDLDRGVI 231
Cdd:PRK11124  152 IARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAEtGItqVIVTHEVEVARKTASRVVYMENGHI 219
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
19-231 5.30e-15

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 76.66  E-value: 5.30e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  19 LDNAELSIERGERLCLVGRNGAGKSTLMKIIAG-ELPlDDGR-MVQQQDLkvTRLEQDppassdltvfdytaeglagvgE 96
Cdd:COG1135    21 LDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLlERP-TSGSvLVDGVDL--TALSER---------------------E 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  97 LLKKYHHISMELAHdpsdANIrimsdLQEQLDYQN--------GW---QFETRISQVLTLLNLDP--DATLDSLSGGWLR 163
Cdd:COG1135    77 LRAARRKIGMIFQH----FNL-----LSSRTVAENvalpleiaGVpkaEIRKRVAELLELVGLSDkaDAYPSQLSGGQKQ 147
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1411607396 164 KVALARALACDPDLLLLDEPTNHLDIE---AInwLeDFLKDFRG----AIVFISHDREFIHKLATRIIDLDRGVI 231
Cdd:COG1135   148 RVGIARALANNPKVLLCDEATSALDPEttrSI--L-DLLKDINRelglTIVLITHEMDVVRRICDRVAVLENGRI 219
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
331-475 6.34e-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: 77.83  E-value: 6.34e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 331 DRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRG-LVKGGTKLEVAYFDQYRDQLDP--------EQTVM 401
Cdd:TIGR02203 344 DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGqILLDGHDLADYTLASLRRQVALvsqdvvlfNDTIA 423
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 402 DNVGEGKQEVMVRGRSRHIL--GYLQDFLFE-PKRARTPVKA----LSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVE 474
Cdd:TIGR02203 424 NNIAYGRTEQADRAEIERALaaAYAQDFVDKlPLGLDTPIGEngvlLSGGQRQRLAIARALLKDAPILILDEATSALDNE 503

                  .
gi 1411607396 475 T 475
Cdd:TIGR02203 504 S 504
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
4-231 7.43e-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: 73.85  E-value: 7.43e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   4 LTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGrmvqqqdlkVTRLEQDPPASSDLTV 83
Cdd:cd03269     1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSG---------EVLFDGKPLDIAARNR 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  84 FDYTAE--GL---AGVGELLKKYhhismelahdpsdANIRIM--SDLQEQLDYqngWqfetrisqvLTLLNLDP--DATL 154
Cdd:cd03269    72 IGYLPEerGLypkMKVIDQLVYL-------------AQLKGLkkEEARRRIDE---W---------LERLELSEyaNKRV 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 155 DSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRGA---IVFISHDREFIHKLATRIIDLDRGVI 231
Cdd:cd03269   127 EELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAgktVILSTHQMELVEELCDRVLLLNKGRA 206
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
330-516 8.07e-15

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: 74.11  E-value: 8.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 330 GDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKGGTK----LEVAYFdqyrdqLDPEQTVMDNV- 404
Cdd:cd03220    33 GEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRvsslLGLGGG------FNPELTGRENIy 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 405 ------GEGKQEvmVRGRSRHILGY--LQDFLfepkraRTPVKALSGGEKNRLLLA-KLFLKPsNLLILDEPTNDLDVET 475
Cdd:cd03220   107 lngrllGLSRKE--IDEKIDEIIEFseLGDFI------DLPVKTYSSGMKARLAFAiATALEP-DILLIDEVLAVGDAAF 177
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1411607396 476 LELLEELLADY---PGTLLLVSHDRRFIDNTVT-GCWLFegDGRI 516
Cdd:cd03220   178 QEKCQRRLRELlkqGKTVILVSHDPSSIKRLCDrALVLE--KGKI 220
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
319-472 9.06e-15

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 74.42  E-value: 9.06e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 319 VFETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGlvkggtklEVAYFDQYRDQLDPEQ 398
Cdd:PRK13548    2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSG--------EVRLNGRPLADWSPAE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 399 ------------------TVmdnvgegkQEVMVRGRSRHILGYLQD-FLFEPKRART--------PVKALSGGEKNRLLL 451
Cdd:PRK13548   74 larrravlpqhsslsfpfTV--------EEVVAMGRAPHGLSRAEDdALVAAALAQVdlahlagrDYPQLSGGEQQRVQL 145
                         170       180
                  ....*....|....*....|....*..
gi 1411607396 452 AKLFL------KPSNLLILDEPTNDLD 472
Cdd:PRK13548  146 ARVLAqlwepdGPPRWLLLDEPTSALD 172
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
320-473 9.16e-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: 9.16e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 320 FETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGlvkggtklevayfdqyrdqldpeqt 399
Cdd:cd03216     1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSG------------------------- 55
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1411607396 400 vmdnvgegkqEVMVRGRSRHILGylqdflfePKRAR----TPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDV 473
Cdd:cd03216    56 ----------EILVDGKEVSFAS--------PRDARragiAMVYQLSVGERQMVEIARALARNARLLILDEPTAALTP 115
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
19-229 9.22e-15

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: 74.04  E-value: 9.22e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  19 LDNAELSIERGERLCLVGRNGAGKSTLMKIIAG-ELPLDDGRMVQQQDLkvtrleqDPPASSDLTVF-DYTAEGLAGVGE 96
Cdd:TIGR01184   1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGlAQPTSGGVILEGKQI-------TEPGPDRMVVFqNYSLLPWLTVRE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  97 llkkyhhiSMELAHDpsdaniRIMSDLQEQldyqngwQFETRISQVLTLLNLD--PDATLDSLSGGWLRKVALARALACD 174
Cdd:TIGR01184  74 --------NIALAVD------RVLPDLSKS-------ERRAIVEEHIALVGLTeaADKRPGQLSGGMKQRVAIARALSIR 132
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1411607396 175 PDLLLLDEPTNHLD-IEAINWLEDFLK---DFRGAIVFISHDREFIHKLATRIIDLDRG 229
Cdd:TIGR01184 133 PKVLLLDEPFGALDaLTRGNLQEELMQiweEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
12-258 9.69e-15

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 74.36  E-value: 9.69e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  12 SFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKII-------AGELPLD-----DGR-----------MVQQQ-DL- 66
Cdd:PRK09493   10 HFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCInkleeitSGDLIVDglkvnDPKvderlirqeagMVFQQfYLf 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  67 -KVTRLE-------QDPPASSDltvfdyTAEGLAGvgELLKKYHhISMELAHDPSDanirimsdlqeqldyqngwqfetr 138
Cdd:PRK09493   90 pHLTALEnvmfgplRVRGASKE------EAEKQAR--ELLAKVG-LAERAHHYPSE------------------------ 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 139 isqvltllnldpdatldsLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDF--RG-AIVFISHDREF 215
Cdd:PRK09493  137 ------------------LSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLaeEGmTMVIVTHEIGF 198
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1411607396 216 IHKLATRIIDLDRGVITSwPGNYDEYLQGK-EEALRvEELQHAE 258
Cdd:PRK09493  199 AEKVASRLIFIDKGRIAE-DGDPQVLIKNPpSQRLQ-EFLQHVS 240
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
3-229 9.87e-15

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 76.41  E-value: 9.87e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   3 LLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAG-ELPLDDGRMVQQQDLKVTRLEQDPpassdl 81
Cdd:PRK11607   19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGfEQPTAGQIMLDGVDLSHVPPYQRP------ 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  82 tvfdytaeglagVGELLKKYH---HISMElahdpsdANIRIMSDlQEQLDYQngwQFETRISQVLTLLNLDPDATLD--S 156
Cdd:PRK11607   93 ------------INMMFQSYAlfpHMTVE-------QNIAFGLK-QDKLPKA---EIASRVNEMLGLVHMQEFAKRKphQ 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1411607396 157 LSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLE----DFLKDFRGAIVFISHDREFIHKLATRIIDLDRG 229
Cdd:PRK11607  150 LSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQlevvDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRG 226
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
17-212 1.44e-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: 76.63  E-value: 1.44e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  17 PLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRmVQQQDLKVTRLEQDPPAS------SDLTVFDYTaeg 90
Cdd:TIGR02868 349 PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGE-VTLDGVPVSSLDQDEVRRrvsvcaQDAHLFDTT--- 424
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  91 lagVGELLKkyhhismeLAH-DPSDANI-------RIMSDLQEQLDYQNGWqfetrisqvltllnLDPDATldSLSGGWL 162
Cdd:TIGR02868 425 ---VRENLR--------LARpDATDEELwaalervGLADWLRALPDGLDTV--------------LGEGGA--RLSGGER 477
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1411607396 163 RKVALARALACDPDLLLLDEPTNHLDIE-AINWLEDFLKDFRG-AIVFISHD 212
Cdd:TIGR02868 478 QRLALARALLADAPILLLDEPTEHLDAEtADELLEDLLAALSGrTVVLITHH 529
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
25-227 1.47e-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: 73.60  E-value: 1.47e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  25 SIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMVQQQDlKVTRLEQDPPASSDLTVFDYTAEGLAGVGEllkkyhhi 104
Cdd:cd03237    21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELD-TVSYKPQYIKADYEGTVRDLLSSITKDFYT-------- 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 105 smelahDPsdanirimsdlqeqldyqngwQFETRISQVLTLLNLdPDATLDSLSGGWLRKVALARALACDPDLLLLDEPT 184
Cdd:cd03237    92 ------HP---------------------YFKTEIAKPLQIEQI-LDREVPELSGGELQRVAIAACLSKDADIYLLDEPS 143
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1411607396 185 NHLDIE-------AINWLedFLKDFRGAIVfISHDREFIHKLATRIIDLD 227
Cdd:cd03237   144 AYLDVEqrlmaskVIRRF--AENNEKTAFV-VEHDIIMIDYLADRLIVFE 190
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
329-475 1.52e-14

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


Pssm-ID: 213229 [Multi-domain]  Cd Length: 213  Bit Score: 72.95  E-value: 1.52e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 329 FGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRG-LVKGGTKL------------EVAY-FDQYrdQL 394
Cdd:cd03262    10 FGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGtIIIDGLKLtddkkninelrqKVGMvFQQF--NL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 395 DPEQTVMDNVGEGkqEVMVRGRSR-----HILGYLQDFLFEPKRARTPVKaLSGGEKNRLLLAK-LFLKPSnLLILDEPT 468
Cdd:cd03262    88 FPHLTVLENITLA--PIKVKGMSKaeaeeRALELLEKVGLADKADAYPAQ-LSGGQQQRVAIARaLAMNPK-VMLFDEPT 163

                  ....*..
gi 1411607396 469 NDLDVET 475
Cdd:cd03262   164 SALDPEL 170
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
1-183 1.86e-14

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


Pssm-ID: 440752 [Multi-domain]  Cd Length: 240  Bit Score: 73.14  E-value: 1.86e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   1 MALLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGR-MVQQQDlkVTR--------- 70
Cdd:COG1137     1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRiFLDGED--ITHlpmhkrarl 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  71 ----LEQDPPASSDLTVfdytAEGLAGVGELLKKyhhismelahdpsdanirimsDLQEQldyqngwqfETRISQVLTLL 146
Cdd:COG1137    79 gigyLPQEASIFRKLTV----EDNILAVLELRKL---------------------SKKER---------EERLEELLEEF 124
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1411607396 147 NLDP--DATLDSLSGGWLRKVALARALACDPDLLLLDEP 183
Cdd:COG1137   125 GITHlrKSKAYSLSGGERRRVEIARALATNPKFILLDEP 163
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
338-495 2.05e-14

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 76.42  E-value: 2.05e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 338 LDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLePSRGLVK-GGTKLEVAYFDQYRDQLD--------PEQTVMDNVGEGK 408
Cdd:PRK11174  369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKiNGIELRELDPESWRKHLSwvgqnpqlPHGTLRDNVLLGN 447
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 409 QEvMVRGRSRHIL--GYLQDFLFE-PKRARTPVK----ALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDV--ETLELL 479
Cdd:PRK11174  448 PD-ASDEQLQQALenAWVSEFLPLlPQGLDTPIGdqaaGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAhsEQLVMQ 526
                         170
                  ....*....|....*.
gi 1411607396 480 EELLADYPGTLLLVSH 495
Cdd:PRK11174  527 ALNAASRRQTTLMVTH 542
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
11-247 2.21e-14

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 73.87  E-value: 2.21e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  11 LSFS----DFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGEL-PLD-----DGRMVQQQDLKVTR-----LEQDP 75
Cdd:PRK13632   13 VSFSypnsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLkPQSgeikiDGITISKENLKEIRkkigiIFQNP 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  76 passD-----LTVFDYTAEGLAGvgellKKYhhismelahDPSDANiRIMSDLQEQLDYQNgwqfetrisqvltLLNLDP 150
Cdd:PRK13632   93 ----DnqfigATVEDDIAFGLEN-----KKV---------PPKKMK-DIIDDLAKKVGMED-------------YLDKEP 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 151 datlDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRG----AIVFISHDREFIhKLATRIIDL 226
Cdd:PRK13632  141 ----QNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKtrkkTLISITHDMDEA-ILADKVIVF 215
                         250       260
                  ....*....|....*....|..
gi 1411607396 227 DRG-VITSwpGNYDEYLQGKEE 247
Cdd:PRK13632  216 SEGkLIAQ--GKPKEILNNKEI 235
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
6-231 2.29e-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: 2.29e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   6 LHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLmkiiagelplddgrmvqqqdLKVTRLeQDPPASSDLTV-- 83
Cdd:COG4161     5 LKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSL--------------------LRVLNL-LETPDSGQLNIag 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  84 --FDYTAEGLAGVGELLKK--------YH---HISmelahdpsdanirIMSDLQE---QLDYQNGWQFETRISQVLTLLN 147
Cdd:COG4161    64 hqFDFSQKPSEKAIRLLRQkvgmvfqqYNlwpHLT-------------VMENLIEapcKVLGLSKEQAREKAMKLLARLR 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 148 LDP--DATLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRG-AI--VFISHDREFIHKLATR 222
Cdd:COG4161   131 LTDkaDRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQtGItqVIVTHEVEFARKVASQ 210

                  ....*....
gi 1411607396 223 IIDLDRGVI 231
Cdd:COG4161   211 VVYMEKGRI 219
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
21-231 2.69e-14

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: 73.45  E-value: 2.69e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  21 NAELSIERGERLCLVGRNGAGKSTLMKII-------AGELPLDDGRMVQQQDLKVTRLEQDPPAS--------SDLTVFD 85
Cdd:cd03294    42 DVSLDVREGEIFVIMGLSGSGKSTLLRCInrlieptSGKVLIDGQDIAAMSRKELRELRRKKISMvfqsfallPHRTVLE 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  86 YTAEGLagvgellkkyhhismELAHDPsdANIRimsdlqeqldyqngwqfETRISQVLTLLNLDPDAT--LDSLSGGWLR 163
Cdd:cd03294   122 NVAFGL---------------EVQGVP--RAER-----------------EERAAEALELVGLEGWEHkyPDELSGGMQQ 167
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1411607396 164 KVALARALACDPDLLLLDEPTNHLD----IEAINWLEDFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVI 231
Cdd:cd03294   168 RVGLARALAVDPDILLMDEAFSALDplirREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRL 239
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
319-498 2.79e-14

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 72.38  E-value: 2.79e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 319 VFETEGLGLDFGD----RTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTKL----------- 382
Cdd:COG1136     4 LLELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLiDGQDIsslserelarl 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 383 ---EVAY-FDQYrdQLDPEQTVMDNV-------GEGKQEvmVRGRSRHILGYLQdfLfePKRARTPVKALSGGEKNRLLL 451
Cdd:COG1136    84 rrrHIGFvFQFF--NLLPELTALENValplllaGVSRKE--RRERARELLERVG--L--GDRLDHRPSQLSGGQQQRVAI 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1411607396 452 AK-LFLKPSnLLILDEPTNDLDVETLEL---LEELLADYPG-TLLLVSHDRR 498
Cdd:COG1136   156 ARaLVNRPK-LILADEPTGNLDSKTGEEvleLLRELNRELGtTIVMVTHDPE 206
TauB COG4525
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
1-224 2.81e-14

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


Pssm-ID: 443596 [Multi-domain]  Cd Length: 262  Bit Score: 73.36  E-value: 2.81e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   1 MALLTLHGACLSF----SDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMvqqqdlkvtRLEQDPP 76
Cdd:COG4525     1 MSMLTVRHVSVRYpgggQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEI---------TLDGVPV 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  77 ASSD---------------LTVFDYTAEGL--AGVGELlkkyhhismelahdpsdanirimsdlqeqldyqngwQFETRI 139
Cdd:COG4525    72 TGPGadrgvvfqkdallpwLNVLDNVAFGLrlRGVPKA------------------------------------ERRARA 115
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 140 SQVLTLLNLD--PDATLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDieAIN------WLEDFLKDFRGAIVFISH 211
Cdd:COG4525   116 EELLALVGLAdfARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALD--ALTreqmqeLLLDVWQRTGKGVFLITH 193
                         250
                  ....*....|...
gi 1411607396 212 DREFIHKLATRII 224
Cdd:COG4525   194 SVEEALFLATRLV 206
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
3-473 3.20e-14

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 76.05  E-value: 3.20e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   3 LLTLHGACLSFSD----FPLLDNAELSIERGERLCLVGRNGAGKS----TLMKII--AGELPLDDGRMVQQQDLKVTRLE 72
Cdd:PRK10261   12 VLAVENLNIAFMQeqqkIAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqAGGLVQCDKMLLRRRSRQVIELS 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  73 QDPPAS------SDLT-VFDYTAEGLA---GVGELLKKYHHISMELAHDPSDANIRIMSDLqeqldyqngwqfeTRISQV 142
Cdd:PRK10261   92 EQSAAQmrhvrgADMAmIFQEPMTSLNpvfTVGEQIAESIRLHQGASREEAMVEAKRMLDQ-------------VRIPEA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 143 LTLLNLDPDatldSLSGGWLRKVALARALACDPDLLLLDEPTNHLDI----EAINWLEDFLKDFRGAIVFISHDREFIHK 218
Cdd:PRK10261  159 QTILSRYPH----QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVtiqaQILQLIKVLQKEMSMGVIFITHDMGVVAE 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 219 LATRIIDLDRGVITswpgnydeylqgkeEALRVEELQHAEfdrklaqEEVWVRQGIKArrtrnegrVRALEAMR------ 292
Cdd:PRK10261  235 IADRVLVMYQGEAV--------------ETGSVEQIFHAP-------QHPYTRALLAA--------VPQLGAMKgldypr 285
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 293 ------MERSQRRELQ--------GKAKLQMDDV-----------NRSGKLVFETEGLGLDfgdrtlfqgldlqVLRGDK 347
Cdd:PRK10261  286 rfplisLEHPAKQEPPieqdtvvdGEPILQVRNLvtrfplrsgllNRVTREVHAVEKVSFD-------------LWPGET 352
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 348 IALVGPNGCGKSTLIKLLLGQLEPSRG-LVKGGTKLEV---------------AYFDQYRdQLDPEQTVMDNVGEG-KQE 410
Cdd:PRK10261  353 LSLVGESGSGKSTTGRALLRLVESQGGeIIFNGQRIDTlspgklqalrrdiqfIFQDPYA-SLDPRQTVGDSIMEPlRVH 431
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1411607396 411 VMVRGRS--RHILGYLQDFLFEPKRARTPVKALSGGEKNRLLLAK-LFLKPsNLLILDEPTNDLDV 473
Cdd:PRK10261  432 GLLPGKAaaARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARaLALNP-KVIIADEAVSALDV 496
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
338-475 3.52e-14

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: 72.26  E-value: 3.52e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 338 LDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRG--LVKGgtkLEVAYF--DQYRDQL-----DP---EQTVMDNVG 405
Cdd:cd03251    21 ISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGriLIDG---HDVRDYtlASLRRQIglvsqDVflfNDTVAENIA 97
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1411607396 406 EGKQEVM---VRGRSRhiLGYLQDFLFE-PKRARTPVK----ALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVET 475
Cdd:cd03251    98 YGRPGATreeVEEAAR--AANAHEFIMElPEGYDTVIGergvKLSGGQRQRIAIARALLKDPPILILDEATSALDTES 173
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
323-474 4.09e-14

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: 71.84  E-value: 4.09e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 323 EGLGLDFGDRTLFQGLDLQVLRGdKIALVGPNGCGKSTLIKLLLGQLEPSRGLVkggtklevayfdqYRDQLDpeqtvmd 402
Cdd:cd03264     4 ENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTI-------------RIDGQD------- 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 403 nVGEGKQEVmvrgrsRHILGYL-QDFLFEPK------------------------------------RARTPVKALSGGE 445
Cdd:cd03264    63 -VLKQPQKL------RRRIGYLpQEFGVYPNftvrefldyiawlkgipskevkarvdevlelvnlgdRAKKKIGSLSGGM 135
                         170       180
                  ....*....|....*....|....*....
gi 1411607396 446 KNRLLLAKLFLKPSNLLILDEPTNDLDVE 474
Cdd:cd03264   136 RRRVGIAQALVGDPSILIVDEPTAGLDPE 164
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
15-231 5.47e-14

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: 75.14  E-value: 5.47e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  15 DFPLLDNAELSIERGERLCLVGRNGAGKSTLMKII-------AGELPLDDgrmVQQQDLKVTRLE-QDPPASSDLTVFDY 86
Cdd:TIGR02203 344 DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIprfyepdSGQILLDG---HDLADYTLASLRrQVALVSQDVVLFND 420
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  87 TAEGLAGVGELlkkyhhismelaHDPSDANIR---IMSDLQEQLD-YQNGWQFETRISQVLtllnldpdatldsLSGGWL 162
Cdd:TIGR02203 421 TIANNIAYGRT------------EQADRAEIEralAAAYAQDFVDkLPLGLDTPIGENGVL-------------LSGGQR 475
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1411607396 163 RKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDF---RGAIVfISHDREFIHKlATRIIDLDRGVI 231
Cdd:TIGR02203 476 QRLAIARALLKDAPILILDEATSALDNESERLVQAALERLmqgRTTLV-IAHRLSTIEK-ADRIVVMDDGRI 545
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
331-475 6.48e-14

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: 71.80  E-value: 6.48e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 331 DRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTKLEVAYFDQYRDQL-----DP---EQTVM 401
Cdd:cd03249    15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILlDGVDIRDLNLRWLRSQIglvsqEPvlfDGTIA 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 402 DNVGEGK---QEVMVRGRSRhiLGYLQDFLFE-PKRARTPVKA----LSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDV 473
Cdd:cd03249    95 ENIRYGKpdaTDEEVEEAAK--KANIHDFIMSlPDGYDTLVGErgsqLSGGQKQRIAIARALLRNPKILLLDEATSALDA 172

                  ..
gi 1411607396 474 ET 475
Cdd:cd03249   173 ES 174
BtuD COG4138
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ...
24-284 7.09e-14

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


Pssm-ID: 443313 [Multi-domain]  Cd Length: 248  Bit Score: 71.80  E-value: 7.09e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  24 LSIERGERLCLVGRNGAGKSTLMKIIAGELP-----LDDGRMVQQ---QDLKVTR--LEQDPPASSDLTVFDYtaeglag 93
Cdd:COG4138    17 AQVNAGELIHLIGPNGAGKSTLLARMAGLLPgqgeiLLNGRPLSDwsaAELARHRayLSQQQSPPFAMPVFQY------- 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  94 vgellkkyhhISMELAHDPSDANIrimsdlqeqldyqngwqfETRISQVLTLLNLDP--DATLDSLSGG-WLRkVALARA 170
Cdd:COG4138    90 ----------LALHQPAGASSEAV------------------EQLLAQLAEALGLEDklSRPLTQLSGGeWQR-VRLAAV 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 171 L-----ACDPD--LLLLDEPTNHLDIEAINWLEDFLKDFR---GAIVFISHDreFIHKL--ATRIIDLDRGVITSwpgny 238
Cdd:COG4138   141 LlqvwpTINPEgqLLLLDEPMNSLDVAQQAALDRLLRELCqqgITVVMSSHD--LNHTLrhADRVWLLKQGKLVA----- 213
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1411607396 239 deylQGK-EEALRVEELQHAeFdrklaqeevwvrqGIKARRTRNEGR 284
Cdd:COG4138   214 ----SGEtAEVMTPENLSEV-F-------------GVKFRRLEVEGH 242
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
15-231 7.54e-14

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


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 71.65  E-value: 7.54e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  15 DFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRmvqqqdlkVTR-------LEQ----DPpassDLTV 83
Cdd:COG1134    38 EFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGR--------VEVngrvsalLELgagfHP----ELTG 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  84 FDytaeglagvgellkkyhhismelahdpsdaNIRImsdlqeqldyqNGwqfetrisqvlTLLNL---DPDATLD----- 155
Cdd:COG1134   106 RE------------------------------NIYL-----------NG-----------RLLGLsrkEIDEKFDeivef 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 156 ------------SLSGGWLRKVALARALACDPDLLLLDEPTNHLDIE----AINWLEDFLKDFRgAIVFISHDREFIHKL 219
Cdd:COG1134   134 aelgdfidqpvkTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAfqkkCLARIRELRESGR-TVIFVSHSMGAVRRL 212
                         250
                  ....*....|..
gi 1411607396 220 ATRIIDLDRGVI 231
Cdd:COG1134   213 CDRAIWLEKGRL 224
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
316-475 8.57e-14

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: 71.10  E-value: 8.57e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 316 GKLVFETEGLGLDFGDRTLfQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTKLEVAYFDQYRDQL 394
Cdd:cd03254     1 GEIEFENVNFSYDEKKPVL-KDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILiDGIDIRDISRKSLRSMI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 395 -----DP---EQTVMDNVGEGKQ-----EVMVRGRSRHILgylqDFL-FEPKRARTPV----KALSGGEKNRLLLAKLFL 456
Cdd:cd03254    80 gvvlqDTflfSGTIMENIRLGRPnatdeEVIEAAKEAGAH----DFImKLPNGYDTVLgengGNLSQGERQLLAIARAML 155
                         170
                  ....*....|....*....
gi 1411607396 457 KPSNLLILDEPTNDLDVET 475
Cdd:cd03254   156 RDPKILILDEATSNIDTET 174
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
4-228 8.59e-14

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


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 70.59  E-value: 8.59e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   4 LTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELP----------LDDGRM--VQQQDLKVTRL 71
Cdd:COG4136     2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSpafsasgevlLNGRRLtaLPAEQRRIGIL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  72 EQDPPASSDLTVfdytAEGLAgvgellkkyhhisMELAHDPSDANIRimsdlqeqldyqngwqfeTRISQVLTLLNLDP- 150
Cdd:COG4136    82 FQDDLLFPHLSV----GENLA-------------FALPPTIGRAQRR------------------ARVEQALEEAGLAGf 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 151 -DATLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDF----LKDFRGAIVFISHDREFIhKLATRIID 225
Cdd:COG4136   127 aDRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQFREFvfeqIRQRGIPALLVTHDEEDA-PAAGRVLD 205

                  ...
gi 1411607396 226 LDR 228
Cdd:COG4136   206 LGN 208
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
3-231 1.00e-13

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


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 71.18  E-value: 1.00e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   3 LLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMV--------QQQDLKVTRLE-- 72
Cdd:COG1126     1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITvdgedltdSKKDINKLRRKvg 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  73 ---QD----PpassDLTVFDYTAEGLAGVgelLKKyhhismelahDPSDANIRIMS-----DLQEQLD-Yqngwqfetri 139
Cdd:COG1126    81 mvfQQfnlfP----HLTVLENVTLAPIKV---KKM----------SKAEAEERAMEllervGLADKADaY---------- 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 140 sqvltllnldPDatldSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRGA---IVFISHDREFI 216
Cdd:COG1126   134 ----------PA----QLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEgmtMVVVTHEMGFA 199
                         250
                  ....*....|....*
gi 1411607396 217 HKLATRIIDLDRGVI 231
Cdd:COG1126   200 REVADRVVFMDGGRI 214
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
19-229 1.05e-13

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 73.97  E-value: 1.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  19 LDNAELSIERGERLCLVGRNGAGKST----LMKIIA--GELPLDDGRMVQ---QQDLKVTR----LEQDPPASSD--LTV 83
Cdd:PRK15134  302 VKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINsqGEIWFDGQPLHNlnrRQLLPVRHriqvVFQDPNSSLNprLNV 381
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  84 FDYTAEGLagvgellkKYHHISMELAhdpsdanirimsdlqeqldyqngwQFETRISQVLTLLNLDPDATL---DSLSGG 160
Cdd:PRK15134  382 LQIIEEGL--------RVHQPTLSAA------------------------QREQQVIAVMEEVGLDPETRHrypAEFSGG 429
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1411607396 161 WLRKVALARALACDPDLLLLDEPTNHLD--IEA--INWLEDFLKDFRGAIVFISHDREFIHKLATRIIDLDRG 229
Cdd:PRK15134  430 QRQRIAIARALILKPSLIILDEPTSSLDktVQAqiLALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQG 502
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
11-232 1.19e-13

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: 69.65  E-value: 1.19e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  11 LSFS----DFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELplddgrmVQQQdlkvtrleqdppassdltvfdy 86
Cdd:cd03247     6 VSFSypeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDL-------KPQQ---------------------- 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  87 taeglagvGELLKKYHHISmelahdpsdanirimsDLQEQLdyqngwqfetriSQVLTLLNLDP---DATLDS-----LS 158
Cdd:cd03247    57 --------GEITLDGVPVS----------------DLEKAL------------SSLISVLNQRPylfDTTLRNnlgrrFS 100
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1411607396 159 GGWLRKVALARALACDPDLLLLDEPTNHLD----IEAINWLEDFLKDfrGAIVFISHDREFIHKlATRIIDLDRGVIT 232
Cdd:cd03247   101 GGERQRLALARILLQDAPIVLLDEPTVGLDpiteRQLLSLIFEVLKD--KTLIWITHHLTGIEH-MDKILFLENGKII 175
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
344-520 1.23e-13

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


Pssm-ID: 213204 [Multi-domain]  Cd Length: 246  Bit Score: 70.90  E-value: 1.23e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 344 RGDKIALVGPNGCGKSTLIKLLLGQLEPSRGlvKGGTKLE-VAYFDQYRdQLDPEQTVMDNVGEGKQEVMVRGRSR-HIL 421
Cdd:cd03237    24 ESEVIGILGPNGIGKTTFIKMLAGVLKPDEG--DIEIELDtVSYKPQYI-KADYEGTVRDLLSSITKDFYTHPYFKtEIA 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 422 GYLQ-DFLFEPKrartpVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVETLelleelladypgtLLLVSHDRRFI 500
Cdd:cd03237   101 KPLQiEQILDRE-----VPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQR-------------LMASKVIRRFA 162
                         170       180
                  ....*....|....*....|
gi 1411607396 501 DNTVTGCWLFEGDGRISDYV 520
Cdd:cd03237   163 ENNEKTAFVVEHDIIMIDYL 182
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
11-229 1.49e-13

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: 72.44  E-value: 1.49e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  11 LSFSDFPLldNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMV----------QQQDLKVTR-----LEQDP 75
Cdd:COG4148     9 LRRGGFTL--DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRlggevlqdsaRGIFLPPHRrrigyVFQEA 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  76 PASSDLTVfdytaeglagvgellkkyhhismelahdpsdanirimsdlQEQLDY--QNGWQFETRIS--QVLTLLNLDP- 150
Cdd:COG4148    87 RLFPHLSV----------------------------------------RGNLLYgrKRAPRAERRISfdEVVELLGIGHl 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 151 -DATLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDI----EAINWLEDFLKDFRGAIVFISHDREFIHKLATRIID 225
Cdd:COG4148   127 lDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLarkaEILPYLERLRDELDIPILYVSHSLDEVARLADHVVL 206

                  ....
gi 1411607396 226 LDRG 229
Cdd:COG4148   207 LEQG 210
hmuV PRK13547
heme ABC transporter ATP-binding protein;
18-231 1.54e-13

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 71.40  E-value: 1.54e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  18 LLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLD--------------DGRMVQQQD-LKVTRLEQDPPASSDlT 82
Cdd:PRK13547   16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvtgdvtlNGEPLAAIDaPRLARLRAVLPQAAQ-P 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  83 VFDYTAEGLAgvgeLLKKYHHISMELAHDPSDANIrimsdlqeqldyqngwqfetrISQVLTLLNLDPDATLD--SLSGG 160
Cdd:PRK13547   95 AFAFSAREIV----LLGRYPHARRAGALTHRDGEI---------------------AWQALALAGATALVGRDvtTLSGG 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 161 WLRKVALARALA---------CDPDLLLLDEPTNHLDI----EAINWLEDFLKDFRGAIVFISHDREFIHKLATRIIDLD 227
Cdd:PRK13547  150 ELARVQFARVLAqlwpphdaaQPPRYLLLDEPTAALDLahqhRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLA 229

                  ....
gi 1411607396 228 RGVI 231
Cdd:PRK13547  230 DGAI 233
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
1-211 2.56e-13

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 72.65  E-value: 2.56e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   1 MALLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELP--------LDDGRMVQQQDLKVTR-- 70
Cdd:PRK13549    3 EYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPhgtyegeiIFEGEELQASNIRDTEra 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  71 ----LEQDPPASSDLTVfdytAEglagvgellkkyhhiSMELAHDPSDANIrimsdlqeqLDYQNGWQfetRISQVLTLL 146
Cdd:PRK13549   83 giaiIHQELALVKELSV----LE---------------NIFLGNEITPGGI---------MDYDAMYL---RAQKLLAQL 131
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 147 NLD--PDATLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRG---AIVFISH 211
Cdd:PRK13549  132 KLDinPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAhgiACIYISH 201
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
1-247 2.70e-13

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 70.33  E-value: 2.70e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   1 MALLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKI------------IAGELPLDdGRMVQQQDL-- 66
Cdd:PRK14247    1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVfnrlielypearVSGEVYLD-GQDIFKMDVie 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  67 ---KVTRLEQDPPASSDLTVFDYTAEGLagvgellkKYHHIsmelahdpsdanIRIMSDLQEQLDyqngWQFETriSQVL 143
Cdd:PRK14247   80 lrrRVQMVFQIPNPIPNLSIFENVALGL--------KLNRL------------VKSKKELQERVR----WALEK--AQLW 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 144 TLLNLDPDATLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRG--AIVFISHdrefIHKLAT 221
Cdd:PRK14247  134 DEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKdmTIVLVTH----FPQQAA 209
                         250       260       270
                  ....*....|....*....|....*....|
gi 1411607396 222 RIID----LDRGVITSWPGNYDEYLQGKEE 247
Cdd:PRK14247  210 RISDyvafLYKGQIVEWGPTREVFTNPRHE 239
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
17-242 3.02e-13

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


Pssm-ID: 213218 [Multi-domain]  Cd Length: 234  Bit Score: 69.57  E-value: 3.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  17 PLLDNAELSIERGERLCLVGRNGAGKSTLMKII-------AGELPLD--DGRMVQQQDL--KVTRLEQDPPASSDlTVFD 85
Cdd:cd03251    16 PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIprfydvdSGRILIDghDVRDYTLASLrrQIGLVSQDVFLFND-TVAE 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  86 YTAEGLAGVG-----ELLKKYHhismelAHDpsdaniRIMSdLQEQLDyqngwqfeTRISQVLTllnldpdatldSLSGG 160
Cdd:cd03251    95 NIAYGRPGATreeveEAARAAN------AHE------FIME-LPEGYD--------TVIGERGV-----------KLSGG 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 161 WLRKVALARALACDPDLLLLDEPTNHLDIE---AI-NWLEDFLKDfRGAIVfISHDREFIhKLATRIIDLDRGVITSwPG 236
Cdd:cd03251   143 QRQRIAIARALLKDPPILILDEATSALDTEserLVqAALERLMKN-RTTFV-IAHRLSTI-ENADRIVVLEDGKIVE-RG 218

                  ....*.
gi 1411607396 237 NYDEYL 242
Cdd:cd03251   219 THEELL 224
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
335-531 3.23e-13

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


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 69.73  E-value: 3.23e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 335 FQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRG--LVKG--GTKLEV-AYFdqyrdqlDPEQTVMDNV----- 404
Cdd:COG1134    42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGrvEVNGrvSALLELgAGF-------HPELTGRENIylngr 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 405 --GEGKQEvmVRGRSRHILGY--LQDFLfepkraRTPVKALSGGEKNRLLLA-KLFLKPsNLLILDEPT----------- 468
Cdd:COG1134   115 llGLSRKE--IDEKFDEIVEFaeLGDFI------DQPVKTYSSGMRARLAFAvATAVDP-DILLVDEVLavgdaafqkkc 185
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1411607396 469 ----NDLdvetlelleellADYPGTLLLVSHDRRFIDNTVT-GCWLFEG----DGRISDYVGGYADMMATRA 531
Cdd:COG1134   186 lariREL------------RESGRTVIFVSHSMGAVRRLCDrAIWLEKGrlvmDGDPEEVIAAYEALLAGRE 245
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
325-496 3.28e-13

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


Pssm-ID: 213264 [Multi-domain]  Cd Length: 214  Bit Score: 69.25  E-value: 3.28e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 325 LGLDFGDRTLFQGLDLQ-VLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTKL--------------EVAY-F 387
Cdd:cd03297     2 LCVDIEKRLPDFTLKIDfDLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVlNGTVLfdsrkkinlppqqrKIGLvF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 388 DQYrdQLDPEQTVMDNV--GEGKQEVMV-RGRSRHILGYLQ-DFLfepkrARTPVKALSGGEKNRLLLAKLFLKPSNLLI 463
Cdd:cd03297    82 QQY--ALFPHLNVRENLafGLKRKRNREdRISVDELLDLLGlDHL-----LNRYPAQLSGGEKQRVALARALAAQPELLL 154
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1411607396 464 LDEPTNDLDVETLELLEEL----LADYPGTLLLVSHD 496
Cdd:cd03297   155 LDEPFSALDRALRLQLLPElkqiKKNLNIPVIFVTHD 191
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
18-266 3.70e-13

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


Pssm-ID: 440718 [Multi-domain]  Cd Length: 264  Bit Score: 70.11  E-value: 3.70e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  18 LLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGR-MVQQQDlkVTRLE------------QDPPA--SSDLT 82
Cdd:COG1101    21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSiLIDGKD--VTKLPeykrakyigrvfQDPMMgtAPSMT 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  83 VfdytAEGLAgvgelLKKYHHISMELAHDPSDANIRIMSDLQEQLDyqNGwqFETRIsqvltllnldpDATLDSLSGGWL 162
Cdd:COG1101    99 I----EENLA-----LAYRRGKRRGLRRGLTKKRRELFRELLATLG--LG--LENRL-----------DTKVGLLSGGQR 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 163 RKVALARALACDPDLLLLDEPTNHLD---IEAINWL-EDFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVITswpgnY 238
Cdd:COG1101   155 QALSLLMATLTKPKLLLLDEHTAALDpktAALVLELtEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRII-----L 229
                         250       260
                  ....*....|....*....|....*....
gi 1411607396 239 DeyLQGKE-EALRVEELQhAEFDRKLAQE 266
Cdd:COG1101   230 D--VSGEEkKKLTVEDLL-ELFEEIRGEE 255
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
6-230 4.07e-13

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 71.02  E-value: 4.07e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   6 LHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGrmvqqqdlKVTRLEQDPPASSDLtvfd 85
Cdd:PRK13536   44 LAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAG--------KITVLGVPVPARARL---- 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  86 ytaeGLAGVGeLLKKYHHISMELAhdpsdanirimsdLQEQL----DY--QNGWQFETRISQVLTLLNLD--PDATLDSL 157
Cdd:PRK13536  112 ----ARARIG-VVPQFDNLDLEFT-------------VRENLlvfgRYfgMSTREIEAVIPSLLEFARLEskADARVSDL 173
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1411607396 158 SGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDF--RG-AIVFISHDREFIHKLATRIIDLDRGV 230
Cdd:PRK13536  174 SGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLlaRGkTILLTTHFMEEAERLCDRLCVLEAGR 249
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
336-500 4.40e-13

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: 69.28  E-value: 4.40e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 336 QGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGlvkggtKLEVAYFDQY----------------RDQLDPEQT 399
Cdd:cd03267    38 KGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSG------EVRVAGLVPWkrrkkflrrigvvfgqKTQLWWDLP 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 400 VMDNVgegkqEVMVR------GRSRHILGYLQDFLFEPKRARTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDV 473
Cdd:cd03267   112 VIDSF-----YLLAAiydlppARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDV 186
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1411607396 474 ETLEL----LEELLADYPGTLLLVSHDRRFI 500
Cdd:cd03267   187 VAQENirnfLKEYNRERGTTVLLTSHYMKDI 217
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
19-229 4.45e-13

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: 67.84  E-value: 4.45e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  19 LDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRmvqqqdlkVTRLEQDPPASSdltVFDYTAEGLAGVGEll 98
Cdd:cd03215    16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGE--------ITLDGKPVTRRS---PRDAIRAGIAYVPE-- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  99 kkyhhismelahDPSDANI-RIMSdlqeqldyqngwqfetrISQVLTLLNLdpdatldsLSGGWLRKVALARALACDPDL 177
Cdd:cd03215    83 ------------DRKREGLvLDLS-----------------VAENIALSSL--------LSGGNQQKVVLARWLARDPRV 125
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1411607396 178 LLLDEPTNHLDIEAINWLEDFLKDFR---GAIVFISHDREFIHKLATRIIDLDRG 229
Cdd:cd03215   126 LILDEPTRGVDVGAKAEIYRLIRELAdagKAVLLISSELDELLGLCDRILVMYEG 180
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
321-496 4.92e-13

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


Pssm-ID: 213266 [Multi-domain]  Cd Length: 235  Bit Score: 68.90  E-value: 4.92e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 321 ETEGLGLDFGDRTLfQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLV----KGGTKL-----EVAYFdqYR 391
Cdd:cd03299     2 KVENLSKDWKEFKL-KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKIllngKDITNLppekrDISYV--PQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 392 DQ-LDPEQTVMDNVGEG--KQEVMVRGRSRHILGYLQDFLFEPKRARTPvKALSGGEKNRLLLAK-LFLKPSnLLILDEP 467
Cdd:cd03299    79 NYaLFPHMTVYKNIAYGlkKRKVDKKEIERKVLEIAEMLGIDHLLNRKP-ETLSGGEQQRVAIARaLVVNPK-ILLLDEP 156
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1411607396 468 TNDLDVETLELLEELLAD----YPGTLLLVSHD 496
Cdd:cd03299   157 FSALDVRTKEKLREELKKirkeFGVTVLHVTHD 189
cbiO TIGR01166
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ...
330-472 4.98e-13

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


Pssm-ID: 130234 [Multi-domain]  Cd Length: 190  Bit Score: 67.83  E-value: 4.98e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 330 GDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLV-KGGTKLE------------VAYFDQyrdqlDP 396
Cdd:TIGR01166   3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVlIDGEPLDysrkgllerrqrVGLVFQ-----DP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 397 EQTVMD-NVGE---------GKQEVMVRGRSRHILGYLQDFLFEPKrartPVKALSGGEKNRLLLAKLFLKPSNLLILDE 466
Cdd:TIGR01166  78 DDQLFAaDVDQdvafgplnlGLSEAEVERRVREALTAVGASGLRER----PTHCLSGGEKKRVAIAGAVAMRPDVLLLDE 153

                  ....*.
gi 1411607396 467 PTNDLD 472
Cdd:TIGR01166 154 PTAGLD 159
cbiO PRK13645
energy-coupling factor transporter ATPase;
15-233 5.35e-13

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 70.04  E-value: 5.35e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  15 DFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMVQQqDLKVtrleqdpPASSDLT--VFDYTAEglA 92
Cdd:PRK13645   23 EFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVG-DYAI-------PANLKKIkeVKRLRKE--I 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  93 GVGELLKKYHHISMELAHDPSDANIRIMSDLQEQldYQngwqfetRISQVLTLLNLDPDATLDS---LSGGWLRKVALAR 169
Cdd:PRK13645   93 GLVFQFPEYQLFQETIEKDIAFGPVNLGENKQEA--YK-------KVPELLKLVQLPEDYVKRSpfeLSGGQKRRVALAG 163
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1411607396 170 ALACDPDLLLLDEPTNHLDIEA----INWLEDFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVITS 233
Cdd:PRK13645  164 IIAMDGNTLVLDEPTGGLDPKGeedfINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVIS 231
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
18-255 5.63e-13

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: 69.05  E-value: 5.63e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  18 LLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGR-MVQQQDLKVTRLE----QDPPASSDLTVFDYT-AEGL 91
Cdd:cd03252    17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRvLVDGHDLALADPAwlrrQVGVVLQENVLFNRSiRDNI 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  92 AGVGELLKKYHHI---SMELAHDpsdaNIRIMSDLQEQLDYQNGwqfetrisqvltllnldpdatlDSLSGGWLRKVALA 168
Cdd:cd03252    97 ALADPGMSMERVIeaaKLAGAHD----FISELPEGYDTIVGEQG----------------------AGLSGGQRQRIAIA 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 169 RALACDPDLLLLDEPTNHLDIEAINWLEDFLKDF---RGAIVfISHDREFIhKLATRIIDLDRGVITSwPGNYDEYLQGK 245
Cdd:cd03252   151 RALIHNPRILIFDEATSALDYESEHAIMRNMHDIcagRTVII-IAHRLSTV-KNADRIIVMEKGRIVE-QGSHDELLAEN 227
                         250
                  ....*....|
gi 1411607396 246 EEALRVEELQ 255
Cdd:cd03252   228 GLYAYLYQLQ 237
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
1-188 6.56e-13

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 68.77  E-value: 6.56e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   1 MALLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMVQQQDlkvtrleqdppassD 80
Cdd:PRK10895    1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDE--------------D 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  81 LTVFDYTAEGLAGVGELLKKYHHISMELAHDPSDANIRIMSDLQEQldyqngwQFETRISQVLTLLNLD--PDATLDSLS 158
Cdd:PRK10895   67 ISLLPLHARARRGIGYLPQEASIFRRLSVYDNLMAVLQIRDDLSAE-------QREDRANELMEEFHIEhlRDSMGQSLS 139
                         170       180       190
                  ....*....|....*....|....*....|
gi 1411607396 159 GGWLRKVALARALACDPDLLLLDEPTNHLD 188
Cdd:PRK10895  140 GGERRRVEIARALAANPKFILLDEPFAGVD 169
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
24-251 7.69e-13

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 68.46  E-value: 7.69e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  24 LSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRM-VQQQDLKVTrleqdPPAS-------------SDLTVFDYTAE 89
Cdd:PRK10771   20 LTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLtLNGQDHTTT-----PPSRrpvsmlfqennlfSHLTVAQNIGL 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  90 GLagvgellkkyhhismelahdpsDANIRIMSDLQEQLdyqngwqfETRISQV--LTLLNLDPDAtldsLSGGWLRKVAL 167
Cdd:PRK10771   95 GL----------------------NPGLKLNAAQREKL--------HAIARQMgiEDLLARLPGQ----LSGGQRQRVAL 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 168 ARALACDPDLLLLDEPTNHLD----IEAINWLEDFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVItSWPGNYDEYLQ 243
Cdd:PRK10771  141 ARCLVREQPILLLDEPFSALDpalrQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRI-AWDGPTDELLS 219

                  ....*...
gi 1411607396 244 GKEEALRV 251
Cdd:PRK10771  220 GKASASAL 227
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
321-474 8.02e-13

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 67.52  E-value: 8.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTKLEvAYFDQYRDQL----- 394
Cdd:PRK13538    3 EARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLwQGEPIR-RQRDEYHQDLlylgh 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 395 ----DPEQTVMDNV-------GEGKQEVMVRGRSRHILGylqdflfepKRARTPVKALSGGEKNRLLLAKLFLKPSNLLI 463
Cdd:PRK13538   82 qpgiKTELTALENLrfyqrlhGPGDDEALWEALAQVGLA---------GFEDVPVRQLSAGQQRRVALARLWLTRAPLWI 152
                         170
                  ....*....|.
gi 1411607396 464 LDEPTNDLDVE 474
Cdd:PRK13538  153 LDEPFTAIDKQ 163
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
2-233 9.40e-13

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


Pssm-ID: 443338 [Multi-domain]  Cd Length: 233  Bit Score: 68.23  E-value: 9.40e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   2 ALLTLHGACLSFSD----FPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAG-ELPlDDGR-MVQQQDLkvTRLEQDP 75
Cdd:COG4181     7 PIIELRGLTKTVGTgageLTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGlDRP-TSGTvRLAGQDL--FALDEDA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  76 PAssdltvfdytaeGL--AGVGELLKKYHHI-SM----------ELAHDPsDAnirimsdlqeqldyqngwqfETRISQV 142
Cdd:COG4181    84 RA------------RLraRHVGFVFQSFQLLpTLtalenvmlplELAGRR-DA--------------------RARARAL 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 143 LTLLNLDP--DATLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEA----INWLEDFLKDFRGAIVFISHDREfi 216
Cdd:COG4181   131 LERVGLGHrlDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATgeqiIDLLFELNRERGTTLVLVTHDPA-- 208
                         250       260
                  ....*....|....*....|
gi 1411607396 217 hkLAT---RIIDLDRGVITS 233
Cdd:COG4181   209 --LAArcdRVLRLRAGRLVE 226
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
11-232 1.09e-12

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 70.96  E-value: 1.09e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  11 LSFS---DFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGR-MVQQQDLKvtrleqdppassdltvfDY 86
Cdd:COG1132   345 VSFSypgDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRiLIDGVDIR-----------------DL 407
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  87 TAEGLagvgellkkYHHISMELaHDPS--DANIRimsdlqEQLDYQNGWQFETRISQVLTLLNLD------PDAtLD--- 155
Cdd:COG1132   408 TLESL---------RRQIGVVP-QDTFlfSGTIR------ENIRYGRPDATDEEVEEAAKAAQAHefiealPDG-YDtvv 470
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 156 -----SLSGGWLRKVALARALACDPDLLLLDEPTNHLDIE---AINW-LEDFLKDfRGAIVfIShdrefiHKLAT----- 221
Cdd:COG1132   471 gergvNLSGGQRQRIAIARALLKDPPILILDEATSALDTEteaLIQEaLERLMKG-RTTIV-IA------HRLSTirnad 542
                         250
                  ....*....|.
gi 1411607396 222 RIIDLDRGVIT 232
Cdd:COG1132   543 RILVLDDGRIV 553
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
24-231 1.22e-12

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: 67.52  E-value: 1.22e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  24 LSIERGERLCLVGRNGAGKSTLMKIIAG-ELPLDDGRMVQQQDLK--------VTRLEQDPPASSDLTVFDYTAEGLAgv 94
Cdd:cd03298    19 LTFAQGEITAIVGPSGSGKSTLLNLIAGfETPQSGRVLINGVDVTaappadrpVSMLFQENNLFAHLTVEQNVGLGLS-- 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  95 gellkkyhhismelahdpsdANIRIMSDLQEQLDY---QNGWQ-FETRISqvltllnldpdatlDSLSGGWLRKVALARA 170
Cdd:cd03298    97 --------------------PGLKLTAEDRQAIEValaRVGLAgLEKRLP--------------GELSGGERQRVALARV 142
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1411607396 171 LACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRG----AIVFISHDREFIHKLATRIIDLDRGVI 231
Cdd:cd03298   143 LVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAetkmTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
18-231 1.36e-12

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: 67.68  E-value: 1.36e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  18 LLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDD---GR-MVQQQDLKVtrlEQDPPASSDLTVFDYTAEGLAg 93
Cdd:cd03234    22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQiLFNGQPRKP---DQFQKCVAYVRQDDILLPGLT- 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  94 VGELLKKYHHISMelaHDPSDANIRIMSDLQEqldyqngwqfetrisqVLTLLNLDP--DATLDSLSGGWLRKVALARAL 171
Cdd:cd03234    98 VRETLTYTAILRL---PRKSSDAIRKKRVEDV----------------LLRDLALTRigGNLVKGISGGERRRVSIAVQL 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1411607396 172 ACDPDLLLLDEPTNHLDIEAINWLEDFLKDF----RGAIVFISHDREFIHKLATRIIDLDRGVI 231
Cdd:cd03234   159 LWDPKVLILDEPTSGLDSFTALNLVSTLSQLarrnRIVILTIHQPRSDLFRLFDRILLLSSGEI 222
BtuD COG4138
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ...
328-473 1.46e-12

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


Pssm-ID: 443313 [Multi-domain]  Cd Length: 248  Bit Score: 67.94  E-value: 1.46e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 328 DFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGqLEPSRGLVK-GGTKL------EVAYFDQYRDQLDPEQTV 400
Cdd:COG4138     5 DVAVAGRLGPISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEILlNGRPLsdwsaaELARHRAYLSQQQSPPFA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 401 MDnVGE--------GKQEVMVRGRSRHILGYLQdflFEPKRARtPVKALSGGEKNRLLLAKLFLK-------PSNLLILD 465
Cdd:COG4138    84 MP-VFQylalhqpaGASSEAVEQLLAQLAEALG---LEDKLSR-PLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLD 158

                  ....*...
gi 1411607396 466 EPTNDLDV 473
Cdd:COG4138   159 EPMNSLDV 166
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
321-473 1.64e-12

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: 66.75  E-value: 1.64e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVkggtKLEVAYFDQYRDQLDPEQTV 400
Cdd:cd03231     2 EADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRV----LLNGGPLDFQRDSIARGLLY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 401 MDNVGEGKQEVMVRGRSRHILGYLQDFLFEPKRART--------PVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:cd03231    78 LGHAPGIKTTLSVLENLRFWHADHSDEQVEEALARVglngfedrPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157

                  .
gi 1411607396 473 V 473
Cdd:cd03231   158 K 158
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
338-472 1.96e-12

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 69.09  E-value: 1.96e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 338 LDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRG-LVKGGTKLEVA---------YFDQYrdQLDPEQTVMDNVGEG 407
Cdd:PRK11607   38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGqIMLDGVDLSHVppyqrpinmMFQSY--ALFPHMTVEQNIAFG 115
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1411607396 408 -KQEVMVRG----RSRHILG--YLQDFlfepkRARTPvKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:PRK11607  116 lKQDKLPKAeiasRVNEMLGlvHMQEF-----AKRKP-HQLSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
1-224 1.97e-12

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 68.61  E-value: 1.97e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   1 MALLTLHGACLSFSD----FPLLDNAELSIERGERLCLVGRNGAGKS----TLM-------KIIAGELPLDdgrmvqQQD 65
Cdd:PRK11022    1 MALLNVDKLSVHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKSvsslAIMglidypgRVMAEKLEFN------GQD 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  66 LK--------------VTRLEQDPPASSDLTvfdYTaeglagVGellkkyhhismelahdpsdanIRIMsdlqEQLDYQN 131
Cdd:PRK11022   75 LQrisekerrnlvgaeVAMIFQDPMTSLNPC---YT------VG---------------------FQIM----EAIKVHQ 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 132 GWQFETRISQVLTLLNL----DPDATLD----SLSGGWLRKVALARALACDPDLLLLDEPTNHLD--IEA--INWLEDFL 199
Cdd:PRK11022  121 GGNKKTRRQRAIDLLNQvgipDPASRLDvyphQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDvtIQAqiIELLLELQ 200
                         250       260
                  ....*....|....*....|....*
gi 1411607396 200 KDFRGAIVFISHDREFIHKLATRII 224
Cdd:PRK11022  201 QKENMALVLITHDLALVAEAAHKII 225
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
329-472 2.10e-12

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 68.98  E-value: 2.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 329 FGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRG--LVKGG--TKLEVayfdQYRD--------QLDP 396
Cdd:PRK11432   16 FGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGqiFIDGEdvTHRSI----QQRDicmvfqsyALFP 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 397 EQTVMDNVGEG-------KQEvmVRGRSRHILGYLQDFLFEPKRartpVKALSGGEKNRLLLAK-LFLKPSNLLiLDEPT 468
Cdd:PRK11432   92 HMSLGENVGYGlkmlgvpKEE--RKQRVKEALELVDLAGFEDRY----VDQISGGQQQRVALARaLILKPKVLL-FDEPL 164

                  ....
gi 1411607396 469 NDLD 472
Cdd:PRK11432  165 SNLD 168
PRK13543 PRK13543
heme ABC exporter ATP-binding protein CcmA;
309-474 2.12e-12

heme ABC exporter ATP-binding protein CcmA;


Pssm-ID: 184129 [Multi-domain]  Cd Length: 214  Bit Score: 66.80  E-value: 2.12e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 309 MDDVNRSGKLVFETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLV----KGGTKLEV 384
Cdd:PRK13543    1 MIEPLHTAPPLLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIqidgKTATRGDR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 385 AYFDQYRDQL---DPEQTVMDNVG-----EGKQEVMVRGRSRHILGyLQDFlfepkrARTPVKALSGGEKNRLLLAKLFL 456
Cdd:PRK13543   81 SRFMAYLGHLpglKADLSTLENLHflcglHGRRAKQMPGSALAIVG-LAGY------EDTLVRQLSAGQKKRLALARLWL 153
                         170
                  ....*....|....*...
gi 1411607396 457 KPSNLLILDEPTNDLDVE 474
Cdd:PRK13543  154 SPAPLWLLDEPYANLDLE 171
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
336-468 2.13e-12

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


Pssm-ID: 213191 [Multi-domain]  Cd Length: 222  Bit Score: 66.69  E-value: 2.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 336 QGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGT-----------KLEVAYFDQYRdQLDPEQTVMDN 403
Cdd:cd03224    17 FGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRfDGRditglppheraRAGIGYVPEGR-RIFPELTVEEN 95
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1411607396 404 --VGEGKQEvmvRGRSRHILgylqDFLFE--PK---RARTPVKALSGGEKNRLLLAK-LFLKPSnLLILDEPT 468
Cdd:cd03224    96 llLGAYARR---RAKRKARL----ERVYElfPRlkeRRKQLAGTLSGGEQQMLAIARaLMSRPK-LLLLDEPS 160
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
20-224 2.19e-12

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 68.58  E-value: 2.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  20 DNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMV---------QQQDLKVTRLE-----QDPPASSD--LTV 83
Cdd:PRK15079   38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAwlgkdllgmKDDEWRAVRSDiqmifQDPLASLNprMTI 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  84 FDYTAEGLagvgellKKYHHismELAHDPSDANIRIMSdlqeqldyqngwqfeTRISQVLTLLNLDPDatldSLSGGWLR 163
Cdd:PRK15079  118 GEIIAEPL-------RTYHP---KLSRQEVKDRVKAMM---------------LKVGLLPNLINRYPH----EFSGGQCQ 168
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1411607396 164 KVALARALACDPDLLLLDEPTNHLD--IEA--INWLEDFLKDFRGAIVFISHDREFIHKLATRII 224
Cdd:PRK15079  169 RIGIARALILEPKLIICDEPVSALDvsIQAqvVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVL 233
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
3-473 2.19e-12

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


Pssm-ID: 131681 [Multi-domain]  Cd Length: 500  Bit Score: 69.85  E-value: 2.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   3 LLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDgrmvqqQDLKVTRLEQDPPASSdlt 82
Cdd:TIGR02633   1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGT------WDGEIYWSGSPLKASN--- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  83 VFDYTAEGLAGVgellkkyhHISMELAHDPSDA-NIRIMSDLQEQLDYQNGWQFETRISQVLTLLNLD--PDA-TLDSLS 158
Cdd:TIGR02633  72 IRDTERAGIVII--------HQELTLVPELSVAeNIFLGNEITLPGGRMAYNAMYLRAKNLLRELQLDadNVTrPVGDYG 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 159 GGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRG---AIVFISHDREFIHKLATRIIDLDRGvitswp 235
Cdd:TIGR02633 144 GGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAhgvACVYISHKLNEVKAVCDTICVIRDG------ 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 236 gnydeylqgkeealrveelQHAefdrklaqeevwvrqGIKARRTRNEGRVRALEAMRMERSqrrelqgkakLQMDDVNRS 315
Cdd:TIGR02633 218 -------------------QHV---------------ATKDMSTMSEDDIITMMVGREITS----------LYPHEPHEI 253
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 316 GKLVFETEGLGLDFGDRTLFQGLD---LQVLRGDKIALVGPNGCGKSTLIKLLLGQLE------------------PSRG 374
Cdd:TIGR02633 254 GDVILEARNLTCWDVINPHRKRVDdvsFSLRRGEILGVAGLVGAGRTELVQALFGAYPgkfegnvfingkpvdirnPAQA 333
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 375 LVKGgtkLEVAYFDQYRDQLDPEQTVMDNV---------------GEGKQEVMVRGRSRHILGYLQDFLfepkrartPVK 439
Cdd:TIGR02633 334 IRAG---IAMVPEDRKRHGIVPILGVGKNItlsvlksfcfkmridAAAELQIIGSAIQRLKVKTASPFL--------PIG 402
                         490       500       510
                  ....*....|....*....|....*....|....
gi 1411607396 440 ALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDV 473
Cdd:TIGR02633 403 RLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDV 436
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
336-472 2.30e-12

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 67.73  E-value: 2.30e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 336 QGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTKLEVAYFDQYRDQL-----DPEQ-----TVMDNV 404
Cdd:PRK13635   24 KDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITvGGMVLSEETVWDVRRQVgmvfqNPDNqfvgaTVQDDV 103
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1411607396 405 GEG------KQEVMVRgRSRHILG--YLQDFL-FEPKRartpvkaLSGGEKNRLLLAK-LFLKPSnLLILDEPTNDLD 472
Cdd:PRK13635  104 AFGlenigvPREEMVE-RVDQALRqvGMEDFLnREPHR-------LSGGQKQRVAIAGvLALQPD-IIILDEATSMLD 172
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
17-192 2.54e-12

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 66.44  E-value: 2.54e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  17 PLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRmvqqqdlkVTRLEQDPPASSDLTVFDYtaeglagvge 96
Cdd:PRK13539   16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGT--------IKLDGGDIDDPDVAEACHY---------- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  97 llkkyhhismeLAHdpSDANIRIMSdLQEQLDYqngW-----QFETRISQVLTLLNLDPDATL--DSLSGGWLRKVALAR 169
Cdd:PRK13539   78 -----------LGH--RNAMKPALT-VAENLEF---WaaflgGEELDIAAALEAVGLAPLAHLpfGYLSAGQKRRVALAR 140
                         170       180
                  ....*....|....*....|...
gi 1411607396 170 ALACDPDLLLLDEPTNHLDIEAI 192
Cdd:PRK13539  141 LLVSNRPIWILDEPTAALDAAAV 163
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
329-496 2.64e-12

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


Pssm-ID: 213268 [Multi-domain]  Cd Length: 213  Bit Score: 66.51  E-value: 2.64e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 329 FGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRG-LVKGG---TKLEVA------YFDQYrdQLDPEQ 398
Cdd:cd03301    10 FGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGrIYIGGrdvTDLPPKdrdiamVFQNY--ALYPHM 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 399 TVMDNV-------GEGKQEVMVRGRSR----HILGYLQdflfepkraRTPvKALSGGEKNRLLLAKLFLKPSNLLILDEP 467
Cdd:cd03301    88 TVYDNIafglklrKVPKDEIDERVREVaellQIEHLLD---------RKP-KQLSGGQRQRVALGRAIVREPKVFLMDEP 157
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1411607396 468 TNDLD----VETLELLEELLADYPGTLLLVSHD 496
Cdd:cd03301   158 LSNLDaklrVQMRAELKRLQQRLGTTTIYVTHD 190
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
321-472 3.02e-12

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: 66.69  E-value: 3.02e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 321 ETEGLGLDF-----GDRTL--FQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRG--LVK-GGTKLEVAyfdqy 390
Cdd:COG4778     6 EVENLSKTFtlhlqGGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGsiLVRhDGGWVDLA----- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 391 rdQLDPEQtvmdnvgegkqevMVRGRsRHILGYLQDFL--------------------FEPKRARTPVKAL--------- 441
Cdd:COG4778    81 --QASPRE-------------ILALR-RRTIGYVSQFLrviprvsaldvvaepllergVDREEARARARELlarlnlper 144
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1411607396 442 ---------SGGEKNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:COG4778   145 lwdlppatfSGGEQQRVNIARGFIADPPLLLLDEPTASLD 184
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
25-257 3.40e-12

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 66.88  E-value: 3.40e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  25 SIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMVQQQDLKVTRL-----------EQDPPASSdLTVFDYTAeglag 93
Cdd:PRK03695   18 EVRAGEILHLVGPNGAGKSTLLARMAGLLPGSGSIQFAGQPLEAWSAaelarhraylsQQQTPPFA-MPVFQYLT----- 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  94 vgellkkyhhismelAHDPSDANIRimsdlqeqldyqngwQFETRISQVLTLLNLDPDAT--LDSLSGG-WLRkVALARA 170
Cdd:PRK03695   92 ---------------LHQPDKTRTE---------------AVASALNEVAEALGLDDKLGrsVNQLSGGeWQR-VRLAAV 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 171 -LACDPD------LLLLDEPTNHLDIEAINWLEDFLKDF---RGAIVFISHDREFIHKLATRIIDLDRGVITSwpgnyde 240
Cdd:PRK03695  141 vLQVWPDinpagqLLLLDEPMNSLDVAQQAALDRLLSELcqqGIAVVMSSHDLNHTLRHADRVWLLKQGKLLA------- 213
                         250
                  ....*....|....*...
gi 1411607396 241 ylQGK-EEALRVEELQHA 257
Cdd:PRK03695  214 --SGRrDEVLTPENLAQV 229
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
322-472 3.55e-12

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 67.34  E-value: 3.55e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 322 TEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTKLEVAY--FDQYRDQL---- 394
Cdd:PRK13638    4 TSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLwQGKPLDYSKrgLLALRQQVatvf 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 395 -DPEQTV------------MDNVGEGKQEVMVRGRSRHILGYLQDFlfepkrARTPVKALSGGEKNRLLLAKLFLKPSNL 461
Cdd:PRK13638   84 qDPEQQIfytdidsdiafsLRNLGVPEAEITRRVDEALTLVDAQHF------RHQPIQCLSHGQKKRVAIAGALVLQARY 157
                         170
                  ....*....|.
gi 1411607396 462 LILDEPTNDLD 472
Cdd:PRK13638  158 LLLDEPTAGLD 168
ABC_tran_Xtn pfam12848
ABC transporter; This domain is an extension of some members of pfam00005 and other ...
224-300 4.59e-12

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: 62.21  E-value: 4.59e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 224 IDLDRGVITSWPGNYDEYLQGKEEALRVEELQHAEFDRKLAQEEVWV-RQGIKARRTR-NEGRVRALEAM-RMERSQRRE 300
Cdd:pfam12848   1 VELERGKLTTYKGNYSTFLEQKEERLEQQEKAYEKQQKEIKKLEEFIdRFRAKASKAKqAQSRIKALEKMeRIEKPERDK 80
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
338-473 4.90e-12

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 66.49  E-value: 4.90e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 338 LDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKGGTKL------EVAYFDQYRDQLDPEQTVMD-------NV 404
Cdd:PRK03695   15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGSGSIQFAGQPLeawsaaELARHRAYLSQQQTPPFAMPvfqyltlHQ 94
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1411607396 405 GEGKQEvmvrGRSRHILGYLQDFL-FEPKRARtPVKALSGGEKNRLLLAKLFLK------P-SNLLILDEPTNDLDV 473
Cdd:PRK03695   95 PDKTRT----EAVASALNEVAEALgLDDKLGR-SVNQLSGGEWQRVRLAAVVLQvwpdinPaGQLLLLDEPMNSLDV 166
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
12-473 4.98e-12

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 68.66  E-value: 4.98e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  12 SFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGrMVQQQDLKVTRLeqDPPASSDLtvfdytaegl 91
Cdd:PRK09700   14 SFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKG-TITINNINYNKL--DHKLAAQL---------- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  92 aGVGELlkkYHHISM--ELAhdpSDANIRIMSDLQEQLDYQN--GWQFETRISQVLTL---LNLDPDATLDSLSGGWLRK 164
Cdd:PRK09700   81 -GIGII---YQELSVidELT---VLENLYIGRHLTKKVCGVNiiDWREMRVRAAMMLLrvgLKVDLDEKVANLSISHKQM 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 165 VALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRG---AIVFISHDREFIHKLATRIIDLDRGvitswpgnydey 241
Cdd:PRK09700  154 LEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKegtAIVYISHKLAEIRRICDRYTVMKDG------------ 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 242 lqgkeealrveelqhaefdrklaqeeVWVRQGIKARRTrNEGRVRALEAmrmersqrRELQGKAKLQMDDV-NRSGKLVF 320
Cdd:PRK09700  222 --------------------------SSVCSGMVSDVS-NDDIVRLMVG--------RELQNRFNAMKENVsNLAHETVF 266
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 321 ETEGLGLDfgDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLG--------------QLEPSRGL--VKGGtkleV 384
Cdd:PRK09700  267 EVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGvdkraggeirlngkDISPRSPLdaVKKG----M 340
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 385 AYFDQYRDQ--LDPEQTVMDNVGEGKQevMVRGRSRHILGYLQDF----LFEPKRARTPVKA---------LSGGEKNRL 449
Cdd:PRK09700  341 AYITESRRDngFFPNFSIAQNMAISRS--LKDGGYKGAMGLFHEVdeqrTAENQRELLALKChsvnqniteLSGGNQQKV 418
                         490       500
                  ....*....|....*....|....
gi 1411607396 450 LLAKLFLKPSNLLILDEPTNDLDV 473
Cdd:PRK09700  419 LISKWLCCCPEVIIFDEPTRGIDV 442
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
1-472 5.88e-12

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 68.58  E-value: 5.88e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   1 MALLTLHGACLSFS----DFPLLDNAELSIERGERLCLVGRNGAGKStlmkIIAgelplddgrmvqqqdLKVTRLEQDPP 76
Cdd:PRK15134    3 QPLLAIENLSVAFRqqqtVRTVVNDVSLQIEAGETLALVGESGSGKS----VTA---------------LSILRLLPSPP 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  77 A-----------SSDLTVFDYTAEGLAGvgellkkyHHISMELAHDPSDANI--RIMSDLQEQLDYQNGWQFETRISQVL 143
Cdd:PRK15134   64 VvypsgdirfhgESLLHASEQTLRGVRG--------NKIAMIFQEPMVSLNPlhTLEKQLYEVLSLHRGMRREAARGEIL 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 144 TLLNL----DPDATLD----SLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRG----AIVFISH 211
Cdd:PRK15134  136 NCLDRvgirQAAKRLTdyphQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelnmGLLFITH 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 212 DREFIHKLATRIIDLDRG----------------------VITSWPGNYDEYLQGKEEA-LRVEELQHAeFDrklaqeev 268
Cdd:PRK15134  216 NLSIVRKLADRVAVMQNGrcveqnraatlfsapthpytqkLLNSEPSGDPVPLPEPASPlLDVEQLQVA-FP-------- 286
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 269 wVRQGIKARRTrnegrvraleamrmersqrrelqgkaklqmddvnrsgklvfeteglgldfGDRTLFQGLDLQVLRGDKI 348
Cdd:PRK15134  287 -IRKGILKRTV--------------------------------------------------DHNVVVKNISFTLRPGETL 315
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 349 ALVGPNGCGKST----LIKLLLGQLE-----------PSRGLVKGGTKLEVAYFDQYrDQLDPEQTVMDNVGEGKQ---- 409
Cdd:PRK15134  316 GLVGESGSGKSTtglaLLRLINSQGEiwfdgqplhnlNRRQLLPVRHRIQVVFQDPN-SSLNPRLNVLQIIEEGLRvhqp 394
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1411607396 410 EVMVRGRSRHILGYLQDFLFEPK-RARTPvKALSGGEKNRLLLAK-LFLKPSnLLILDEPTNDLD 472
Cdd:PRK15134  395 TLSAAQREQQVIAVMEEVGLDPEtRHRYP-AEFSGGQRQRIAIARaLILKPS-LIILDEPTSSLD 457
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
1-233 6.68e-12

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 66.36  E-value: 6.68e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   1 MALLTLHGACLSFS-DFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELP------LDDGRMVQQQDLKVTR--- 70
Cdd:PRK13652    1 MHLIETRDLCYSYSgSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKptsgsvLIRGEPITKENIREVRkfv 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  71 --LEQDPpassDLTVFDYTAEglagvgellkkyhhisMELAHDPSDANirimsdlqeqLDYQNgwqFETRISQVLTLLNL 148
Cdd:PRK13652   81 glVFQNP----DDQIFSPTVE----------------QDIAFGPINLG----------LDEET---VAHRVSSALHMLGL 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 149 DP--DATLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRG----AIVFISHDREFIHKLATR 222
Cdd:PRK13652  128 EElrDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPEtygmTVIFSTHQLDLVPEMADY 207
                         250
                  ....*....|.
gi 1411607396 223 IIDLDRGVITS 233
Cdd:PRK13652  208 IYVMDKGRIVA 218
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
323-472 1.01e-11

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


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 66.64  E-value: 1.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 323 EGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GG---TKLE-----VAY-FDQYrd 392
Cdd:COG3839     7 ENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILiGGrdvTDLPpkdrnIAMvFQSY-- 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 393 QLDPEQTVMDNV-------GEGKQEvmVRGRSRH---ILGyLQDFLfepkrARTPvKALSGGEKNRLLLA-------KLF 455
Cdd:COG3839    85 ALYPHMTVYENIafplklrKVPKAE--IDRRVREaaeLLG-LEDLL-----DRKP-KQLSGGQRQRVALGralvrepKVF 155
                         170
                  ....*....|....*..
gi 1411607396 456 LkpsnlliLDEPTNDLD 472
Cdd:COG3839   156 L-------LDEPLSNLD 165
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
17-233 1.03e-11

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 65.81  E-value: 1.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  17 PLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRM-----------VQQQDLKVTRLEQDPpassD----- 80
Cdd:PRK13635   21 YALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTItvggmvlseetVWDVRRQVGMVFQNP----Dnqfvg 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  81 LTVFDYTAEGLAGVGEllkkyhhismelahdPSDANIRimsdlqeqldyqngwqfetRISQVLTLLNLDPDATLD--SLS 158
Cdd:PRK13635   97 ATVQDDVAFGLENIGV---------------PREEMVE-------------------RVDQALRQVGMEDFLNREphRLS 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 159 GGWLRKVALARALACDPDLLLLDEPTNHLD----IEAINWLEDfLKDFRGAIVF-ISHDREFIHKlATRIIDLDRGVITS 233
Cdd:PRK13635  143 GGQKQRVAIAGVLALQPDIIILDEATSMLDprgrREVLETVRQ-LKEQKGITVLsITHDLDEAAQ-ADRVIVMNKGEILE 220
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
19-231 1.04e-11

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


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 66.26  E-value: 1.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  19 LDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGR-----MV---QQQDLK-----V----TRLEQDPPAssdl 81
Cdd:COG4586    38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEvrvlgYVpfkRRKEFArrigvVfgqrSQLWWDLPA---- 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  82 tvfdytAEGLagvgELLKKYHHISMElahdpsdanirimsdlqeqldyqngwQFETRISQVLTLLNLDPdaTLD----SL 157
Cdd:COG4586   114 ------IDSF----RLLKAIYRIPDA--------------------------EYKKRLDELVELLDLGE--LLDtpvrQL 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1411607396 158 SGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDF---RGAIVFI-SHDREFIHKLATRIIDLDRGVI 231
Cdd:COG4586   156 SLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYnreRGTTILLtSHDMDDIEALCDRVIVIDHGRI 233
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
1-473 1.12e-11

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 67.63  E-value: 1.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   1 MALLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGelplddgrmVQQQDLKVTRLEQDPpassd 80
Cdd:PRK11288    2 SPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSG---------NYQPDAGSILIDGQE----- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  81 lTVFDYTAEGL-AGVG----ELlkkyhHISME--------LAHDPSDANI----RIMSDLQEQLDyqngwqfetRISqvl 143
Cdd:PRK11288   68 -MRFASTTAALaAGVAiiyqEL-----HLVPEmtvaenlyLGQLPHKGGIvnrrLLNYEAREQLE---------HLG--- 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 144 tlLNLDPDATLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRG---AIVFISHDREFIHKLA 220
Cdd:PRK11288  130 --VDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAegrVILYVSHRMEEIFALC 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 221 TRIIDLDRGvitswpgnydEYLQGKEEalrVEELQHAEfdrkLAQEEVwvrqgikarrTRNEGRVRALEAmrmersqrRE 300
Cdd:PRK11288  208 DAITVFKDG----------RYVATFDD---MAQVDRDQ----LVQAMV----------GREIGDIYGYRP--------RP 252
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 301 LqGKAKLQMDDVnrsgklvfetEGLGLDfgdrtlfQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GG 379
Cdd:PRK11288  253 L-GEVRLRLDGL----------KGPGLR-------EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYlDG 314
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 380 TKLEvayFDQYRDQ------LDPEqtvmdnvgEGKQEVMVRGRS----------RHIL--GYLQDFLFEPKRA------- 434
Cdd:PRK11288  315 KPID---IRSPRDAiragimLCPE--------DRKAEGIIPVHSvadninisarRHHLraGCLINNRWEAENAdrfirsl 383
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*.
gi 1411607396 435 -------RTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDV 473
Cdd:PRK11288  384 niktpsrEQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDV 429
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
338-516 1.41e-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: 64.44  E-value: 1.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 338 LDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRG-LVKGG---TKLEVA------YFDQyrDQLDPEQTVMDNVGEG 407
Cdd:cd03298    17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGrVLINGvdvTAAPPAdrpvsmLFQE--NNLFAHLTVEQNVGLG 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 408 -----KQEVMVRGRSRHILGYLQDFLFEPKRARTpvkaLSGGEKNRLLLAKLFLKPSNLLILDEPTNDLD----VETLEL 478
Cdd:cd03298    95 lspglKLTAEDRQAIEVALARVGLAGLEKRLPGE----LSGGERQRVALARVLVRDKPVLLLDEPFAALDpalrAEMLDL 170
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1411607396 479 LEELLADYPGTLLLVSH---DRRFIDNTVtgcwLFEGDGRI 516
Cdd:cd03298   171 VLDLHAETKMTVLMVTHqpeDAKRLAQRV----VFLDNGRI 207
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
331-495 1.52e-11

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: 64.41  E-value: 1.52e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 331 DRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKGGTKLEVAYFDQY-RDQL-----DP---EQTVM 401
Cdd:cd03248    26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYlHSKVslvgqEPvlfARSLQ 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 402 DNVGEGKQ-----EVMVRGRSRHILGYLQDFlfePKRARTPV----KALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:cd03248   106 DNIAYGLQscsfeCVKEAAQKAHAHSFISEL---ASGYDTEVgekgSQLSGGQKQRVAIARALIRNPQVLILDEATSALD 182
                         170       180
                  ....*....|....*....|....*
gi 1411607396 473 VETLELLEELLADYPG--TLLLVSH 495
Cdd:cd03248   183 AESEQQVQQALYDWPErrTVLVIAH 207
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
3-212 1.71e-11

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 64.75  E-value: 1.71e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   3 LLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMVQQQDLKV----TRLEQDPpaS 78
Cdd:PRK09544    4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIgyvpQKLYLDT--T 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  79 SDLTVFDYtaeglagvgellkkyhhisMELAhdPSDANIRIMSDLQeqldyqngwqfetRIsQVLTLLnldpDATLDSLS 158
Cdd:PRK09544   82 LPLTVNRF-------------------LRLR--PGTKKEDILPALK-------------RV-QAGHLI----DAPMQKLS 122
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1411607396 159 GGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRG----AIVFISHD 212
Cdd:PRK09544  123 GGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRReldcAVLMVSHD 180
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
17-242 1.81e-11

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: 67.07  E-value: 1.81e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  17 PLLDNAELSIERGERLCLVGRNGAGKSTLMKII-------AGELPLDdGRMVQQQDLKVTR-----LEQDPpassdlTVF 84
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLvgffqarSGEILLN-GFSLKDIDRHTLRqfinyLPQEP------YIF 560
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  85 DYTA-EGLagvgeLLKKYHHISMELAhdpsDANIRIMSDLQEQLDYQNGWQfeTRISQvltllnldpDATldSLSGGWLR 163
Cdd:TIGR01193 561 SGSIlENL-----LLGAKENVSQDEI----WAACEIAEIKDDIENMPLGYQ--TELSE---------EGS--SISGGQKQ 618
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 164 KVALARALACDPDLLLLDEPTNHLD-IEAINWLEDFLKDFRGAIVFISHdREFIHKLATRIIDLDRGVITSwPGNYDEYL 242
Cdd:TIGR01193 619 RIALARALLTDSKVLILDESTSNLDtITEKKIVNNLLNLQDKTIIFVAH-RLSVAKQSDKIIVLDHGKIIE-QGSHDELL 696
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
335-475 2.23e-11

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 66.77  E-value: 2.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 335 FQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTKLE-----------------VAYF-DQYRDQL- 394
Cdd:PRK11160  356 LKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILlNGQPIAdyseaalrqaisvvsqrVHLFsATLRDNLl 435
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 395 --DPEQT------VMDNVGegkqevmvrgrsrhiLGYLQD-------FLFEPKRArtpvkaLSGGEKNRLLLAKLFLKPS 459
Cdd:PRK11160  436 laAPNASdealieVLQQVG---------------LEKLLEddkglnaWLGEGGRQ------LSGGEQRRLGIARALLHDA 494
                         170
                  ....*....|....*.
gi 1411607396 460 NLLILDEPTNDLDVET 475
Cdd:PRK11160  495 PLLLLDEPTEGLDAET 510
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
339-533 2.30e-11

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 64.01  E-value: 2.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 339 DLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRG--LVKGG--TKLEVA------YFDQyrDQLDPEQTVMDNVGEG- 407
Cdd:COG3840    19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGriLWNGQdlTALPPAerpvsmLFQE--NNLFPHLTVAQNIGLGl 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 408 ----------KQEVmvrgrsRHILGY--LQDFLfepkrARTPvKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLD--- 472
Cdd:COG3840    97 rpglkltaeqRAQV------EQALERvgLAGLL-----DRLP-GQLSGGQRQRVALARCLVRKRPILLLDEPFSALDpal 164
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1411607396 473 -VETLELLEELLADYPGTLLLVSHD----RRFIDNTvtgcwLFEGDGRISdYVGGYADMMATRAQQ 533
Cdd:COG3840   165 rQEMLDLVDELCRERGLTVLMVTHDpedaARIADRV-----LLVADGRIA-ADGPTAALLDGEPPP 224
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
323-473 2.43e-11

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 64.62  E-value: 2.43e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 323 EGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVkggtklevaYFDQYRDQLDPEQTVMD 402
Cdd:PRK10253   11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHV---------WLDGEHIQHYASKEVAR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 403 NVG--------EGK---QEVMVRGRSRHILGYL------QDFLFEPKR-------ARTPVKALSGGEKNRLLLAKLFLKP 458
Cdd:PRK10253   82 RIGllaqnattPGDitvQELVARGRYPHQPLFTrwrkedEEAVTKAMQatgithlADQSVDTLSGGQRQRAWIAMVLAQE 161
                         170
                  ....*....|....*
gi 1411607396 459 SNLLILDEPTNDLDV 473
Cdd:PRK10253  162 TAIMLLDEPTTWLDI 176
PLN03073 PLN03073
ABC transporter F family; Provisional
416-546 2.81e-11

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 66.42  E-value: 2.81e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 416 RSRHILGYLQdflFEPKRARTPVKALSGGEKNRLLLAK-LFLKPsNLLILDEPTNDLDVETLELLEELLADYPGTLLLVS 494
Cdd:PLN03073  323 RAASILAGLS---FTPEMQVKATKTFSGGWRMRIALARaLFIEP-DLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVS 398
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1411607396 495 HDRRFIDNTVTGCWLFEGDgRISDYVGGYADMMATRAQQ-STQLAAKAAQVKT 546
Cdd:PLN03073  399 HAREFLNTVVTDILHLHGQ-KLVTYKGDYDTFERTREEQlKNQQKAFESNERS 450
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
15-246 2.87e-11

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: 63.71  E-value: 2.87e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  15 DFPLLDNAELSIERGERLCLVGRNGAGKSTLMKII-------AGELPLDdGRMVQQQDLKVTR-----LEQDPpassdlT 82
Cdd:cd03249    15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLerfydptSGEILLD-GVDIRDLNLRWLRsqiglVSQEP------V 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  83 VFDYT-AEGLAgvgelLKKYHHISMELAHDPSDANIR--IMSdLQEQLDYQNGwqfeTRISQvltllnldpdatldsLSG 159
Cdd:cd03249    88 LFDGTiAENIR-----YGKPDATDEEVEEAAKKANIHdfIMS-LPDGYDTLVG----ERGSQ---------------LSG 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 160 GWLRKVALARALACDPDLLLLDEPTNHLDI--EAI--NWLEDFLKDfRGAIVfISHDREFIHKlATRIIDLDRGVITSwP 235
Cdd:cd03249   143 GQKQRIAIARALLRNPKILLLDEATSALDAesEKLvqEALDRAMKG-RTTIV-IAHRLSTIRN-ADLIAVLQNGQVVE-Q 218
                         250
                  ....*....|.
gi 1411607396 236 GNYDEYLQGKE 246
Cdd:cd03249   219 GTHDELMAQKG 229
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
1-231 2.99e-11

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 64.00  E-value: 2.99e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   1 MALLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMK------------IIAGELPLDDGRMVQQQDLKV 68
Cdd:PRK11264    1 MSAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRcinlleqpeagtIRVGDITIDTARSLSQQKGLI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  69 TRLEQDppassdltvfdytaeglagVGELLKKY----HHISMElahDPSDANIRIMSDLQEQLdyqngwqfETRISQVLT 144
Cdd:PRK11264   81 RQLRQH-------------------VGFVFQNFnlfpHRTVLE---NIIEGPVIVKGEPKEEA--------TARARELLA 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 145 LLNLD--PDATLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINwleDFLKDFRG------AIVFISHDREFI 216
Cdd:PRK11264  131 KVGLAgkETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVG---EVLNTIRQlaqekrTMVIVTHEMSFA 207
                         250
                  ....*....|....*
gi 1411607396 217 HKLATRIIDLDRGVI 231
Cdd:PRK11264  208 RDVADRAIFMDQGRI 222
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
3-231 3.33e-11

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 65.35  E-value: 3.33e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   3 LLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGR-MVQQQDlkVTRLeqdPPASSD- 80
Cdd:PRK09452   14 LVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRiMLDGQD--ITHV---PAENRHv 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  81 ------------LTVFDYTAEGLAgvgelLKKYhhismelahdPSDanirimsdlqeqldyqngwQFETRISQVLTLLNL 148
Cdd:PRK09452   89 ntvfqsyalfphMTVFENVAFGLR-----MQKT----------PAA-------------------EITPRVMEALRMVQL 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 149 DPDAT--LDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRGAI----VFISHDREFIHKLATR 222
Cdd:PRK09452  135 EEFAQrkPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLgitfVFVTHDQEEALTMSDR 214

                  ....*....
gi 1411607396 223 IIDLDRGVI 231
Cdd:PRK09452  215 IVVMRDGRI 223
cbiO PRK13643
energy-coupling factor transporter ATPase;
329-472 3.38e-11

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 64.37  E-value: 3.38e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 329 FGDRTLFQgLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKGG---------------TKLEVAYFDQYRDQ 393
Cdd:PRK13643   17 FASRALFD-IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGdivvsstskqkeikpVRKKVGVVFQFPES 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 394 LDPEQTVMDNVGEGKQEV--------MVRGRSRHILGYLQDFLfepkrARTPVKaLSGGEKNRLLLAKLFLKPSNLLILD 465
Cdd:PRK13643   96 QLFEETVLKDVAFGPQNFgipkekaeKIAAEKLEMVGLADEFW-----EKSPFE-LSGGQMRRVAIAGILAMEPEVLVLD 169

                  ....*..
gi 1411607396 466 EPTNDLD 472
Cdd:PRK13643  170 EPTAGLD 176
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
11-183 3.65e-11

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 64.02  E-value: 3.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  11 LSFS--DFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRM---------VQQQDL-----KVTRLEQD 74
Cdd:PRK11831   13 VSFTrgNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEIlfdgenipaMSRSRLytvrkRMSMLFQS 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  75 PPASSDLTVFDytaeglaGVGELLKKYHHISMELAHdpsdanirimsdlqeqldyqngwqfeTRISQVLTLLNLDPDATL 154
Cdd:PRK11831   93 GALFTDMNVFD-------NVAYPLREHTQLPAPLLH--------------------------STVMMKLEAVGLRGAAKL 139
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1411607396 155 --DSLSGGWLRKVALARALACDPDLLLLDEP 183
Cdd:PRK11831  140 mpSELSGGMARRAALARAIALEPDLIMFDEP 170
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
14-231 3.72e-11

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: 63.26  E-value: 3.72e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  14 SDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKII-------AGELPLDdGRMVQQQDLK-----VTRLEQDPPASSDl 81
Cdd:cd03248    25 PDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLenfyqpqGGQVLLD-GKPISQYEHKylhskVSLVGQEPVLFAR- 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  82 TVFDYTAEGLAG-----VGELLKKYHhismelAHDpsdaNIRIMsdlqeqldyQNGWQFET--RISQvltllnldpdatl 154
Cdd:cd03248   103 SLQDNIAYGLQScsfecVKEAAQKAH------AHS----FISEL---------ASGYDTEVgeKGSQ------------- 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1411607396 155 dsLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDF--RGAIVFISHDREFIHKlATRIIDLDRGVI 231
Cdd:cd03248   151 --LSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWpeRRTVLVIAHRLSTVER-ADQILVLDGGRI 226
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
4-189 3.77e-11

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 63.88  E-value: 3.77e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   4 LTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIA-------GELPLDDGRMVQQQDLKVTR----LE 72
Cdd:PRK11231    3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFArlltpqsGTVFLGDKPISMLSSRQLARrlalLP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  73 QDPPASSDLTVFDYTAEG----LAGVGELLKKYHHI---SMElahdpsdanirimsdlqeqldyqngwqfETRISQVltl 145
Cdd:PRK11231   83 QHHLTPEGITVRELVAYGrspwLSLWGRLSAEDNARvnqAME----------------------------QTRINHL--- 131
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1411607396 146 lnldPDATLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDI 189
Cdd:PRK11231  132 ----ADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDI 171
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
297-475 3.80e-11

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 66.14  E-value: 3.80e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 297 QRRELQGKAKLQmddvNRSGKLVFETEGLGLDfGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLV 376
Cdd:PRK13657  318 DVRDPPGAIDLG----RVKGAVEFDDVSFSYD-NSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRI 392
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 377 K-GGTKLEVAYFDQYRDQL-----DP---EQTVMDNVGEGK----QEVMVRGRSRhilGYLQDFLF-EPKRARTPV---- 438
Cdd:PRK13657  393 LiDGTDIRTVTRASLRRNIavvfqDAglfNRSIEDNIRVGRpdatDEEMRAAAER---AQAHDFIErKPDGYDTVVgerg 469
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1411607396 439 KALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVET 475
Cdd:PRK13657  470 RQLSGGERQRLAIARALLKDPPILILDEATSALDVET 506
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
141-233 3.83e-11

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 64.90  E-value: 3.83e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 141 QVLTLLNLDPdaTLD----SLSGGWLRKVALARALACDPDLLLLDEPTNHLDI----EAINWLEDFLKDFRGAIVFISHD 212
Cdd:PRK11144  111 KIVALLGIEP--LLDrypgSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLprkrELLPYLERLAREINIPILYVSHS 188
                          90       100
                  ....*....|....*....|.
gi 1411607396 213 REFIHKLATRIIDLDRGVITS 233
Cdd:PRK11144  189 LDEILRLADRVVVLEQGKVKA 209
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
321-474 3.84e-11

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 63.62  E-value: 3.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKGGT---------KLEVAYFDQYR 391
Cdd:PRK11264    5 EVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDitidtarslSQQKGLIRQLR 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 392 DQ---------LDPEQTVMDNVGEG--------KQEVMVRGRSrhilgYLQDFLFEPKRARTPvKALSGGEKNRLLLAKL 454
Cdd:PRK11264   85 QHvgfvfqnfnLFPHRTVLENIIEGpvivkgepKEEATARARE-----LLAKVGLAGKETSYP-RRLSGGQQQRVAIARA 158
                         170       180
                  ....*....|....*....|
gi 1411607396 455 FLKPSNLLILDEPTNDLDVE 474
Cdd:PRK11264  159 LAMRPEVILFDEPTSALDPE 178
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
333-498 3.90e-11

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 63.26  E-value: 3.90e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 333 TLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGlvkggtklEVAYFDQYRDQLDPEQTVM---DNVGEGKQ 409
Cdd:PRK10584   24 SILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSG--------EVSLVGQPLHQMDEEARAKlraKHVGFVFQ 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 410 EVMV----------------RG----RSRHILGYLQDFLFEPKRARTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTN 469
Cdd:PRK10584   96 SFMLiptlnalenvelpallRGessrQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTG 175
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1411607396 470 DLDVETLELLE----ELLADYPGTLLLVSHDRR 498
Cdd:PRK10584  176 NLDRQTGDKIAdllfSLNREHGTTLILVTHDLQ 208
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
4-188 3.95e-11

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 65.13  E-value: 3.95e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   4 LTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAG-ELPLD-----DG-----RMVQQQDLKVtrle 72
Cdd:PRK11432    7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGlEKPTEgqifiDGedvthRSIQQRDICM---- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  73 qdppassdltVFDYTAeglagvgellkKYHHISmelahdpsdanirimsdLQEQLDY------QNGWQFETRISQVLTLL 146
Cdd:PRK11432   83 ----------VFQSYA-----------LFPHMS-----------------LGENVGYglkmlgVPKEERKQRVKEALELV 124
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1411607396 147 NLD--PDATLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLD 188
Cdd:PRK11432  125 DLAgfEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLD 168
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
313-475 5.22e-11

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: 65.92  E-value: 5.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 313 NRSGKLVFETEGLGLDFGDRTLfQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTKLEVAYFDQYR 391
Cdd:TIGR01193 469 NLNGDIVINDVSYSYGYGSNIL-SDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILlNGFSLKDIDRHTLR 547
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 392 DQLD--PEQ------TVMDNV------GEGKQEVMVRGRSRHI--------LGYLQDFLFEPKrartpvkALSGGEKNRL 449
Cdd:TIGR01193 548 QFINylPQEpyifsgSILENLllgakeNVSQDEIWAACEIAEIkddienmpLGYQTELSEEGS-------SISGGQKQRI 620
                         170       180
                  ....*....|....*....|....*.
gi 1411607396 450 LLAKLFLKPSNLLILDEPTNDLDVET 475
Cdd:TIGR01193 621 ALARALLTDSKVLILDESTSNLDTIT 646
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
321-472 5.57e-11

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: 63.13  E-value: 5.57e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLV----KGGTKLEVA------YFDQY 390
Cdd:cd03296     4 EVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTIlfggEDATDVPVQernvgfVFQHY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 391 rdQLDPEQTVMDNVGEG---------KQEVMVRGRSRHILGYLQ-DFLFEpkraRTPVKaLSGGEKNRLLLAKLFLKPSN 460
Cdd:cd03296    84 --ALFRHMTVFDNVAFGlrvkprserPPEAEIRAKVHELLKLVQlDWLAD----RYPAQ-LSGGQRQRVALARALAVEPK 156
                         170
                  ....*....|..
gi 1411607396 461 LLILDEPTNDLD 472
Cdd:cd03296   157 VLLLDEPFGALD 168
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
331-495 5.58e-11

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 65.51  E-value: 5.58e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 331 DRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRG--LVKGG--TKLEVAYFDQYRDQLDPE-----QTVM 401
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGqvLLDGVplVQYDHHYLHRQVALVGQEpvlfsGSVR 572
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 402 DNVGEG-----KQEVMVRGRSRHILGYLQDFlfePKRARTPV----KALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:TIGR00958 573 ENIAYGltdtpDEEIMAAAKAANAHDFIMEF---PNGYDTEVgekgSQLSGGQKQRIAIARALVRKPRVLILDEATSALD 649
                         170       180
                  ....*....|....*....|...
gi 1411607396 473 VETLELLEELLADYPGTLLLVSH 495
Cdd:TIGR00958 650 AECEQLLQESRSRASRTVLLIAH 672
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
15-231 7.06e-11

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 65.04  E-value: 7.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  15 DFPLLDNAELSIERGERLCLVGRNGAGKSTLMKII-------AGELPLDdGRMVQQQDLKVTRlEQDPPASSDLTVF-DY 86
Cdd:PRK11176  355 EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLtrfydidEGEILLD-GHDLRDYTLASLR-NQVALVSQNVHLFnDT 432
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  87 TAEGLAGVGEllKKYHHISMELAhdpsdANIRIMSDLQEQLDyqNGwqFETRISQVLTllnldpdatldSLSGGWLRKVA 166
Cdd:PRK11176  433 IANNIAYART--EQYSREQIEEA-----ARMAYAMDFINKMD--NG--LDTVIGENGV-----------LLSGGQRQRIA 490
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1411607396 167 LARALACDPDLLLLDEPTNHLDIE---AINWLEDFLKDFRGAIVfISHDREFIHKlATRIIDLDRGVI 231
Cdd:PRK11176  491 IARALLRDSPILILDEATSALDTEserAIQAALDELQKNRTSLV-IAHRLSTIEK-ADEILVVEDGEI 556
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
323-475 9.00e-11

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 63.96  E-value: 9.00e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 323 EGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTKLevayfdqyrDQLDPEQ--- 398
Cdd:COG3842     9 ENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILlDGRDV---------TGLPPEKrnv 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 399 -------------TVMDNVGEG-------KQEvmVRGRSRHILGY--LQDFlfepkrARTPVKALSGGEKNRLLLAK-LF 455
Cdd:COG3842    80 gmvfqdyalfphlTVAENVAFGlrmrgvpKAE--IRARVAELLELvgLEGL------ADRYPHQLSGGQQQRVALARaLA 151
                         170       180
                  ....*....|....*....|
gi 1411607396 456 LKPSnLLILDEPTNDLDVET 475
Cdd:COG3842   152 PEPR-VLLLDEPLSALDAKL 170
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
309-473 9.83e-11

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 62.88  E-value: 9.83e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 309 MDDVNRSGKLVFETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRG-LVKGGTKL----- 382
Cdd:PRK10575    1 MQEYTNHSDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGeILLDAQPLeswss 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 383 -----EVAYFDQyrdQLDPEQtvmdnvGEGKQEVMVRGR-SRHilGYLQDFLFEPKR--------------ARTPVKALS 442
Cdd:PRK10575   81 kafarKVAYLPQ---QLPAAE------GMTVRELVAIGRyPWH--GALGRFGAADREkveeaislvglkplAHRLVDSLS 149
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1411607396 443 GGEKNRLLLAKLFLKPSNLLILDEPTNDLDV 473
Cdd:PRK10575  150 GGERQRAWIAMLVAQDSRCLLLDEPTSALDI 180
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
19-231 1.10e-10

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 63.67  E-value: 1.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  19 LDNAELSIERGERLCLVGRNGAGKSTLMKIIAG-ELPlDDGR-MVQQQDLkvTRLEQDPPAS---------------SDL 81
Cdd:PRK11153   21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLlERP-TSGRvLVDGQDL--TALSEKELRKarrqigmifqhfnllSSR 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  82 TVFDYTAeglagvgellkkyhhISMELAHDPSDanirimsdlqeqldyqngwQFETRISQVLTLLNLDP--DATLDSLSG 159
Cdd:PRK11153   98 TVFDNVA---------------LPLELAGTPKA-------------------EIKARVTELLELVGLSDkaDRYPAQLSG 143
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1411607396 160 GWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKD----FRGAIVFISHDREFIHKLATRIIDLDRGVI 231
Cdd:PRK11153  144 GQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDinreLGLTIVLITHEMDVVKRICDRVAVIDAGRL 219
ABC_tran_CTD pfam16326
ABC transporter C-terminal domain; This domain is found at the C-terminus of ABC transporters. ...
562-631 1.13e-10

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: 57.48  E-value: 1.13e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 562 KLSYKLQLELDNLPARLEQLETELNALQAEVNHPGFFALPSDQTQLkLDALNAAEAALEQAFSRWEELEA 631
Cdd:pfam16326   1 KLSYKEQRELEELEAEIEKLEEEIAELEAQLADPELYSDYEKLQEL-SAELEELEAELEELYERWEELEE 69
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
317-472 1.43e-10

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 62.17  E-value: 1.43e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 317 KLVFETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLL--LGQLEPSrGLVKGGTKL------------ 382
Cdd:PRK14267    2 KFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrLLELNEE-ARVEGEVRLfgrniyspdvdp 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 383 -----EVAYFDQYRDQLdPEQTVMDNVGEG-KQEVMVRGRS----RHILGYLQDFLFEPKRARTPVKA--LSGGEKNRLL 450
Cdd:PRK14267   81 ievrrEVGMVFQYPNPF-PHLTIYDNVAIGvKLNGLVKSKKeldeRVEWALKKAALWDEVKDRLNDYPsnLSGGQRQRLV 159
                         170       180
                  ....*....|....*....|...
gi 1411607396 451 LAK-LFLKPsNLLILDEPTNDLD 472
Cdd:PRK14267  160 IARaLAMKP-KILLMDEPTANID 181
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
17-191 1.51e-10

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 63.87  E-value: 1.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  17 PLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMVQQQDLKVTRLEQDPPASSdltvFDYTAEGLAGVGE 96
Cdd:PRK10762  266 PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLANG----IVYISEDRKRDGL 341
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  97 LLkkyhhiSMELAHDPSDANIRIMSDLQEQLDYQNGWQfetRISQVLTLLNL---DPDATLDSLSGGWLRKVALARALAC 173
Cdd:PRK10762  342 VL------GMSVKENMSLTALRYFSRAGGSLKHADEQQ---AVSDFIRLFNIktpSMEQAIGLLSGGNQQKVAIARGLMT 412
                         170
                  ....*....|....*...
gi 1411607396 174 DPDLLLLDEPTNHLDIEA 191
Cdd:PRK10762  413 RPKVLILDEPTRGVDVGA 430
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
321-473 1.53e-10

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: 61.48  E-value: 1.53e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKGGTKlEVAYFDQYRDQ------- 393
Cdd:cd03300     2 ELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGK-DITNLPPHKRPvntvfqn 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 394 --LDPEQTVMDNVG-----EGKQEVMVRGRSRHILGYLQdflFEPKRARTPvKALSGGEKNRLLLAK-LFLKPSnLLILD 465
Cdd:cd03300    81 yaLFPHLTVFENIAfglrlKKLPKAEIKERVAEALDLVQ---LEGYANRKP-SQLSGGQQQRVAIARaLVNEPK-VLLLD 155

                  ....*...
gi 1411607396 466 EPTNDLDV 473
Cdd:cd03300   156 EPLGALDL 163
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
337-473 1.88e-10

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


Pssm-ID: 443658 [Multi-domain]  Cd Length: 329  Bit Score: 62.83  E-value: 1.88e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 337 GLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRG--LVKGG--TKLEVAYFDQYRDQ-----------LDPEQTVM 401
Cdd:COG4608    36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGeiLFDGQdiTGLSGRELRPLRRRmqmvfqdpyasLNPRMTVG 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 402 DNVGEG--------KQEvmVRGRSRHIL---GYLQDFLfepkrARTPvKALSGGEKNRLLLAK-LFLKPSnLLILDEPTN 469
Cdd:COG4608   116 DIIAEPlrihglasKAE--RRERVAELLelvGLRPEHA-----DRYP-HEFSGGQRQRIGIARaLALNPK-LIVCDEPVS 186

                  ....
gi 1411607396 470 DLDV 473
Cdd:COG4608   187 ALDV 190
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
19-212 1.99e-10

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 62.67  E-value: 1.99e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  19 LDNAELSIERGERLCLVGRNGAGKSTLMKII-------AGELPLD-------DGRMVQQQDLKVTRLEQDPPASsdltvf 84
Cdd:PRK11308   31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLtmietptGGELYYQgqdllkaDPEAQKLLRQKIQIVFQNPYGS------ 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  85 dytaeglagvgelLKKYHHISMELAhDPsdanIRIMSDLQEQldyqngwQFETRISQVLTLLNLDP---DATLDSLSGGW 161
Cdd:PRK11308  105 -------------LNPRKKVGQILE-EP----LLINTSLSAA-------ERREKALAMMAKVGLRPehyDRYPHMFSGGQ 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1411607396 162 LRKVALARALACDPDLLLLDEPTNHLD--IEA--INWLEDFLKDFRGAIVFISHD 212
Cdd:PRK11308  160 RQRIAIARALMLDPDVVVADEPVSALDvsVQAqvLNLMMDLQQELGLSYVFISHD 214
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
284-475 2.02e-10

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 63.67  E-value: 2.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 284 RVRAL-EAMRMERSQRRELQGKaklqmdDVNRSGKLVFEteGLGLDFGD-RTLFQGLDLQVLRGDKIALVGPNGCGKSTL 361
Cdd:COG4178   334 RLAGFeEALEAADALPEAASRI------ETSEDGALALE--DLTLRTPDgRPLLEDLSLSLKPGERLLITGPSGSGKSTL 405
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 362 IKLLLG------------QLE-----PSRGLVKGGTKLEVAYFDQYRDQLDPEQ--TVMDNVGegkqevmvrgrsrhiLG 422
Cdd:COG4178   406 LRAIAGlwpygsgriarpAGArvlflPQRPYLPLGTLREALLYPATAEAFSDAElrEALEAVG---------------LG 470
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1411607396 423 YLQDFLFEPKR-ARTpvkaLSGGEKNRLLLAKLFL-KPSnLLILDEPTNDLDVET 475
Cdd:COG4178   471 HLAERLDEEADwDQV----LSLGEQQRLAFARLLLhKPD-WLFLDEATSALDEEN 520
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
17-245 2.03e-10

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


Pssm-ID: 213221 [Multi-domain]  Cd Length: 229  Bit Score: 61.09  E-value: 2.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  17 PLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLD------DGRMVQQQDLKVTR-----LEQDPPASSDlTVFD 85
Cdd:cd03254    17 PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQkgqiliDGIDIRDISRKSLRsmigvVLQDTFLFSG-TIME 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  86 ytaeglagvgellkkyhhismelahdpsdaNIRIMSDLQEqldyqngwqfETRISQVLTLLNLDP---------DATL-- 154
Cdd:cd03254    96 ------------------------------NIRLGRPNAT----------DEEVIEAAKEAGAHDfimklpngyDTVLge 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 155 --DSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAinwlEDFLKDfrgAIVFISHDREFI---HKLAT-----RII 224
Cdd:cd03254   136 ngGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTET----EKLIQE---ALEKLMKGRTSIiiaHRLSTiknadKIL 208
                         250       260
                  ....*....|....*....|.
gi 1411607396 225 DLDRGVITSwPGNYDEYLQGK 245
Cdd:cd03254   209 VLDDGKIIE-EGTHDELLAKK 228
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
3-243 2.06e-10

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 61.64  E-value: 2.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   3 LLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRmVQQQDLKVtrleqDPPASSDLT 82
Cdd:PRK11248    1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGS-ITLDGKPV-----EGPGAERGV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  83 VFDYtaEGLAGVGELLKKYHhISMELAHDPSDANIRIMSDLQEQLDYQNgwqFETR-ISQvltllnldpdatldsLSGGW 161
Cdd:PRK11248   75 VFQN--EGLLPWRNVQDNVA-FGLQLAGVEKMQRLEIAHQMLKKVGLEG---AEKRyIWQ---------------LSGGQ 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 162 LRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFL----KDFRGAIVFISHDREFIHKLATRIIDLDRGvitswPGN 237
Cdd:PRK11248  134 RQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLlklwQETGKQVLLITHDIEEAVFMATELVLLSPG-----PGR 208

                  ....*.
gi 1411607396 238 YDEYLQ 243
Cdd:PRK11248  209 VVERLP 214
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
321-501 2.10e-10

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


Pssm-ID: 213184 [Multi-domain]  Cd Length: 200  Bit Score: 60.62  E-value: 2.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQlePSRGLVKGgtklEVAYFDQYRDQLDPEQTV 400
Cdd:cd03217     2 EIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH--PKYEVTEG----EILFKGEDITDLPPEERA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 401 MDNVGEGKQE-VMVRGRSrhilgyLQDFLfepkraRTPVKALSGGEKNRL-LLAKLFLKPSnLLILDEPTNDLDVETLEL 478
Cdd:cd03217    76 RLGIFLAFQYpPEIPGVK------NADFL------RYVNEGFSGGEKKRNeILQLLLLEPD-LAILDEPDSGLDIDALRL 142
                         170       180
                  ....*....|....*....|....*.
gi 1411607396 479 LEELLADY--PGT-LLLVSHDRRFID 501
Cdd:cd03217   143 VAEVINKLreEGKsVLIITHYQRLLD 168
cbiO PRK13646
energy-coupling factor transporter ATPase;
19-233 2.20e-10

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 62.10  E-value: 2.20e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  19 LDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRmVQQQDLKVTRLEQD----PPASSDLTVFDYTAEGLAgv 94
Cdd:PRK13646   23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGT-VTVDDITITHKTKDkyirPVRKRIGMVFQFPESQLF-- 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  95 gellkkYHHISMELAHDPSDANIrimsDLQEQLDYQNGWQFETRISQvlTLLNLDPDatldSLSGGWLRKVALARALACD 174
Cdd:PRK13646  100 ------EDTVEREIIFGPKNFKM----NLDEVKNYAHRLLMDLGFSR--DVMSQSPF----QMSGGQMRKIAIVSILAMN 163
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1411607396 175 PDLLLLDEPTNHLDIEAINWLEDFLKDFR----GAIVFISHDREFIHKLATRIIDLDRGVITS 233
Cdd:PRK13646  164 PDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdenKTIILVSHDMNEVARYADEVIVMKEGSIVS 226
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
2-473 2.22e-10

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 63.48  E-value: 2.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   2 ALLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMVQQQdlKVTRLeQDPPASSDl 81
Cdd:PRK10762    3 ALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLG--KEVTF-NGPKSSQE- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  82 tvfdytaeglAGVGELlkkyhHISMELAHDPSDA-NIRImsdlqeqldyqnGWQFETRI------------SQVLTLLNL 148
Cdd:PRK10762   79 ----------AGIGII-----HQELNLIPQLTIAeNIFL------------GREFVNRFgridwkkmyaeaDKLLARLNL 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 149 --DPDATLDSLSGGWLRKVALARALACDPDLLLLDEPTNHL-DIE------AINwlEdfLKDFRGAIVFISH-------- 211
Cdd:PRK10762  132 rfSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTEteslfrVIR--E--LKSQGRGIVYISHrlkeifei 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 212 --------DREFIHKLATRIIDLDRGVitswpgnydEYLQGkeealrveelqhaefdRKLaqEEVWVRQGIKarrtrneg 283
Cdd:PRK10762  208 cddvtvfrDGQFIAEREVADLTEDSLI---------EMMVG----------------RKL--EDQYPRLDKA-------- 252
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 284 rvraleamrmersqrrelQGKAKLQmddvnrsgklVFETEGLGLDFGDRTLFQGLDLQVlrgdkialVGPNGCGKSTLIK 363
Cdd:PRK10762  253 ------------------PGEVRLK----------VDNLSGPGVNDVSFTLRKGEILGV--------SGLMGAGRTELMK 296
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 364 LLLGQLEPSRGLVK------------GGTKLEVAYF--DQYRDQLDPEQTVMDNVG--------------EGKQEVMVRG 415
Cdd:PRK10762  297 VLYGALPRTSGYVTldghevvtrspqDGLANGIVYIseDRKRDGLVLGMSVKENMSltalryfsraggslKHADEQQAVS 376
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1411607396 416 rsrhilgylqDF--LFEPKrarTP-----VKALSGGEKNRLLLAK-LFLKPsNLLILDEPTNDLDV 473
Cdd:PRK10762  377 ----------DFirLFNIK---TPsmeqaIGLLSGGNQQKVAIARgLMTRP-KVLILDEPTRGVDV 428
cbiO PRK13637
energy-coupling factor transporter ATPase;
345-495 2.24e-10

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 61.99  E-value: 2.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 345 GDKIALVGPNGCGKSTLIKLLLGQLEPSRG--------LVKGGTKL-----EVAYFDQYRD-QLDPEQTVMD------NV 404
Cdd:PRK13637   33 GEFVGLIGHTGSGKSTLIQHLNGLLKPTSGkiiidgvdITDKKVKLsdirkKVGLVFQYPEyQLFEETIEKDiafgpiNL 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 405 GEGKQEVMVR-GRSRHILGylqdFLFEPKRARTPVKaLSGGEKNRLLLAKLF-LKPSnLLILDEPTNDLDV----ETLEL 478
Cdd:PRK13637  113 GLSEEEIENRvKRAMNIVG----LDYEDYKDKSPFE-LSGGQKRRVAIAGVVaMEPK-ILILDEPTAGLDPkgrdEILNK 186
                         170
                  ....*....|....*..
gi 1411607396 479 LEELLADYPGTLLLVSH 495
Cdd:PRK13637  187 IKELHKEYNMTIILVSH 203
cbiO PRK13640
energy-coupling factor transporter ATPase;
14-231 2.27e-10

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 61.74  E-value: 2.27e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  14 SDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDD---------GRMVQQQDL-----KVTRLEQDPPAS- 78
Cdd:PRK13640   18 SKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnskitvdGITLTAKTVwdireKVGIVFQNPDNQf 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  79 SDLTVFDYTAEGLAGVGEllkkyhhismelahdPSDANIRIMSDLQEQ---LDYQngwqfetrisqvltllnldpDATLD 155
Cdd:PRK13640   98 VGATVGDDVAFGLENRAV---------------PRPEMIKIVRDVLADvgmLDYI--------------------DSEPA 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 156 SLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRG----AIVFISHDREFIhKLATRIIDLDRGVI 231
Cdd:PRK13640  143 NLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknnlTVISITHDIDEA-NMADQVLVLDDGKL 221
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
334-495 2.33e-10

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 61.14  E-value: 2.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 334 LFQGL----DLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRG--LVKGGT-------KLEVAYFDQyRDQLDPEQTV 400
Cdd:PRK10771   10 LYHHLpmrfDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGslTLNGQDhtttppsRRPVSMLFQ-ENNLFSHLTV 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 401 MDNVGEG-----KQEVMVRGRSRHILGY--LQDFLfepkrARTPvKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLD- 472
Cdd:PRK10771   89 AQNIGLGlnpglKLNAAQREKLHAIARQmgIEDLL-----ARLP-GQLSGGQRQRVALARCLVREQPILLLDEPFSALDp 162
                         170       180
                  ....*....|....*....|....*.
gi 1411607396 473 ---VETLELLEELLADYPGTLLLVSH 495
Cdd:PRK10771  163 alrQEMLTLVSQVCQERQLTLLMVSH 188
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
17-232 2.39e-10

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 63.12  E-value: 2.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  17 PLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRM-VQQQDlkVTRLeqDPPASSDLTVF----DYTAEGL 91
Cdd:COG3845   272 PALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIrLDGED--ITGL--SPRERRRLGVAyipeDRLGRGL 347
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  92 AG---VGE--LLKKYHH--------ISMELAHDPSDANIRimsdlqeqldyqngwQFETRISqvltllnlDPDATLDSLS 158
Cdd:COG3845   348 VPdmsVAEnlILGRYRRppfsrggfLDRKAIRAFAEELIE---------------EFDVRTP--------GPDTPARSLS 404
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1411607396 159 GGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFR---GAIVFISHDREFIHKLATRIIDLDRGVIT 232
Cdd:COG3845   405 GGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRdagAAVLLISEDLDEILALSDRIAVMYEGRIV 481
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
306-472 2.56e-10

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 62.66  E-value: 2.56e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 306 KLQMDDVNRSGKLVFETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGlvkggtklEVA 385
Cdd:PRK09452    1 SKKLNKQPSSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSG--------RIM 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 386 YFDQYRDQLDPEQ----------------TVMDNVGEG-------KQEV---------MVRgrsrhilgyLQDFlfepkr 433
Cdd:PRK09452   73 LDGQDITHVPAENrhvntvfqsyalfphmTVFENVAFGlrmqktpAAEItprvmealrMVQ---------LEEF------ 137
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1411607396 434 ARTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:PRK09452  138 AQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALD 176
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
323-473 2.76e-10

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 61.10  E-value: 2.76e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 323 EGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLV----KGGTKLEVA------------- 385
Cdd:PRK11701   10 RGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVhyrmRDGQLRDLYalseaerrrllrt 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 386 ---YFDQY-RDQLDPEQTVMDNVGEGKQEVMVR--GRSRHILG-YLQDFLFEPKRARTPVKALSGGEKNRLLLAKLFLKP 458
Cdd:PRK11701   90 ewgFVHQHpRDGLRMQVSAGGNIGERLMAVGARhyGDIRATAGdWLERVEIDAARIDDLPTTFSGGMQQRLQIARNLVTH 169
                         170
                  ....*....|....*
gi 1411607396 459 SNLLILDEPTNDLDV 473
Cdd:PRK11701  170 PRLVFMDEPTGGLDV 184
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
334-475 2.80e-10

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: 60.18  E-value: 2.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 334 LFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKGGTKleVAYFDQYrdqldP---EQTVMDNVGEGKQe 410
Cdd:cd03250    20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS--IAYVSQE-----PwiqNGTIRENILFGKP- 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 411 vmvrgrsrhilgylqdflFEPKRARTPVKA------------------------LSGGEKNRLLLAKLFLKPSNLLILDE 466
Cdd:cd03250    92 ------------------FDEERYEKVIKAcalepdleilpdgdlteigekginLSGGQKQRISLARAVYSDADIYLLDD 153

                  ....*....
gi 1411607396 467 PTNDLDVET 475
Cdd:cd03250   154 PLSAVDAHV 162
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
317-472 3.10e-10

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 60.50  E-value: 3.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 317 KLVFETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRG-LVKGGTKLEVAYFDQYRDQLD 395
Cdd:PRK10247    5 SPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGtLLFEGEDISTLKPEIYRQQVS 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 396 -----PE---QTVMDNVGEGKQEVMVRGRSRHILGYLQDFLFEPKRARTPVKALSGGEKNRL-LLAKLFLKPSNLLiLDE 466
Cdd:PRK10247   85 ycaqtPTlfgDTVYDNLIFPWQIRNQQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRIsLIRNLQFMPKVLL-LDE 163

                  ....*.
gi 1411607396 467 PTNDLD 472
Cdd:PRK10247  164 ITSALD 169
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
13-231 3.16e-10

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 61.14  E-value: 3.16e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  13 FSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAG-ELPLDDGRMVQQQDLKVTRlEQDppasSDLTVFDYTAEGL 91
Cdd:PRK10619   15 YGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFlEKPSEGSIVVNGQTINLVR-DKD----GQLKVADKNQLRL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  92 AGVgELLKKYHHIS----MELAHDPSDANIRIMSdLQEQldyqngwQFETRISQVLTLLNLDPDATLD---SLSGGWLRK 164
Cdd:PRK10619   90 LRT-RLTMVFQHFNlwshMTVLENVMEAPIQVLG-LSKQ-------EARERAVKYLAKVGIDERAQGKypvHLSGGQQQR 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 165 VALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFR---GAIVFISHDREFIHKLATRIIDLDRGVI 231
Cdd:PRK10619  161 VSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAeegKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
336-496 3.51e-10

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: 60.56  E-value: 3.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 336 QGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK---------GGTKLEVayFDQYrdQLDPEQTVMDNVGE 406
Cdd:TIGR01184   2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVIlegkqitepGPDRMVV--FQNY--SLLPWLTVRENIAL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 407 GKQEV---MVRGRSRHILGYLQDFLFEPKRARTPVKALSGGEKNRLLLAK-LFLKPSnLLILDEPTNDLDVETLELLEEL 482
Cdd:TIGR01184  78 AVDRVlpdLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARaLSIRPK-VLLLDEPFGALDALTRGNLQEE 156
                         170
                  ....*....|....*...
gi 1411607396 483 L----ADYPGTLLLVSHD 496
Cdd:TIGR01184 157 LmqiwEEHRVTVLMVTHD 174
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
19-231 3.73e-10

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 61.29  E-value: 3.73e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  19 LDNAELSIERGERLCLVGRNGAGKSTLMKIIAG-ELPLDD-----GRMVQQQDLKVTRLE-----QDPpassDLTVFDYT 87
Cdd:PRK13647   21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGiYLPQRGrvkvmGREVNAENEKWVRSKvglvfQDP----DDQVFSST 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  88 AEGLAGVGEllkkyhhISMELAHDpsdaniRIMSDLQEQLDYQNGWQFETRISQvltllnldpdatldSLSGGWLRKVAL 167
Cdd:PRK13647   97 VWDDVAFGP-------VNMGLDKD------EVERRVEEALKAVRMWDFRDKPPY--------------HLSYGQKKRVAI 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1411607396 168 ARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDF--RGAIVFIS-HDREFIHKLATRIIDLDRGVI 231
Cdd:PRK13647  150 AGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLhnQGKTVIVAtHDVDLAAEWADQVIVLKEGRV 216
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
330-528 4.10e-10

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: 63.04  E-value: 4.10e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  330 GDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKggTKLEVAYFdqyrdqldPEQ------TVMDN 403
Cdd:TIGR00957  649 DLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVH--MKGSVAYV--------PQQawiqndSLREN 718
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  404 VGEGKQevMVRGRSRHIL---GYLQDFLFEPKRARTPVKA----LSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVETL 476
Cdd:TIGR00957  719 ILFGKA--LNEKYYQQVLeacALLPDLEILPSGDRTEIGEkgvnLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVG 796
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1411607396  477 ELLEELLADYPGTL-----LLVSHDRRFIDNtvTGCWLFEGDGRISDyVGGYADMMA 528
Cdd:TIGR00957  797 KHIFEHVIGPEGVLknktrILVTHGISYLPQ--VDVIIVMSGGKISE-MGSYQELLQ 850
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
336-496 4.22e-10

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


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 61.64  E-value: 4.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 336 QGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GG---TKLEVAY-------FDQyRDQL--D------- 395
Cdd:COG4586    39 DDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRvLGyvpFKRRKEFarrigvvFGQ-RSQLwwDlpaidsf 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 396 ---------PEQTVMDNVGEgkqevMVrgrsrHILGyLQDFLfepkraRTPVKALSGGEKNRL-LLAKLFLKPSnLLILD 465
Cdd:COG4586   118 rllkaiyriPDAEYKKRLDE-----LV-----ELLD-LGELL------DTPVRQLSLGQRMRCeLAAALLHRPK-ILFLD 179
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1411607396 466 EPTNDLDVETLEL----LEELLADYPGTLLLVSHD 496
Cdd:COG4586   180 EPTIGLDVVSKEAirefLKEYNRERGTTILLTSHD 214
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
2-229 4.72e-10

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 61.36  E-value: 4.72e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   2 ALLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGelplddgrMVQqqdlkvtrleqdpPASSDL 81
Cdd:PRK13537    6 APIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLG--------LTH-------------PDAGSI 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  82 TVFDYTAEGLAgvgellkkyHHISMELAHDPS----DANIRIMSDLQEQLDY--QNGWQFETRISQVLTLLNLD--PDAT 153
Cdd:PRK13537   65 SLCGEPVPSRA---------RHARQRVGVVPQfdnlDPDFTVRENLLVFGRYfgLSAAAARALVPPLLEFAKLEnkADAK 135
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1411607396 154 LDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDF--RG-AIVFISHDREFIHKLATRIIDLDRG 229
Cdd:PRK13537  136 VGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLlaRGkTILLTTHFMEEAERLCDRLCVIEEG 214
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
21-242 4.91e-10

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


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 61.97  E-value: 4.91e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  21 NAELSIERGERLCLVGRNGAGKSTLMKII-------AGELPLD--------DGRMVQQQDLKVTRLEQDPPASSDLTVFD 85
Cdd:PRK10070   46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLnrlieptRGQVLIDgvdiakisDAELREVRRKKIAMVFQSFALMPHMTVLD 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  86 YTAEGlagvgellkkyhhisMELAHDPSDANIRIMSDLQEQL---DYQNGWQfetrisqvltllnldpdatlDSLSGGWL 162
Cdd:PRK10070  126 NTAFG---------------MELAGINAEERREKALDALRQVgleNYAHSYP--------------------DELSGGMR 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 163 RKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRG----AIVFISHDREFIHKLATRIIDLDRGVITSwPGNY 238
Cdd:PRK10070  171 QRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAkhqrTIVFISHDLDEAMRIGDRIAIMQNGEVVQ-VGTP 249

                  ....
gi 1411607396 239 DEYL 242
Cdd:PRK10070  250 DEIL 253
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
319-472 5.25e-10

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 60.86  E-value: 5.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 319 VFETEGLGLDFGDRTL-FQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRG--LVKGGtklEVAY--------- 386
Cdd:PRK13639    1 ILETRDLKYSYPDGTEaLKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGevLIKGE---PIKYdkksllevr 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 387 ------FDQYRDQLDPEQTVMD------NVGEGKQEvmVRGRSRHILGYLQDFLFEPKrartPVKALSGGEKNRLLLAKL 454
Cdd:PRK13639   78 ktvgivFQNPDDQLFAPTVEEDvafgplNLGLSKEE--VEKRVKEALKAVGMEGFENK----PPHHLSGGQKKRVAIAGI 151
                         170
                  ....*....|....*...
gi 1411607396 455 FLKPSNLLILDEPTNDLD 472
Cdd:PRK13639  152 LAMKPEIIVLDEPTSGLD 169
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
316-475 5.61e-10

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: 62.14  E-value: 5.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 316 GKLVFEteglGLDFG---DRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTKL-EVAYfDQY 390
Cdd:COG5265   356 GEVRFE----NVSFGydpERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILiDGQDIrDVTQ-ASL 430
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 391 RDQLD--PEQTVM------DNVGEGK-----QEVMVRGRSRHILGYLQDFlfePKRARTPV-----KaLSGGEKNRLLLA 452
Cdd:COG5265   431 RAAIGivPQDTVLfndtiaYNIAYGRpdaseEEVEAAARAAQIHDFIESL---PDGYDTRVgerglK-LSGGEKQRVAIA 506
                         170       180
                  ....*....|....*....|...
gi 1411607396 453 KLFLKPSNLLILDEPTNDLDVET 475
Cdd:COG5265   507 RTLLKNPPILIFDEATSALDSRT 529
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
330-472 6.13e-10

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 60.59  E-value: 6.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 330 GDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRG--LVKGG--TKLEVA--------YFDQYRDQLDPE 397
Cdd:PRK13652   15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGsvLIRGEpiTKENIRevrkfvglVFQNPDDQIFSP 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 398 QTVMD------NVGEGKQEVMVRGRSR-HILGylqdflFEPKRARTPvKALSGGEKNRLLLAKLFLKPSNLLILDEPTND 470
Cdd:PRK13652   95 TVEQDiafgpiNLGLDEETVAHRVSSAlHMLG------LEELRDRVP-HHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAG 167

                  ..
gi 1411607396 471 LD 472
Cdd:PRK13652  168 LD 169
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
18-222 6.49e-10

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 59.79  E-value: 6.49e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  18 LLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGelpLDDGRMVQQQDLKVTRLEQDPPASSDLTVFDytaeglagVGEL 97
Cdd:PRK10584   25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAG---LDDGSSGEVSLVGQPLHQMDEEARAKLRAKH--------VGFV 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  98 LKKYHHISMELAHDpsdaNIRIMSDLQEQLDYQNgwqfETRISQVLTLLNLDP--DATLDSLSGGWLRKVALARALACDP 175
Cdd:PRK10584   94 FQSFMLIPTLNALE----NVELPALLRGESSRQS----RNGAKALLEQLGLGKrlDHLPAQLSGGEQQRVALARAFNGRP 165
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1411607396 176 DLLLLDEPTNHLDIEAINWLEDFL----KDFRGAIVFISHDREfihkLATR 222
Cdd:PRK10584  166 DVLFADEPTGNLDRQTGDKIADLLfslnREHGTTLILVTHDLQ----LAAR 212
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
330-472 7.30e-10

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: 58.72  E-value: 7.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 330 GDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSR--GLVK-GGTKLE-------VAYFDQyRDQLDPEQT 399
Cdd:cd03213    20 SGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLiNGRPLDkrsfrkiIGYVPQ-DDILHPTLT 98
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1411607396 400 VmdnvgegkQEVMvrgrsrhilgylqdfLFEPKrartpVKALSGGEKNRLLLA-KLFLKPSnLLILDEPTNDLD 472
Cdd:cd03213    99 V--------RETL---------------MFAAK-----LRGLSGGERKRVSIAlELVSNPS-LLFLDEPTSGLD 143
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
2-214 7.69e-10

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 61.57  E-value: 7.69e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   2 ALLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPlddgrmvqqQDLkvtrleqdppaSSDL 81
Cdd:PRK10938  259 PRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHP---------QGY-----------SNDL 318
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  82 TVFDYTaeglAGVGELL---KKyhHI-----SMELAHDPSdANIR--IMS-------------DLQEQLDYQngWqfetr 138
Cdd:PRK10938  319 TLFGRR----RGSGETIwdiKK--HIgyvssSLHLDYRVS-TSVRnvILSgffdsigiyqavsDRQQKLAQQ--W----- 384
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 139 isqvLTLLNLD---PDATLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDieAIN------WLEDFLKDFRGAIVFI 209
Cdd:PRK10938  385 ----LDILGIDkrtADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLD--PLNrqlvrrFVDVLISEGETQLLFV 458

                  ....*
gi 1411607396 210 SHDRE 214
Cdd:PRK10938  459 SHHAE 463
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
11-188 7.80e-10

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: 58.72  E-value: 7.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  11 LSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELP--------LDDGRMVQQQDLK--VTRLEQDPPASSD 80
Cdd:cd03213    17 PSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTglgvsgevLINGRPLDKRSFRkiIGYVPQDDILHPT 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  81 LTVfdytaeglagvgellkkyhhismelahdpsdanirimsdlQEQLDYQngwqfetrisqvltllnldpdATLDSLSGG 160
Cdd:cd03213    97 LTV----------------------------------------RETLMFA---------------------AKLRGLSGG 115
                         170       180
                  ....*....|....*....|....*...
gi 1411607396 161 WLRKVALARALACDPDLLLLDEPTNHLD 188
Cdd:cd03213   116 ERKRVSIALELVSNPSLLFLDEPTSGLD 143
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
309-472 8.26e-10

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


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 59.67  E-value: 8.26e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 309 MDDVNRSGKLVFETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLL--LGQLEPS-RglVKGgtklEVA 385
Cdd:COG1117     1 MTAPASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrMNDLIPGaR--VEG----EIL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 386 YFDQ--YRDQLDPEQ-----------------TVMDNVGEGkqeVMVRG-RSRHILgylqDFLFEP--KRA--------- 434
Cdd:COG1117    75 LDGEdiYDPDVDVVElrrrvgmvfqkpnpfpkSIYDNVAYG---LRLHGiKSKSEL----DEIVEEslRKAalwdevkdr 147
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1411607396 435 -RTPVKALSGGEKNRLLLAK-LFLKPSNLLiLDEPTNDLD 472
Cdd:COG1117   148 lKKSALGLSGGQQQRLCIARaLAVEPEVLL-MDEPTSALD 186
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
329-474 8.94e-10

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 59.34  E-value: 8.94e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 329 FGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKlLLGQLEPSRG---LVKG----GTKLEV--------AYFDQYrdQ 393
Cdd:PRK09493   11 FGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLR-CINKLEEITSgdlIVDGlkvnDPKVDErlirqeagMVFQQF--Y 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 394 LDPEQTVMDNVGEGKqeVMVRGRSRHILGYLQDFLFE----PKRARTPVKALSGGEKNRLLLAK-LFLKPsNLLILDEPT 468
Cdd:PRK09493   88 LFPHLTALENVMFGP--LRVRGASKEEAEKQARELLAkvglAERAHHYPSELSGGQQQRVAIARaLAVKP-KLMLFDEPT 164

                  ....*.
gi 1411607396 469 NDLDVE 474
Cdd:PRK09493  165 SALDPE 170
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
17-209 9.08e-10

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


Pssm-ID: 273491 [Multi-domain]  Cd Length: 198  Bit Score: 58.52  E-value: 9.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  17 PLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRM-VQQQDLKVTRleqDPPASSDLtvfdYT--AEGLAG 93
Cdd:TIGR01189  14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVrWNGTPLAEQR---DEPHENIL----YLghLPGLKP 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  94 ---VGELLKKYHHIsmelaHDPSDANIrimsdlqeqldyqngwqfetriSQVLTLLNLD--PDATLDSLSGGWLRKVALA 168
Cdd:TIGR01189  87 elsALENLHFWAAI-----HGGAQRTI----------------------EDALAAVGLTgfEDLPAAQLSAGQQRRLALA 139
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1411607396 169 RALACDPDLLLLDEPTNHLDIEAINWLEDFLKDF--RGAIVFI 209
Cdd:TIGR01189 140 RLWLSRRPLWILDEPTTALDKAGVALLAGLLRAHlaRGGIVLL 182
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
325-497 9.48e-10

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127 [Multi-domain]  Cd Length: 200  Bit Score: 58.81  E-value: 9.48e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 325 LGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLV----KGGTKLEVAYFDQ-----YRDQLD 395
Cdd:PRK13540    7 LDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEIlferQSIKKDLCTYQKQlcfvgHRSGIN 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 396 PEQTVMDN------VGEGKQEV--MVRGRSrhiLGYLQDFlfepkrartPVKALSGGEKNRLLLAKLFLKPSNLLILDEP 467
Cdd:PRK13540   87 PYLTLRENclydihFSPGAVGIteLCRLFS---LEHLIDY---------PCGLLSSGQKRQVALLRLWMSKAKLWLLDEP 154
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1411607396 468 TNDLD---VETLELLEELLADYPGTLLLVSHDR 497
Cdd:PRK13540  155 LVALDelsLLTIITKIQEHRAKGGAVLLTSHQD 187
cbiO PRK13650
energy-coupling factor transporter ATPase;
14-233 9.65e-10

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 60.13  E-value: 9.65e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  14 SDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMVQQQDL-----------KVTRLEQDPPAS-SDL 81
Cdd:PRK13650   18 QEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLlteenvwdirhKIGMVFQNPDNQfVGA 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  82 TVFDYTAEGLAGVGellkkyhhismeLAHDpsdaniRIMSDLQEQLDYQNGWQFETRisqvltllnlDPDatldSLSGGW 161
Cdd:PRK13650   98 TVEDDVAFGLENKG------------IPHE------EMKERVNEALELVGMQDFKER----------EPA----RLSGGQ 145
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1411607396 162 LRKVALARALACDPDLLLLDEPTNHLD----IEAINWLEDFLKDFRGAIVFISHDREFIhKLATRIIDLDRGVITS 233
Cdd:PRK13650  146 KQRVAIAGAVAMRPKIIILDEATSMLDpegrLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQVES 220
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
331-472 9.96e-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: 59.21  E-value: 9.96e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 331 DRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQL---------------EPSRGLVKGgtklEVAYFDQYrDQLD 395
Cdd:cd03234    19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVegggttsgqilfngqPRKPDQFQK----CVAYVRQD-DILL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 396 PEQTVMDNV-------------GEGKQEVMVRGRSRHIlgylqdflfEPKRARTP-VKALSGGEKNRLLLAKLFLKPSNL 461
Cdd:cd03234    94 PGLTVRETLtytailrlprkssDAIRKKRVEDVLLRDL---------ALTRIGGNlVKGISGGERRRVSIAVQLLWDPKV 164
                         170
                  ....*....|.
gi 1411607396 462 LILDEPTNDLD 472
Cdd:cd03234   165 LILDEPTSGLD 175
cbiO PRK13644
energy-coupling factor transporter ATPase;
17-231 1.00e-09

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 60.00  E-value: 1.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  17 PLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMVqqqdlkVTRLEQ-DP---PASSDLTVFDYTAEGLA 92
Cdd:PRK13644   16 PALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVL------VSGIDTgDFsklQGIRKLVGIVFQNPETQ 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  93 GVGELLKKyhhismELAHDPSDANIRIMsdlqeqldyqngwQFETRISQVLTLLNLDP--DATLDSLSGGWLRKVALARA 170
Cdd:PRK13644   90 FVGRTVEE------DLAFGPENLCLPPI-------------EIRKRVDRALAEIGLEKyrHRSPKTLSGGQGQCVALAGI 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1411607396 171 LACDPDLLLLDEPTNHLDIEA-INWLEDFLKDFRGA--IVFISHDREFIHkLATRIIDLDRGVI 231
Cdd:PRK13644  151 LTMEPECLIFDEVTSMLDPDSgIAVLERIKKLHEKGktIVYITHNLEELH-DADRIIVMDRGKI 213
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
29-253 1.03e-09

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: 59.69  E-value: 1.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  29 GERLCLVGRNGAGKSTLMKIIAGELPLDDGRMvqqqdlkvtrleQDPPASSD-LTVFDYTAeglagVGELLKKYHHISME 107
Cdd:cd03236    26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGKF------------DDPPDWDEiLDEFRGSE-----LQNYFTKLLEGDVK 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 108 LAHDPS---------DANIRimsDLQEQLDYQNgwQFETRISQvltlLNLDP--DATLDSLSGGWLRKVALARALACDPD 176
Cdd:cd03236    89 VIVKPQyvdlipkavKGKVG---ELLKKKDERG--KLDELVDQ----LELRHvlDRNIDQLSGGELQRVAIAAALARDAD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 177 LLLLDEPTNHLDI----EAINWLEDFLKDFRgAIVFISHDREFIHKLATRIIDL-----DRGVITSWPG---NYDEYLQG 244
Cdd:cd03236   160 FYFFDEPSSYLDIkqrlNAARLIRELAEDDN-YVLVVEHDLAVLDYLSDYIHCLygepgAYGVVTLPKSvreGINEFLDG 238
                         250
                  ....*....|.
gi 1411607396 245 --KEEALRVEE 253
Cdd:cd03236   239 ylPTENMRFRE 249
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
344-473 1.32e-09

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 60.98  E-value: 1.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 344 RGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKG------------GT------------KLEVAYFDQYRDQLdPEQt 399
Cdd:PRK13409   98 EGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEepswdevlkrfrGTelqnyfkklyngEIKVVHKPQYVDLI-PKV- 175
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1411607396 400 VMDNVGEGKQEVMVRGRSRHILGYLQdflFEPKRARtPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDV 473
Cdd:PRK13409  176 FKGKVRELLKKVDERGKLDEVVERLG---LENILDR-DISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDI 245
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
323-475 1.33e-09

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 59.33  E-value: 1.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 323 EGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGL-------VKG-GTKLEVAYFDqyrDQL 394
Cdd:PRK11248    5 SHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSitldgkpVEGpGAERGVVFQN---EGL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 395 DPEQTVMDNVGEGKQEVMV-----RGRSRHILGYLQDFLFEPKRartpVKALSGGEKNRLLLAKLFLKPSNLLILDEPTN 469
Cdd:PRK11248   82 LPWRNVQDNVAFGLQLAGVekmqrLEIAHQMLKKVGLEGAEKRY----IWQLSGGQRQRVGIARALAANPQLLLLDEPFG 157

                  ....*.
gi 1411607396 470 DLDVET 475
Cdd:PRK11248  158 ALDAFT 163
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
345-474 1.35e-09

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 58.87  E-value: 1.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 345 GDKIALVGPNGCGKSTLIKlLLGQLE-PSRGlvkggtKLEVA--YFD----------------------QYrdQLDPEQT 399
Cdd:PRK11124   28 GETLVLLGPSGAGKSSLLR-VLNLLEmPRSG------TLNIAgnHFDfsktpsdkairelrrnvgmvfqQY--NLWPHLT 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 400 VMDNV--------GEGKQEVMvrGRSRHILGYLQdflFEPKRARTPVKaLSGGEKNRLLLAK-LFLKPSNLLiLDEPTND 470
Cdd:PRK11124   99 VQQNLieapcrvlGLSKDQAL--ARAEKLLERLR---LKPYADRFPLH-LSGGQQQRVAIARaLMMEPQVLL-FDEPTAA 171

                  ....
gi 1411607396 471 LDVE 474
Cdd:PRK11124  172 LDPE 175
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
4-229 1.61e-09

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: 57.86  E-value: 1.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   4 LTLHGACLSFSD-----FPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGrMVQQQDlKVTRLEQDPPAS 78
Cdd:cd03250     1 ISVEDASFTWDSgeqetSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSG-SVSVPG-SIAYVSQEPWIQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  79 SDlTVFDytaeglagvgellkkyhhismelahdpsdaNIRIMSDLQEQldyqngwqfetRISQVLTLLNLDPD-ATLD-- 155
Cdd:cd03250    79 NG-TIRE------------------------------NILFGKPFDEE-----------RYEKVIKACALEPDlEILPdg 116
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 156 ----------SLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLED-----FLKDFRgAIVFISHDREFIHKlA 220
Cdd:cd03250   117 dlteigekgiNLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFEncilgLLLNNK-TRILVTHQLQLLPH-A 194

                  ....*....
gi 1411607396 221 TRIIDLDRG 229
Cdd:cd03250   195 DQIVVLDNG 203
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
15-231 1.80e-09

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


Pssm-ID: 213184 [Multi-domain]  Cd Length: 200  Bit Score: 57.92  E-value: 1.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  15 DFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGelplddgrmvqQQDLKVTRleqdppassdltvfdytaeglagv 94
Cdd:cd03217    12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG-----------HPKYEVTE------------------------ 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  95 GELLKKYHHISMELAHDPSDANIRIMsdlqeqldyqngWQFETRISQVLT---LLNLDpdatlDSLSGGWLRKVALARAL 171
Cdd:cd03217    57 GEILFKGEDITDLPPEERARLGIFLA------------FQYPPEIPGVKNadfLRYVN-----EGFSGGEKKRNEILQLL 119
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1411607396 172 ACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRG---AIVFISHDREFI-HKLATRIIDLDRGVI 231
Cdd:cd03217   120 LLEPDLAILDEPDSGLDIDALRLVAEVINKLREegkSVLIITHYQRLLdYIKPDRVHVLYDGRI 183
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
11-247 1.86e-09

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 58.91  E-value: 1.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  11 LSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMvqQQDLKVTRLEQDppassdltVFDYTAEG 90
Cdd:PRK14246   18 LYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKI--KVDGKVLYFGKD--------IFQIDAIK 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  91 L-AGVGELLKK---YHHISM--ELAHDPSDANIR----IMSDLQEQLDYQNGWQfetrisQVLTLLNldpdATLDSLSGG 160
Cdd:PRK14246   88 LrKEVGMVFQQpnpFPHLSIydNIAYPLKSHGIKekreIKKIVEECLRKVGLWK------EVYDRLN----SPASQLSGG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 161 WLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRG--AIVFISHDREFIHKLATRIIDLDRGVITSWPGNY 238
Cdd:PRK14246  158 QQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSN 237

                  ....*....
gi 1411607396 239 DEYLQGKEE 247
Cdd:PRK14246  238 EIFTSPKNE 246
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
329-472 1.92e-09

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 59.66  E-value: 1.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 329 FGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRG-LVKGGTKL-EVA--------YFDQYrdQLDPEQ 398
Cdd:PRK11000   13 YGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGdLFIGEKRMnDVPpaergvgmVFQSY--ALYPHL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 399 TVMDNV-------GEGKQEvmVRGRSRHILGYLQ-DFLFEpkraRTPvKALSGGEKNRLLLAKLFLKPSNLLILDEPTND 470
Cdd:PRK11000   91 SVAENMsfglklaGAKKEE--INQRVNQVAEVLQlAHLLD----RKP-KALSGGQRQRVAIGRTLVAEPSVFLLDEPLSN 163

                  ..
gi 1411607396 471 LD 472
Cdd:PRK11000  164 LD 165
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
4-231 1.95e-09

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 58.92  E-value: 1.95e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   4 LTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGelplddgrmvqqqdlkvtrLEQdpPASSDLtv 83
Cdd:PRK11247   13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAG-------------------LET--PSAGEL-- 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  84 fdytaegLAGVGELlkkyhhismelaHDPSDaNIRIMsdLQEQ-------------LDYQNGWQFETRisQVLTLLNLDP 150
Cdd:PRK11247   70 -------LAGTAPL------------AEARE-DTRLM--FQDArllpwkkvidnvgLGLKGQWRDAAL--QALAAVGLAD 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 151 DAT--LDSLSGGWLRKVALARALACDPDLLLLDEPTNHLD----IEAINWLEDFLKDFRGAIVFISHDREFIHKLATRII 224
Cdd:PRK11247  126 RANewPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDaltrIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVL 205

                  ....*..
gi 1411607396 225 DLDRGVI 231
Cdd:PRK11247  206 LIEEGKI 212
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
337-473 2.20e-09

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: 57.76  E-value: 2.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 337 GLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGlvkggtKLEVAYFDQYRDQLD---------------PEQTVM 401
Cdd:cd03266    23 GVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAG------FATVDGFDVVKEPAEarrrlgfvsdstglyDRLTAR 96
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1411607396 402 DNVG-----EGKQEVMVRGRSRHILGYLQdflFEPKRARtPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDV 473
Cdd:cd03266    97 ENLEyfaglYGLKGDELTARLEELADRLG---MEELLDR-RVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDV 169
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
331-475 2.43e-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: 2.43e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 331 DRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGqLEPSR-GLVKGGTKLEVAYFDQ--Yrdqldpeqtvmdnvgeg 407
Cdd:cd03223    13 GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAG-LWPWGsGRIGMPEGEDLLFLPQrpY----------------- 74
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1411607396 408 kqevMVRGRSRHILGYLQDflfepkrartpvKALSGGEKNRLLLAKLFL-KPSnLLILDEPTNDLDVET 475
Cdd:cd03223    75 ----LPLGTLREQLIYPWD------------DVLSGGEQQRLAFARLLLhKPK-FVFLDEATSALDEES 126
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
320-548 2.52e-09

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 58.54  E-value: 2.52e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 320 FETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTKLEVAYFDQYRD-----Q 393
Cdd:PRK10419   13 YAHGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSwRGEPLAKLNRAQRKAfrrdiQ 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 394 L---------DPEQTVMDNVGEGKQEVMV---RGRSRHILGYLQDFLFEPKRARTPVKALSGGEKNRLLLAKLFLKPSNL 461
Cdd:PRK10419   93 MvfqdsisavNPRKTVREIIREPLRHLLSldkAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKL 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 462 LILDEPTNDLDVETLELLEELLADYP---GT-LLLVSHDRRFIDNTVTGCWLFEGDGRISDYVGGYADMM---ATRAQQS 534
Cdd:PRK10419  173 LILDEAVSNLDLVLQAGVIRLLKKLQqqfGTaCLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDKLTFsspAGRVLQN 252
                         250
                  ....*....|....
gi 1411607396 535 TQLAAKAAQVKTPE 548
Cdd:PRK10419  253 AVLPAFPVRRRTTE 266
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
149-232 2.66e-09

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 60.06  E-value: 2.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 149 DPDATLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRG---AIVFISHDREFIHKLATRIID 225
Cdd:PRK15439  396 HAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAqnvAVLFISSDLEEIEQMADRVLV 475

                  ....*..
gi 1411607396 226 LDRGVIT 232
Cdd:PRK15439  476 MHQGEIS 482
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
336-468 2.80e-09

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: 58.07  E-value: 2.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 336 QGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRG----------------LVKGGtkleVAYFDQYRdQLDPEQT 399
Cdd:COG0410    20 HGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGsirfdgeditglpphrIARLG----IGYVPEGR-RIFPSLT 94
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1411607396 400 VMDN--VGegkqevMVRGRSRHILGYLQDFLFE--PK---RARTPVKALSGGEKNRLLLAK-LFLKPSnLLILDEPT 468
Cdd:COG0410    95 VEENllLG------AYARRDRAEVRADLERVYElfPRlkeRRRQRAGTLSGGEQQMLAIGRaLMSRPK-LLLLDEPS 164
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
17-232 2.81e-09

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 59.65  E-value: 2.81e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  17 PLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRM-VQQQDLKVTrleqDPPASSDLTVF----DYTAEGL 91
Cdd:COG1129   266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIrLDGKPVRIR----SPRDAIRAGIAyvpeDRKGEGL 341
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  92 AG---VGEllkkyhHISmeLAHDPSDANIRIMSDLQEQldyqngwqfeTRISQVLTLLNL---DPDATLDSLSGGWLRKV 165
Cdd:COG1129   342 VLdlsIRE------NIT--LASLDRLSRGGLLDRRRER----------ALAEEYIKRLRIktpSPEQPVGNLSGGNQQKV 403
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 166 ALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDF--RG-AIVFISHDREFIHKLATRIIDLDRGVIT 232
Cdd:COG1129   404 VLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELaaEGkAVIVISSELPELLGLSDRILVMREGRIV 473
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
14-231 2.84e-09

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 58.22  E-value: 2.84e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  14 SDFPL-LDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRM------VQQQDLKVTRLE-----QDPPASsdl 81
Cdd:PRK13648   19 SDASFtLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnqaITDDNFEKLRKHigivfQNPDNQ--- 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  82 tvFdytaeglagVGELLKKYHHISMELAHDPSDANIRIMSDLQEQLDYQNGWQFETRisqvltllnldpdatldSLSGGW 161
Cdd:PRK13648   96 --F---------VGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPN-----------------ALSGGQ 147
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1411607396 162 LRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRG----AIVFISHD-REFIHklATRIIDLDRGVI 231
Cdd:PRK13648  148 KQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSehniTIISITHDlSEAME--ADHVIVMNKGTV 220
cbiO PRK13649
energy-coupling factor transporter ATPase;
326-472 2.97e-09

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 58.60  E-value: 2.97e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 326 GLDFGDRTLFqGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKGGTKL---------------EVAYFDQY 390
Cdd:PRK13649   15 GTPFEGRALF-DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLitstsknkdikqirkKVGLVFQF 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 391 RDQLDPEQTVMDNVGEGKQ-------EVMVRGRSRHILGYLQDFLFEpkraRTPVKaLSGGEKNRLLLAKLFLKPSNLLI 463
Cdd:PRK13649   94 PESQLFEETVLKDVAFGPQnfgvsqeEAEALAREKLALVGISESLFE----KNPFE-LSGGQMRRVAIAGILAMEPKILV 168

                  ....*....
gi 1411607396 464 LDEPTNDLD 472
Cdd:PRK13649  169 LDEPTAGLD 177
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
11-189 3.04e-09

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: 60.31  E-value: 3.04e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   11 LSFSDF-----PLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMVQQqdlkvTRLEQDPPASSDL--TV 83
Cdd:TIGR01271  429 LFFSNFslyvtPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHS-----GRISFSPQTSWIMpgTI 503
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   84 FDYTAEGLAgvgelLKKYHHISMelahdpsdanirimsdlqeqldyQNGWQFETRISQvltLLNLDPDATLD---SLSGG 160
Cdd:TIGR01271  504 KDNIIFGLS-----YDEYRYTSV-----------------------IKACQLEEDIAL---FPEKDKTVLGEggiTLSGG 552
                          170       180
                   ....*....|....*....|....*....
gi 1411607396  161 WLRKVALARALACDPDLLLLDEPTNHLDI 189
Cdd:TIGR01271  553 QRARISLARAVYKDADLYLLDSPFTHLDV 581
PRK13543 PRK13543
heme ABC exporter ATP-binding protein CcmA;
2-226 3.36e-09

heme ABC exporter ATP-binding protein CcmA;


Pssm-ID: 184129 [Multi-domain]  Cd Length: 214  Bit Score: 57.17  E-value: 3.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   2 ALLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMvqqqdlkvtRLEQDPPASSDL 81
Cdd:PRK13543   10 PLLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQI---------QIDGKTATRGDR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  82 TvfdytaeglagvgellkkyHHISMeLAHDPSdanirIMSDLQ--EQLDYQNGWQ---FETRISQVLTLLNLD--PDATL 154
Cdd:PRK13543   81 S-------------------RFMAY-LGHLPG-----LKADLStlENLHFLCGLHgrrAKQMPGSALAIVGLAgyEDTLV 135
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1411607396 155 DSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDF---RGAIVFISHDREFIHKLATRIIDL 226
Cdd:PRK13543  136 RQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISAHlrgGGAALVTTHGAYAAPPVRTRMLTL 210
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
319-472 3.84e-09

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 58.32  E-value: 3.84e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 319 VFETEGLGLDFGDRT-LFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLV-----------KGGTKLEVA- 385
Cdd:PRK13636    5 ILKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRIlfdgkpidysrKGLMKLRESv 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 386 --YFDQYRDQLDPEQTVMD------NVGEGKQEvmVRGRSRHILGYLQdflFEPKRARtPVKALSGGEKNRLLLAKLFLK 457
Cdd:PRK13636   85 gmVFQDPDNQLFSASVYQDvsfgavNLKLPEDE--VRKRVDNALKRTG---IEHLKDK-PTHCLSFGQKKRVAIAGVLVM 158
                         170
                  ....*....|....*
gi 1411607396 458 PSNLLILDEPTNDLD 472
Cdd:PRK13636  159 EPKVLVLDEPTAGLD 173
ycf16 CHL00131
sulfate ABC transporter protein; Validated
12-211 3.85e-09

sulfate ABC transporter protein; Validated


Pssm-ID: 214372 [Multi-domain]  Cd Length: 252  Bit Score: 57.73  E-value: 3.85e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  12 SFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGElP----LDDGRMVQQQDLkvtrLEQDPPASSDLTV---F 84
Cdd:CHL00131   16 SVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGH-PaykiLEGDILFKGESI----LDLEPEERAHLGIflaF 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  85 DYTAEgLAGVG--ELLKkyhhismeLAHdpsdaNIRIMSDLQEQLDyqnGWQFETRISQVLTLLNLDPD----ATLDSLS 158
Cdd:CHL00131   91 QYPIE-IPGVSnaDFLR--------LAY-----NSKRKFQGLPELD---PLEFLEIINEKLKLVGMDPSflsrNVNEGFS 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1411607396 159 GGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRG---AIVFISH 211
Cdd:CHL00131  154 GGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTsenSIILITH 209
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
29-231 4.56e-09

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 59.48  E-value: 4.56e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  29 GERLCLVGRNGAGKST----LMKII---AGELPLDDGRMVQQQDLKVTRLE-------QDPPASSD--LTVFDYTAEGLa 92
Cdd:PRK10261  350 GETLSLVGESGSGKSTtgraLLRLVesqGGEIIFNGQRIDTLSPGKLQALRrdiqfifQDPYASLDprQTVGDSIMEPL- 428
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  93 gvgellkkyhhismelahdpsdaniRIMSDLQeqldyqnGWQFETRISQVLTLLNLDPDATL---DSLSGGWLRKVALAR 169
Cdd:PRK10261  429 -------------------------RVHGLLP-------GKAAAARVAWLLERVGLLPEHAWrypHEFSGGQRQRICIAR 476
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1411607396 170 ALACDPDLLLLDEPTNHLDI----EAINWLEDFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVI 231
Cdd:PRK10261  477 ALALNPKVIIADEAVSALDVsirgQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQI 542
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
5-189 5.02e-09

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 57.49  E-value: 5.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   5 TLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGR-MVQQQDL----------KVTRLEQ 73
Cdd:PRK10575   13 ALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEiLLDAQPLeswsskafarKVAYLPQ 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  74 DPPASSDLTVFDYTAEGLAGVGELLKKYhhismelahdpsdanirimsdlqeqldyqnGWQFETRISQVLTLLNLDPDAT 153
Cdd:PRK10575   93 QLPAAEGMTVRELVAIGRYPWHGALGRF------------------------------GAADREKVEEAISLVGLKPLAH 142
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1411607396 154 --LDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDI 189
Cdd:PRK10575  143 rlVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDI 180
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
320-467 5.76e-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: 56.78  E-value: 5.76e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 320 FETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRG--LVKGG--TKLEVayfdQYRDQLD 395
Cdd:cd03218     1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGkiLLDGQdiTKLPM----HKRARLG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 396 ----PEQ-------TVMDN---VGEGkQEVMVRGRSRHILGYLQDFLFEPKRaRTPVKALSGGEKNRLLLAK-LFLKPSN 460
Cdd:cd03218    77 igylPQEasifrklTVEENilaVLEI-RGLSKKEREEKLEELLEEFHITHLR-KSKASSLSGGERRRVEIARaLATNPKF 154

                  ....*..
gi 1411607396 461 LLiLDEP 467
Cdd:cd03218   155 LL-LDEP 160
cbiO PRK13641
energy-coupling factor transporter ATPase;
19-229 6.07e-09

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 57.53  E-value: 6.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  19 LDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPlddgrmvqqqdlkvtrleqdpPASSDLTVFDY--TAE-GLAGVG 95
Cdd:PRK13641   23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLK---------------------PSSGTITIAGYhiTPEtGNKNLK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  96 ELLKKyhhisMELAHDPSDANI---RIMSDLQ---------EQLDYQNGWQFETRISQVLTLLNLDPDatldSLSGGWLR 163
Cdd:PRK13641   82 KLRKK-----VSLVFQFPEAQLfenTVLKDVEfgpknfgfsEDEAKEKALKWLKKVGLSEDLISKSPF----ELSGGQMR 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1411607396 164 KVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRGA---IVFISHDREFIHKLATRIIDLDRG 229
Cdd:PRK13641  153 RVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAghtVILVTHNMDDVAEYADDVLVLEHG 221
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
330-472 6.41e-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: 56.93  E-value: 6.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 330 GDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKGGTKlEVAYFDQ--------YRDQ---LDPEQ 398
Cdd:cd03295    12 GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGE-DIREQDPvelrrkigYVIQqigLFPHM 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 399 TVMDNVG-----EGKQEVMVRGRSRHILGYLQdflFEPK--RARTPvKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDL 471
Cdd:cd03295    91 TVEENIAlvpklLKWPKEKIRERADELLALVG---LDPAefADRYP-HELSGGQQQRVGVARALAADPPLLLMDEPFGAL 166

                  .
gi 1411607396 472 D 472
Cdd:cd03295   167 D 167
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
18-226 6.48e-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: 6.48e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  18 LLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMVQQQdlkvtrleqdppassdltvfdytaeglAGVGEL 97
Cdd:cd03231    15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNG---------------------------GPLDFQ 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  98 LKKYHHISMELAHDPSdanIRIMSDLQEQLDYQNGWQFETRISQVLTLLNLD--PDATLDSLSGGWLRKVALARALACDP 175
Cdd:cd03231    68 RDSIARGLLYLGHAPG---IKTTLSVLENLRFWHADHSDEQVEEALARVGLNgfEDRPVAQLSAGQQRRVALARLLLSGR 144
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1411607396 176 DLLLLDEPTNHLDIEAINWLEDFLKDFR---GAIVFISHDREFIHKLATRIIDL 226
Cdd:cd03231   145 PLWILDEPTTALDKAGVARFAEAMAGHCargGMVVLTTHQDLGLSEAGARELDL 198
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
1-216 6.62e-09

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


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 56.51  E-value: 6.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   1 MALLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELP-LDDGRMVQQQDLKVTR----LEQDP 75
Cdd:COG2401    28 AIVLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgTPVAGCVDVPDNQFGReaslIDAIG 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  76 PASSDLTVFDY-TAEGLAGVGELLKKYHHISmelahdpsdanirimsdlqeqldyqNGWQFetrisqvltllnldpdatl 154
Cdd:COG2401   108 RKGDFKDAVELlNAVGLSDAVLWLRRFKELS-------------------------TGQKF------------------- 143
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1411607396 155 dslsggwlrKVALARALACDPDLLLLDEPTNHLD-----IEAINWLEdFLKDFRGAIVFISHDREFI 216
Cdd:COG2401   144 ---------RFRLALLLAERPKLLVIDEFCSHLDrqtakRVARNLQK-LARRAGITLVVATHHYDVI 200
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
329-497 6.71e-09

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


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 57.85  E-value: 6.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 329 FGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTKLE---------VAY-FDQYrdQLDPE 397
Cdd:COG1118    12 FGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVlNGRDLFtnlpprerrVGFvFQHY--ALFPH 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 398 QTVMDNVGEGKQevmVRGRSRH-----ILGYLQDFLFEPKRARTPvKALSGGEKNRLLLAK-LFLKPSnLLILDEPTNDL 471
Cdd:COG1118    90 MTVAENIAFGLR---VRPPSKAeirarVEELLELVQLEGLADRYP-SQLSGGQRQRVALARaLAVEPE-VLLLDEPFGAL 164
                         170       180       190
                  ....*....|....*....|....*....|
gi 1411607396 472 DV----ETLELLEELLADYPGTLLLVSHDR 497
Cdd:COG1118   165 DAkvrkELRRWLRRLHDELGGTTVFVTHDQ 194
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
319-520 7.36e-09

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 56.84  E-value: 7.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 319 VFETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLL--LGQLEPsRGLVKGGT--------KLEVAYFD 388
Cdd:PRK14247    3 KIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFnrLIELYP-EARVSGEVyldgqdifKMDVIELR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 389 QyRDQL-------DPEQTVMDNVGEG-------KQEVMVRGRSRHILGYLQDFLFEPKRARTPVKALSGGEKNRLLLAKL 454
Cdd:PRK14247   82 R-RVQMvfqipnpIPNLSIFENVALGlklnrlvKSKKELQERVRWALEKAQLWDEVKDRLDAPAGKLSGGQQQRLCIARA 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1411607396 455 FLKPSNLLILDEPTNDLDVETLELLEELLADYPG--TLLLVSHdrrfidntvtgcwlFEGD-GRISDYV 520
Cdd:PRK14247  161 LAFQPEVLLADEPTANLDPENTAKIESLFLELKKdmTIVLVTH--------------FPQQaARISDYV 215
nickel_nikE TIGR02769
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ...
320-516 7.49e-09

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: 57.12  E-value: 7.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 320 FETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKGG----TKLEVAYFDQYRDQL- 394
Cdd:TIGR02769  12 YRTGGLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRgqdlYQLDRKQRRAFRRDVq 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 395 ----------DPEQTVMDNVGEGKQEVM---VRGRSRHILGYLQDFLFEPKRARTPVKALSGGEKNRLLLAK-LFLKPsN 460
Cdd:TIGR02769  92 lvfqdspsavNPRMTVRQIIGEPLRHLTsldESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARaLAVKP-K 170
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 461 LLILDEPTNDLDV----ETLELLEELLADYPGTLLLVSHDRRFIDNTVTGCWLFEGdGRI 516
Cdd:TIGR02769 171 LIVLDEAVSNLDMvlqaVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDK-GQI 229
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
17-227 8.05e-09

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 55.97  E-value: 8.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  17 PLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRmVQQQDLKVTRleQDPPASSDLTVFDYtaegLAGVGE 96
Cdd:PRK13538   15 ILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGE-VLWQGEPIRR--QRDEYHQDLLYLGH----QPGIKT 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  97 LLKkyhhismelahdpSDANIRIMSDLQEQLDyqngwqfETRISQVLTLLNLD--PDATLDSLSGGWLRKVALARALACD 174
Cdd:PRK13538   88 ELT-------------ALENLRFYQRLHGPGD-------DEALWEALAQVGLAgfEDVPVRQLSAGQQRRVALARLWLTR 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1411607396 175 PDLLLLDEPTNHLDIEAINWLEDFLKDF--RGAIV-FISHDREFIHKLATRIIDLD 227
Cdd:PRK13538  148 APLWILDEPFTAIDKQGVARLEALLAQHaeQGGMViLTTHQDLPVASDKVRKLRLG 203
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
11-188 8.47e-09

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 58.32  E-value: 8.47e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  11 LSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLddgrmvqQQDLKVTRLEQdppasSDLTVFDYTAEg 90
Cdd:PRK11174  358 LSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPY-------QGSLKINGIEL-----RELDPESWRKH- 424
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  91 LAGVGE---LLKKYHHISMELA-HDPSDAnirimsDLQEQLDYQNGWQFETRISQVLTLLNLDPDATLdslSGGWLRKVA 166
Cdd:PRK11174  425 LSWVGQnpqLPHGTLRDNVLLGnPDASDE------QLQQALENAWVSEFLPLLPQGLDTPIGDQAAGL---SVGQAQRLA 495
                         170       180
                  ....*....|....*....|..
gi 1411607396 167 LARALACDPDLLLLDEPTNHLD 188
Cdd:PRK11174  496 LARALLQPCQLLLLDEPTASLD 517
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
345-473 1.05e-08

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: 56.61  E-value: 1.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 345 GDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKG------------GTKLEvAYFD-------------QYRDQLdPEQt 399
Cdd:cd03236    26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDppdwdeildefrGSELQ-NYFTkllegdvkvivkpQYVDLI-PKA- 102
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1411607396 400 VMDNVGegkqEVMVRGRSRHILGYLQDFL-FEPKRARTpVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDV 473
Cdd:cd03236   103 VKGKVG----ELLKKKDERGKLDELVDQLeLRHVLDRN-IDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDI 172
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
11-233 1.05e-08

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 56.53  E-value: 1.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  11 LSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIA-------GELPLDDGRMVQQQDLKVTR----LEQDPPASS 79
Cdd:PRK10253   15 LGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSrlmtpahGHVWLDGEHIQHYASKEVARriglLAQNATTPG 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  80 DLTVFDYTAEGlagvgellkKYhhismelAHDPSDANIRimsdlQEQLDYQNGWQFETRISQVltllnldPDATLDSLSG 159
Cdd:PRK10253   95 DITVQELVARG---------RY-------PHQPLFTRWR-----KEDEEAVTKAMQATGITHL-------ADQSVDTLSG 146
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1411607396 160 GWLRKVALARALACDPDLLLLDEPTNHLD----IEAINWLEDFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVITS 233
Cdd:PRK10253  147 GQRQRAWIAMVLAQETAIMLLDEPTTWLDishqIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVA 224
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
334-475 1.12e-08

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: 58.38  E-value: 1.12e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  334 LFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKGGTKleVAYFDQYrDQLDPeQTVMDNVGEGKQEVMV 413
Cdd:TIGR01271  441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR--ISFSPQT-SWIMP-GTIKDNIIFGLSYDEY 516
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1411607396  414 RGRSrhILGYLQ---DFLFEPKRARTPVK----ALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVET 475
Cdd:TIGR01271  517 RYTS--VIKACQleeDIALFPEKDKTVLGeggiTLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVT 583
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
316-475 1.17e-08

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: 55.13  E-value: 1.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 316 GKLVFETEGLGLdfgdRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRG--LVKGGT----------KLE 383
Cdd:cd03215     1 GEPVLEVRGLSV----KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGeiTLDGKPvtrrsprdaiRAG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 384 VAYF--DQYRDQLDPEQTVMDNVgegkqevmvrgrsrhILGYLqdflfepkrartpvkaLSGGEKNRLLLAKLFLKPSNL 461
Cdd:cd03215    77 IAYVpeDRKREGLVLDLSVAENI---------------ALSSL----------------LSGGNQQKVVLARWLARDPRV 125
                         170
                  ....*....|....
gi 1411607396 462 LILDEPTNDLDVET 475
Cdd:cd03215   126 LILDEPTRGVDVGA 139
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
329-499 1.20e-08

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 56.52  E-value: 1.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 329 FGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLV------------KGGtKLEVAYFDQYRD---- 392
Cdd:PRK10619   15 YGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIvvngqtinlvrdKDG-QLKVADKNQLRLlrtr 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 393 --------QLDPEQTVMDNVGEGKQEVM----VRGRSRHILGYLQDFLFEPKRARTPVKaLSGGEKNRLLLAKLFLKPSN 460
Cdd:PRK10619   94 ltmvfqhfNLWSHMTVLENVMEAPIQVLglskQEARERAVKYLAKVGIDERAQGKYPVH-LSGGQQQRVSIARALAMEPE 172
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1411607396 461 LLILDEPTNDLDVE---TLELLEELLADYPGTLLLVSHDRRF 499
Cdd:PRK10619  173 VLLFDEPTSALDPElvgEVLRIMQQLAEEGKTMVVVTHEMGF 214
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
345-474 1.25e-08

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


Pssm-ID: 443326 [Multi-domain]  Cd Length: 242  Bit Score: 56.17  E-value: 1.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 345 GDKIALVGPNGCGKSTLIKLL-------LGQLE--------PSRGLVKGGTKL--EVAY-FDQYrdQLDPEQTVMDNV-- 404
Cdd:COG4161    28 GETLVLLGPSGAGKSSLLRVLnlletpdSGQLNiaghqfdfSQKPSEKAIRLLrqKVGMvFQQY--NLWPHLTVMENLie 105
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1411607396 405 ------GEGKQEVmvRGRSRHILGYLQdflFEPKRARTPVkALSGGEKNRLLLAK-LFLKPSNLLiLDEPTNDLDVE 474
Cdd:COG4161   106 apckvlGLSKEQA--REKAMKLLARLR---LTDKADRFPL-HLSGGQQQRVAIARaLMMEPQVLL-FDEPTAALDPE 175
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
334-475 1.47e-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: 56.40  E-value: 1.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 334 LFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKGGTKleVAYFDQYrDQLDPeQTVMDNVGEGKQEVMV 413
Cdd:cd03291    52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR--ISFSSQF-SWIMP-GTIKENIIFGVSYDEY 127
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1411607396 414 RGRSRHILGYL-QDFLFEPKRARTPVK----ALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVET 475
Cdd:cd03291   128 RYKSVVKACQLeEDITKFPEKDNTVLGeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFT 194
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
337-473 1.50e-08

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


Pssm-ID: 440213 [Multi-domain]  Cd Length: 320  Bit Score: 56.60  E-value: 1.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 337 GLDLQVLRGDKIALVGPNGCGKSTLIKLLLGqLEPSRGLVKG-----G---TKLEVAYFDQYRDQ------------LDP 396
Cdd:COG0444    23 GVSFDVRRGETLGLVGESGSGKSTLARAILG-LLPPPGITSGeilfdGedlLKLSEKELRKIRGReiqmifqdpmtsLNP 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 397 EQTVMDNVGE--------GKQEVmvRGRSRHILG---------YLQDFLFEpkrartpvkaLSGGEKNRLLLAK-LFLKP 458
Cdd:COG0444   102 VMTVGDQIAEplrihgglSKAEA--RERAIELLErvglpdperRLDRYPHE----------LSGGMRQRVMIARaLALEP 169
                         170
                  ....*....|....*
gi 1411607396 459 SnLLILDEPTNDLDV 473
Cdd:COG0444   170 K-LLIADEPTTALDV 183
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
321-471 1.58e-08

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 57.49  E-value: 1.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVkggTKLEVAYfdqyrDQLDPEQTV 400
Cdd:PRK09700    7 SMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTI---TINNINY-----NKLDHKLAA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 401 MDNVGEGKQEVMV-------------RGRSRHILGY-LQDFLFEPKRAR-------------TPVKALSGGEKNRLLLAK 453
Cdd:PRK09700   79 QLGIGIIYQELSVideltvlenlyigRHLTKKVCGVnIIDWREMRVRAAmmllrvglkvdldEKVANLSISHKQMLEIAK 158
                         170
                  ....*....|....*...
gi 1411607396 454 LFLKPSNLLILDEPTNDL 471
Cdd:PRK09700  159 TLMLDAKVIIMDEPTSSL 176
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
329-500 1.66e-08

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 55.27  E-value: 1.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 329 FGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKGG----TKL---EVAYFDQ-----YRD-QLD 395
Cdd:PRK10908   12 LGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSghdiTRLknrEVPFLRRqigmiFQDhHLL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 396 PEQTVMDNVGegkQEVMVRGRS-----RHILGYLQDFLFEPKRARTPVKaLSGGEKNRLLLAKLFLKPSNLLILDEPTND 470
Cdd:PRK10908   92 MDRTVYDNVA---IPLIIAGASgddirRRVSAALDKVGLLDKAKNFPIQ-LSGGEQQRVGIARAVVNKPAVLLADEPTGN 167
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1411607396 471 LDVETLELLEELLADYPG---TLLLVSHDRRFI 500
Cdd:PRK10908  168 LDDALSEGILRLFEEFNRvgvTVLMATHDIGLI 200
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
344-503 1.71e-08

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: 53.92  E-value: 1.71e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  344 RGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKggtklevaYFDqyrdqldpeqtvmdnvGEGKQEVMVRGRSRHILGy 423
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVI--------YID----------------GEDILEEVLDQLLLIIVG- 55
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  424 lqdflfepkrarTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVETLELLEELLADYPGTLLLVSHDRRFIDNT 503
Cdd:smart00382  56 ------------GKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLTVILTT 123
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
2-243 1.92e-08

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 57.14  E-value: 1.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   2 ALLTLHGACLSFSD--FPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIA-------GELPLDDgrmvqqQDLKvtrle 72
Cdd:PRK11160  337 VSLTLNNVSFTYPDqpQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTrawdpqqGEILLNG------QPIA----- 405
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  73 qdppassdltvfDYTAEGL-AGVGELLKKYHHISMEL-------AHDPSDAnirimsdlqeqldyqngwQFETRISQV-L 143
Cdd:PRK11160  406 ------------DYSEAALrQAISVVSQRVHLFSATLrdnlllaAPNASDE------------------ALIEVLQQVgL 455
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 144 TLLnLDPDATLDS--------LSGGWLRKVALARALACDPDLLLLDEPTNHLDIEA---InwLEDFLKDFRG-AIVFISH 211
Cdd:PRK11160  456 EKL-LEDDKGLNAwlgeggrqLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETerqI--LELLAEHAQNkTVLMITH 532
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1411607396 212 DREFIHKLaTRIIDLDRG-VITSwpGNYDEYLQ 243
Cdd:PRK11160  533 RLTGLEQF-DRICVMDNGqIIEQ--GTHQELLA 562
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
4-231 1.98e-08

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 55.48  E-value: 1.98e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   4 LTLHGACLSfSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELP----------LDDGRMVQQQDL---KVTR 70
Cdd:PRK10418    5 IELRNIALQ-AAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPagvrqtagrvLLDGKPVAPCALrgrKIAT 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  71 LEQDPPASSD--LTVFDYTAEGLAGVGELlkkyhhismelahdPSDAnirimsdlqeqldyqngwqfetRISQVLTLLNL 148
Cdd:PRK10418   84 IMQNPRSAFNplHTMHTHARETCLALGKP--------------ADDA----------------------TLTAALEAVGL 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 149 -DPDATLDS----LSGGWLRKVALARALACDPDLLLLDEPTNHLDIEA----INWLEDFLKDFRGAIVFISHDREFIHKL 219
Cdd:PRK10418  128 eNAARVLKLypfeMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAqariLDLLESIVQKRALGMLLVTHDMGVVARL 207
                         250
                  ....*....|..
gi 1411607396 220 ATRIIDLDRGVI 231
Cdd:PRK10418  208 ADDVAVMSHGRI 219
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
17-232 2.24e-08

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: 57.07  E-value: 2.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  17 PLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELP-------LDD-----------GRMV----QQQDL-------K 67
Cdd:COG4618   346 PILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPptagsvrLDGadlsqwdreelGRHIgylpQDVELfdgtiaeN 425
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  68 VTRLEQDPPASsdltVFDytAEGLAGVGELlkkyhhismelahdpsdanirIMSdlqeqldYQNGwqFETRIsqvltlln 147
Cdd:COG4618   426 IARFGDADPEK----VVA--AAKLAGVHEM---------------------ILR-------LPDG--YDTRI-------- 461
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 148 ldpDATLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLD-------IEAInwleDFLKDFRGAIVFISHDREFIhKLA 220
Cdd:COG4618   462 ---GEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDdegeaalAAAI----RALKARGATVVVITHRPSLL-AAV 533
                         250
                  ....*....|..
gi 1411607396 221 TRIIDLDRGVIT 232
Cdd:COG4618   534 DKLLVLRDGRVQ 545
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
2-226 2.50e-08

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 55.11  E-value: 2.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   2 ALLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMV-QQQDL----------KVTR 70
Cdd:PRK10247    6 PLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLfEGEDIstlkpeiyrqQVSY 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  71 LEQDPPASSDlTVFDytaeglagvgELLKKYhhismELAHDPSDANiRIMSDLQeqldyqngwQFETrisqvltllnldP 150
Cdd:PRK10247   86 CAQTPTLFGD-TVYD----------NLIFPW-----QIRNQQPDPA-IFLDDLE---------RFAL------------P 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 151 DATLD----SLSGGWLRKVALARALACDPDLLLLDEPTNHLD----IEAINWLEDFLKDFRGAIVFISHDREFIhKLATR 222
Cdd:PRK10247  128 DTILTkniaELSGGEKQRISLIRNLQFMPKVLLLDEITSALDesnkHNVNEIIHRYVREQNIAVLWVTHDKDEI-NHADK 206

                  ....
gi 1411607396 223 IIDL 226
Cdd:PRK10247  207 VITL 210
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
12-229 2.63e-08

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 55.40  E-value: 2.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  12 SFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDD---------GRMVQQQ-----DLKVTRLE----- 72
Cdd:PRK09984   13 TFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagshiellGRTVQREgrlarDIRKSRANtgyif 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  73 QDPPASSDLTVFDYTAEGLAGVGELLKkyhhismelahdpsdANIRIMSDLQEQldyqngwqfetRISQVLTLLNLDPDA 152
Cdd:PRK09984   93 QQFNLVNRLSVLENVLIGALGSTPFWR---------------TCFSWFTREQKQ-----------RALQALTRVGMVHFA 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 153 --TLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFR---GAIVFIS-HDREFIHKLATRIIDL 226
Cdd:PRK09984  147 hqRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINqndGITVVVTlHQVDYALRYCERIVAL 226

                  ...
gi 1411607396 227 DRG 229
Cdd:PRK09984  227 RQG 229
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
17-229 2.67e-08

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: 57.33  E-value: 2.67e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   17 PLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMVQQQDLKVTRLEQDPPASSDLTVFDYTAEGLAGvge 96
Cdd:TIGR01257 1953 PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMGYCPQFDAIDDLLTG--- 2029
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   97 llKKYHHISMELAHDPSdanirimsdlqEQLDYQNGWQFETrisqvlTLLNLDPDATLDSLSGGWLRKVALARALACDPD 176
Cdd:TIGR01257 2030 --REHLYLYARLRGVPA-----------EEIEKVANWSIQS------LGLSLYADRLAGTYSGGNKRKLSTAIALIGCPP 2090
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1411607396  177 LLLLDEPTNHLDIEA----INWLEDFLKDFRgAIVFISHDREFIHKLATRIIDLDRG 229
Cdd:TIGR01257 2091 LVLLDEPTTGMDPQArrmlWNTIVSIIREGR-AVVLTSHSMEECEALCTRLAIMVKG 2146
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
2-237 2.68e-08

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 57.04  E-value: 2.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   2 ALLTLHGACLSF----SDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIaGEL--PLDDGRMVQQQDlkVTRLEQDP 75
Cdd:PRK10535    3 ALLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNIL-GCLdkPTSGTYRVAGQD--VATLDADA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  76 PASSDLTVFdytaeglagvGELLKKYHHismeLAHDPSDANIRI---MSDLQEQldyqngwQFETRISQVLTLLNLDP-- 150
Cdd:PRK10535   80 LAQLRREHF----------GFIFQRYHL----LSHLTAAQNVEVpavYAGLERK-------QRLLRAQELLQRLGLEDrv 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 151 DATLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLD----IEAINWLEDfLKDfRGAIVFI-SHDREfIHKLATRIID 225
Cdd:PRK10535  139 EYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDshsgEEVMAILHQ-LRD-RGHTVIIvTHDPQ-VAAQAERVIE 215
                         250
                  ....*....|..
gi 1411607396 226 LDRGVITSWPGN 237
Cdd:PRK10535  216 IRDGEIVRNPPA 227
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
311-521 2.84e-08

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 55.44  E-value: 2.84e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 311 DVNRSGKLVFETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKGGTKleVAYFDQY 390
Cdd:PRK14246    2 EAGKSAEDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGK--VLYFGKD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 391 RDQLD------------------PEQTVMDNVGEGKQEVMVRGRsRHILGYLQDFLFEP-------KRARTPVKALSGGE 445
Cdd:PRK14246   80 IFQIDaiklrkevgmvfqqpnpfPHLSIYDNIAYPLKSHGIKEK-REIKKIVEECLRKVglwkevyDRLNSPASQLSGGQ 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1411607396 446 KNRLLLAK-LFLKPSnLLILDEPTNDLDVETLELLEELLADYPG--TLLLVSHDRRFIdntvtgcwlfegdGRISDYVG 521
Cdd:PRK14246  159 QQRLTIARaLALKPK-VLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHNPQQV-------------ARVADYVA 223
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
19-231 2.88e-08

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 55.48  E-value: 2.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  19 LDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRM-VQQQDLKVTRLEQDPPASSDLtVFDYTAEGLagVGEL 97
Cdd:PRK13633   26 LDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVyVDGLDTSDEENLWDIRNKAGM-VFQNPDNQI--VATI 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  98 LKKyhhismELAHDPSDANI---RIMSDLQEQLDYQNGWQFETRISQVLtllnldpdatldslSGGWLRKVALARALACD 174
Cdd:PRK13633  103 VEE------DVAFGPENLGIppeEIRERVDESLKKVGMYEYRRHAPHLL--------------SGGQKQRVAIAGILAMR 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1411607396 175 PDLLLLDEPTNHLD----IEAINWLEDFLKDFRGAIVFISHDREFIHKlATRIIDLDRGVI 231
Cdd:PRK13633  163 PECIIFDEPTAMLDpsgrREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKV 222
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
321-472 3.71e-08

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


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 55.11  E-value: 3.71e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGlvkggtklEVAYFDQYRDQLD----- 395
Cdd:COG4152     3 ELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSG--------EVLWDGEPLDPEDrrrig 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 396 --PE-------QTVMDNV-------GEGKQEVMVRGrsrhilgylqDFLFE----PKRARTPVKALSGGEKNRL-LLAKL 454
Cdd:COG4152    75 ylPEerglypkMKVGEQLvylarlkGLSKAEAKRRA----------DEWLErlglGDRANKKVEELSKGNQQKVqLIAAL 144
                         170
                  ....*....|....*...
gi 1411607396 455 FLKPSnLLILDEPTNDLD 472
Cdd:COG4152   145 LHDPE-LLILDEPFSGLD 161
PRK15093 PRK15093
peptide ABC transporter ATP-binding protein SapD;
1-223 3.74e-08

peptide ABC transporter ATP-binding protein SapD;


Pssm-ID: 185049 [Multi-domain]  Cd Length: 330  Bit Score: 55.58  E-value: 3.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   1 MALLTLHGACLSF--SDFPL--LDNAELSIERGERLCLVGRNGAGKSTLMKIIAGelplddgrmVQQQDLKVT--RLEQD 74
Cdd:PRK15093    1 MPLLDIRNLTIEFktSDGWVkaVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICG---------VTKDNWRVTadRMRFD 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  75 ppassDLTVFDYTA-EGLAGVGellkkyHHISMELAH-----DPSDaniRIMSDLQEQL---DYQNGW--QFETRISQVL 143
Cdd:PRK15093   72 -----DIDLLRLSPrERRKLVG------HNVSMIFQEpqsclDPSE---RVGRQLMQNIpgwTYKGRWwqRFGWRKRRAI 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 144 TLLNL----DPDATLDS----LSGGWLRKVALARALACDPDLLLLDEPTNHLD----IEAINWLEDFLKDFRGAIVFISH 211
Cdd:PRK15093  138 ELLHRvgikDHKDAMRSfpyeLTEGECQKVMIAIALANQPRLLIADEPTNAMEpttqAQIFRLLTRLNQNNNTTILLISH 217
                         250
                  ....*....|..
gi 1411607396 212 DREFIHKLATRI 223
Cdd:PRK15093  218 DLQMLSQWADKI 229
3a01203 TIGR00954
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...
281-495 3.98e-08

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: 56.30  E-value: 3.98e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 281 NEGRVRALEAMRMERSQRRELQGKAKLQMDDvNRsgkLVFETEGLGLDFGDrTLFQGLDLQVLRGDKIALVGPNGCGKST 360
Cdd:TIGR00954 419 KRPRVEEIESGREGGRNSNLVPGRGIVEYQD-NG---IKFENIPLVTPNGD-VLIESLSFEVPSGNNLLICGPNGCGKSS 493
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 361 LIKLLlGQLEPSR-GLVKGGTKLEVAYFDQ--------YRDQL----DPEQTVMDNVGEGK-QEVMVRGRSRHIL----G 422
Cdd:TIGR00954 494 LFRIL-GELWPVYgGRLTKPAKGKLFYVPQrpymtlgtLRDQIiypdSSEDMKRRGLSDKDlEQILDNVQLTHILeregG 572
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1411607396 423 Y--LQDFLFEpkrartpvkaLSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVETLELLEELLADYPGTLLLVSH 495
Cdd:TIGR00954 573 WsaVQDWMDV----------LSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREFGITLFSVSH 637
SufC COG0396
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ...
11-211 4.59e-08

Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440165 [Multi-domain]  Cd Length: 245  Bit Score: 54.30  E-value: 4.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  11 LSFS--DFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAG--ELPLDDGRM-VQQQDLkvTRLE------------- 72
Cdd:COG0396     6 LHVSveGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGhpKYEVTSGSIlLDGEDI--LELSpderaragiflaf 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  73 QDPPASSDLTVFDytaeglagvgeLLKkyhhismeLAhdpsdanirIMSDLQEQLDYQngwQFETRISQVLTLLNLDPDA 152
Cdd:COG0396    84 QYPVEIPGVSVSN-----------FLR--------TA---------LNARRGEELSAR---EFLKLLKEKMKELGLDEDF 132
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1411607396 153 tLD-----SLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRG---AIVFISH 211
Cdd:COG0396   133 -LDryvneGFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSpdrGILIITH 198
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
14-216 4.83e-08

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: 53.87  E-value: 4.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  14 SDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMVQQQDLKVTRLEQDPPASSDLTVfDYTAEglag 93
Cdd:cd03290    12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSV-AYAAQ---- 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  94 vgellKKYhhismeLAHDPSDANIRIMSDLQEQldyqngwqfetRISQVLTLLNLDPDATL-------------DSLSGG 160
Cdd:cd03290    87 -----KPW------LLNATVEENITFGSPFNKQ-----------RYKAVTDACSLQPDIDLlpfgdqteigergINLSGG 144
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1411607396 161 WLRKVALARALACDPDLLLLDEPTNHLDIEAINWLE-----DFLKDFRGAIVFISHDREFI 216
Cdd:cd03290   145 QRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMqegilKFLQDDKRTLVLVTHKLQYL 205
SapD COG4170
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
19-223 4.95e-08

ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];


Pssm-ID: 443330 [Multi-domain]  Cd Length: 331  Bit Score: 55.30  E-value: 4.95e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  19 LDNAELSIERGERLCLVGRNGAGKSTLMKIIAGelplddgrmVQQQDLKVTrleqdppasSDLTVFDytaeglaGVgELL 98
Cdd:COG4170    23 VDRVSLTLNEGEIRGLVGESGSGKSLIAKAICG---------ITKDNWHVT---------ADRFRWN-------GI-DLL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  99 KKY---------HHISMeLAHDPS---DANIRIMSDLQEQLDYQNG----WQ-FETRISQVLTLLNL----DPDATLDS- 156
Cdd:COG4170    77 KLSprerrkiigREIAM-IFQEPSsclDPSAKIGDQLIEAIPSWTFkgkwWQrFKWRKKRAIELLHRvgikDHKDIMNSy 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1411607396 157 ---LSGGWLRKVALARALACDPDLLLLDEPTNHLdiEAINWLEDF-----LKDFRG-AIVFISHDREFIHKLATRI 223
Cdd:COG4170   156 pheLTEGECQKVMIAMAIANQPRLLIADEPTNAM--ESTTQAQIFrllarLNQLQGtSILLISHDLESISQWADTI 229
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
323-472 5.11e-08

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


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 53.64  E-value: 5.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 323 EGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEP---SRGLVkggtklevaYFDQYR-DQLDPEQ 398
Cdd:COG4136     5 ENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEV---------LLNGRRlTALPAEQ 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 399 ----------------TVMDNVGEGKQEVMVRG-RSRHILGYLQDFLFEPKRARTPvKALSGGEKNRL-LLAKLFLKPSN 460
Cdd:COG4136    76 rrigilfqddllfphlSVGENLAFALPPTIGRAqRRARVEQALEEAGLAGFADRDP-ATLSGGQRARVaLLRALLAEPRA 154
                         170
                  ....*....|..
gi 1411607396 461 LLiLDEPTNDLD 472
Cdd:COG4136   155 LL-LDEPFSKLD 165
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
332-472 5.52e-08

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


Pssm-ID: 440718 [Multi-domain]  Cd Length: 264  Bit Score: 54.32  E-value: 5.52e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 332 RTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTklEVAYFDQYR----------DQLD---PE 397
Cdd:COG1101    19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILiDGK--DVTKLPEYKrakyigrvfqDPMMgtaPS 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 398 QTVMDNV----GEGKQevmvRGRSRHILGYLQDFLFE---------PKRARTPVKALSGGEknR----LLLAKLflKPSN 460
Cdd:COG1101    97 MTIEENLalayRRGKR----RGLRRGLTKKRRELFREllatlglglENRLDTKVGLLSGGQ--RqalsLLMATL--TKPK 168
                         170
                  ....*....|..
gi 1411607396 461 LLILDEPTNDLD 472
Cdd:COG1101   169 LLLLDEHTAALD 180
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
19-203 6.48e-08

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 54.50  E-value: 6.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  19 LDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGR-----MVQQQDLKVTRLEQDPPASSDLTVFDYTAEGLAG 93
Cdd:PRK15056   23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKisilgQPTRQALQKNLVAYVPQSEEVDWSFPVLVEDVVM 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  94 VGellkKYHHisMELAHDPSDANIRIMSDLQEQLDYQngwqfETRISQVltllnldpdatlDSLSGGWLRKVALARALAC 173
Cdd:PRK15056  103 MG----RYGH--MGWLRRAKKRDRQIVTAALARVDMV-----EFRHRQI------------GELSGGQKKRVFLARAIAQ 159
                         170       180       190
                  ....*....|....*....|....*....|
gi 1411607396 174 DPDLLLLDEPTNHLDIEAINWLEDFLKDFR 203
Cdd:PRK15056  160 QGQVILLDEPFTGVDVKTEARIISLLRELR 189
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
319-496 6.49e-08

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 53.94  E-value: 6.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 319 VFETEGLGLDfGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKGGTKLE-------------VA 385
Cdd:PRK10418    4 QIELRNIALQ-AAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGVRQTAGRVLLDgkpvapcalrgrkIA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 386 YFDQY-RDQLDPEQTVMDNVGEGKQEVMVRGRSRHILGYLQDF-LFEPKRA--RTPVKaLSGGEKNRLLLAKLFLKPSNL 461
Cdd:PRK10418   83 TIMQNpRSAFNPLHTMHTHARETCLALGKPADDATLTAALEAVgLENAARVlkLYPFE-MSGGMLQRMMIALALLCEAPF 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1411607396 462 LILDEPTNDLDVETLELLEELLADY-----PGtLLLVSHD 496
Cdd:PRK10418  162 IIADEPTTDLDVVAQARILDLLESIvqkraLG-MLLVTHD 200
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
3-229 7.06e-08

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 54.16  E-value: 7.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   3 LLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDG----RMVQQQDLKVTRL------- 71
Cdd:PRK11701    6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGevhyRMRDGQLRDLYALseaerrr 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  72 ---------EQDPpassdltvfdytAEGL-------AGVGEllkkyhhismelahdpsdaniRIMSdlqeqldyqNGWQF 135
Cdd:PRK11701   86 llrtewgfvHQHP------------RDGLrmqvsagGNIGE---------------------RLMA---------VGARH 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 136 ETRI----SQVLTLLNLDPDATLD---SLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLK----DFRG 204
Cdd:PRK11701  124 YGDIrataGDWLERVEIDAARIDDlptTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRglvrELGL 203
                         250       260
                  ....*....|....*....|....*
gi 1411607396 205 AIVFISHDREFIHKLATRIIDLDRG 229
Cdd:PRK11701  204 AVVIVTHDLAVARLLAHRLLVMKQG 228
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
318-472 7.84e-08

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 53.97  E-value: 7.84e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 318 LVFETEGLGLDFGDRT-LFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTKLEVAYFDQYRDQL- 394
Cdd:PRK13647    3 NIIEVEDLHFRYKDGTkALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKvMGREVNAENEKWVRSKVg 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 395 ----DPEQ-----TVMD-------NVGEGKQEVMVRGRSRHILGYLQDFlfepkRARTPVKaLSGGEKNRLLLAKLFLKP 458
Cdd:PRK13647   83 lvfqDPDDqvfssTVWDdvafgpvNMGLDKDEVERRVEEALKAVRMWDF-----RDKPPYH-LSYGQKKRVAIAGVLAMD 156
                         170
                  ....*....|....
gi 1411607396 459 SNLLILDEPTNDLD 472
Cdd:PRK13647  157 PDVIVLDEPMAYLD 170
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
11-189 8.49e-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: 54.09  E-value: 8.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  11 LSFSDF-----PLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMVQQqdlkvTRLEQDPPASSDL--TV 83
Cdd:cd03291    40 LFFSNLclvgaPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHS-----GRISFSSQFSWIMpgTI 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  84 FDYTAEGLAgvgelLKKYHHISMELAhdpsdanirimSDLQEQLDyqngwQFETRISQVLTLLNLdpdatldSLSGGWLR 163
Cdd:cd03291   115 KENIIFGVS-----YDEYRYKSVVKA-----------CQLEEDIT-----KFPEKDNTVLGEGGI-------TLSGGQRA 166
                         170       180
                  ....*....|....*....|....*.
gi 1411607396 164 KVALARALACDPDLLLLDEPTNHLDI 189
Cdd:cd03291   167 RISLARAVYKDADLYLLDSPFGYLDV 192
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
321-374 9.69e-08

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 53.62  E-value: 9.69e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1411607396 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRG 374
Cdd:PRK11831    9 DMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHG 62
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
157-231 1.06e-07

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 54.09  E-value: 1.06e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1411607396 157 LSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFR--GAIVF-ISHDREFIHKLATRIIDLDRGVI 231
Cdd:PRK13631  177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKanNKTVFvITHTMEHVLEVADEVIVMDKGKI 254
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
18-188 1.11e-07

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


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 55.05  E-value: 1.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  18 LLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELP---------LDDGRMVQQQDLKV--TRLEQDppassDLTVFDY 86
Cdd:TIGR00955  40 LLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPkgvkgsgsvLLNGMPIDAKEMRAisAYVQQD-----DLFIPTL 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  87 TAEglagvgELLKKYHHISMElahdpsdaniRIMSDLQEQLdyqngwqfetRISQVLTLLNLDPDA--------TLDSLS 158
Cdd:TIGR00955 115 TVR------EHLMFQAHLRMP----------RRVTKKEKRE----------RVDEVLQALGLRKCAntrigvpgRVKGLS 168
                         170       180       190
                  ....*....|....*....|....*....|
gi 1411607396 159 GGWLRKVALARALACDPDLLLLDEPTNHLD 188
Cdd:TIGR00955 169 GGERKRLAFASELLTDPPLLFCDEPTSGLD 198
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
1-212 1.18e-07

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 53.96  E-value: 1.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   1 MALLTLHGACLSFS----DFPLLDNAELSIERGERLCLVGRNGAGKS----TLMKIIA-----GELPLDDGRMV---QQQ 64
Cdd:PRK09473   10 DALLDVKDLRVTFStpdgDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAangriGGSATFNGREIlnlPEK 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  65 DLKVTRLE------QDPPASsdLTVFDYTAEGLAgvgELLKKYHHISMELAHDPSdanIRImsdlqeqLDyqngwqfETR 138
Cdd:PRK09473   90 ELNKLRAEqismifQDPMTS--LNPYMRVGEQLM---EVLMLHKGMSKAEAFEES---VRM-------LD-------AVK 147
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1411607396 139 ISQVLTLLNLDPDatldSLSGGWLRKVALARALACDPDLLLLDEPTNHLDI----EAINWLEDFLKDFRGAIVFISHD 212
Cdd:PRK09473  148 MPEARKRMKMYPH----EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVtvqaQIMTLLNELKREFNTAIIMITHD 221
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
28-224 1.21e-07

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: 51.22  E-value: 1.21e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   28 RGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMVqqqdlkvtrleqdppassdltvfdytaeglagvgellkkyhhisme 107
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVI---------------------------------------------- 34
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  108 lAHDPSDANIRIMSDLQEQLDYQNGWQFEtRISQVltllnldpdatldslsggwlrKVALARALACDPDLLLLDEPTNHL 187
Cdd:smart00382  35 -YIDGEDILEEVLDQLLLIIVGGKKASGS-GELRL---------------------RLALALARKLKPDVLILDEITSLL 91
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1411607396  188 DIEA---------INWLEDFLKDFRGAIVFISHDREFIHKLATRII 224
Cdd:smart00382  92 DAEQeallllleeLRLLLLLKSEKNLTVILTTNDEKDLGPALLRRR 137
GguA NF040905
sugar ABC transporter ATP-binding protein;
19-223 1.21e-07

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 54.80  E-value: 1.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  19 LDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELP--------LDDGRMVQQQDLKvtrleqdppassdltvfDYTAEG 90
Cdd:NF040905   17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPhgsyegeiLFDGEVCRFKDIR-----------------DSEALG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  91 LAgvgellkkyhHISMELAHDP--SDA-NIRIMSdlqEQLdyQNG---WQfETRISQVLTL----LNLDPDATLDSLSGG 160
Cdd:NF040905   80 IV----------IIHQELALIPylSIAeNIFLGN---ERA--KRGvidWN-ETNRRARELLakvgLDESPDTLVTDIGVG 143
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1411607396 161 WLRKVALARALACDPDLLLLDEPT---NHLDIEAinwLEDFLKDFRG---AIVFISHDREFIHKLATRI 223
Cdd:NF040905  144 KQQLVEIAKALSKDVKLLILDEPTaalNEEDSAA---LLDLLLELKAqgiTSIIISHKLNEIRRVADSI 209
cbiO PRK13643
energy-coupling factor transporter ATPase;
13-233 1.47e-07

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 53.58  E-value: 1.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  13 FSDFPLLDnAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGrMVQQQDLKVT----RLEQDPPASSDLTVFDYTA 88
Cdd:PRK13643   17 FASRALFD-IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEG-KVTVGDIVVSstskQKEIKPVRKKVGVVFQFPE 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  89 EGLagVGELLKKyhhismELAHDPSdaNIRIMSDLQEQLdyqngwqfetrISQVLTLLNLDPDATLDS---LSGGWLRKV 165
Cdd:PRK13643   95 SQL--FEETVLK------DVAFGPQ--NFGIPKEKAEKI-----------AAEKLEMVGLADEFWEKSpfeLSGGQMRRV 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1411607396 166 ALARALACDPDLLLLDEPTNHLD----IEAINWLEDFLKDFRgAIVFISHDREFIHKLATRIIDLDRGVITS 233
Cdd:PRK13643  154 AIAGILAMEPEVLVLDEPTAGLDpkarIEMMQLFESIHQSGQ-TVVLVTHLMDDVADYADYVYLLEKGHIIS 224
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
321-475 1.71e-07

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: 52.58  E-value: 1.71e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 321 ETEGLGLDFGDR----TLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTKL------------- 382
Cdd:cd03258     3 ELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLvDGTDLtllsgkelrkarr 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 383 EVAY-FDQYrdQLDPEQTVMDNV-------GEGKQEvmVRGRSRHILgylqDFL-FEPKRARTPvKALSGGEKNRLLLAK 453
Cdd:cd03258    83 RIGMiFQHF--NLLSSRTVFENValpleiaGVPKAE--IEERVLELL----ELVgLEDKADAYP-AQLSGGQKQRVGIAR 153
                         170       180
                  ....*....|....*....|...
gi 1411607396 454 -LFLKPSnLLILDEPTNDLDVET 475
Cdd:cd03258   154 aLANNPK-VLLCDEATSALDPET 175
cbiO PRK13642
energy-coupling factor transporter ATPase;
319-496 1.75e-07

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 53.17  E-value: 1.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 319 VFETEGLGLDF---GDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTKLEVAYFDQYRDQL 394
Cdd:PRK13642    4 ILEVENLVFKYekeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKiDGELLTAENVWNLRRKI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 395 -----DPEQ-----TVMDNVGEGKQ------EVMVRGRSRHILGY-LQDFlfepkRARTPVKaLSGGEKNRLLLAKLFLK 457
Cdd:PRK13642   84 gmvfqNPDNqfvgaTVEDDVAFGMEnqgiprEEMIKRVDEALLAVnMLDF-----KTREPAR-LSGGQKQRVAVAGIIAL 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1411607396 458 PSNLLILDEPTNDLD----VETLELLEELLADYPGTLLLVSHD 496
Cdd:PRK13642  158 RPEIIILDESTSMLDptgrQEIMRVIHEIKEKYQLTVLSITHD 200
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
156-267 1.96e-07

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 54.20  E-value: 1.96e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 156 SLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAinwlEDFLKDfrgAIVFISHDR-EFI--HKLAT-----RIIDLD 227
Cdd:PRK13657  471 QLSGGERQRLAIARALLKDPPILILDEATSALDVET----EAKVKA---ALDELMKGRtTFIiaHRLSTvrnadRILVFD 543
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1411607396 228 RG-VITSwpGNYDEYLQGKEealRVEELQHAEFdrkLAQEE 267
Cdd:PRK13657  544 NGrVVES--GSFDELVARGG---RFAALLRAQG---MLQED 576
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
157-231 2.09e-07

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 53.17  E-value: 2.09e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1411607396 157 LSGGWLRKVALARALACDPDLLLLDEPTNHLD----IEAINWLEDFLKDFRgAIVFISHDREFIHKLATRIIDLDRGVI 231
Cdd:PRK13651  166 LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDpqgvKEILEIFDNLNKQGK-TIILVTHDLDNVLEWTKRTIFFKDGKI 243
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
332-475 2.36e-07

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


Pssm-ID: 213219 [Multi-domain]  Cd Length: 237  Bit Score: 52.10  E-value: 2.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 332 RTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRG-LVKGGTKLEVAYFDQYRDQLDP--------EQTVMD 402
Cdd:cd03252    15 PVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGrVLVDGHDLALADPAWLRRQVGVvlqenvlfNRSIRD 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 403 NVGEGKqEVMVRGRSRHI--LGYLQDFLFE-PKRARTPV----KALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVET 475
Cdd:cd03252    95 NIALAD-PGMSMERVIEAakLAGAHDFISElPEGYDTIVgeqgAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYES 173
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
337-473 2.52e-07

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 53.17  E-value: 2.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 337 GLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKG-GTKLEVAYFDQYRD--------------QLDPEQTVM 401
Cdd:PRK15079   39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWlGKDLLGMKDDEWRAvrsdiqmifqdplaSLNPRMTIG 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 402 DNVGE---------GKQEVMVRGRSRHI-LGYLQDFLfepkrARTPvKALSGGEKNRLLLAK-LFLKPsNLLILDEPTND 470
Cdd:PRK15079  119 EIIAEplrtyhpklSRQEVKDRVKAMMLkVGLLPNLI-----NRYP-HEFSGGQCQRIGIARaLILEP-KLIICDEPVSA 191

                  ...
gi 1411607396 471 LDV 473
Cdd:PRK15079  192 LDV 194
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
12-190 2.78e-07

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 53.57  E-value: 2.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  12 SFS-----DFPLLDNAELSIERGERLCLVGRNGAGKSTLMKII-------AGELPLDDGRMVQQQ----DLKVTRLEQDP 75
Cdd:TIGR00958 485 SFSypnrpDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLqnlyqptGGQVLLDGVPLVQYDhhylHRQVALVGQEP 564
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  76 PASSDlTVFDYTAEGLAgvgellkkyhhismelahDPSDANIRIMSDLQEQLDYqngwqfetrISQVLTLLNLDPDATLD 155
Cdd:TIGR00958 565 VLFSG-SVRENIAYGLT------------------DTPDEEIMAAAKAANAHDF---------IMEFPNGYDTEVGEKGS 616
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1411607396 156 SLSGGWLRKVALARALACDPDLLLLDEPTNHLDIE 190
Cdd:TIGR00958 617 QLSGGQKQRIAIARALVRKPRVLILDEATSALDAE 651
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
315-472 2.87e-07

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: 51.49  E-value: 2.87e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 315 SGKLVFETEGLGLDfgDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLE----PSRGLVKGG---------TK 381
Cdd:cd03233     5 SWRNISFTTGKGRS--KIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEgnvsVEGDIHYNGipykefaekYP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 382 LEVAYFDQyRDQLDPEQTV---MDNVGEGKQEVMVRGrsrhilgylqdflfepkrartpvkaLSGGEKNRLLLAKLFLKP 458
Cdd:cd03233    83 GEIIYVSE-EDVHFPTLTVretLDFALRCKGNEFVRG-------------------------ISGGERKRVSIAEALVSR 136
                         170
                  ....*....|....
gi 1411607396 459 SNLLILDEPTNDLD 472
Cdd:cd03233   137 ASVLCWDNSTRGLD 150
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
349-501 3.10e-07

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


Pssm-ID: 213207 [Multi-domain]  Cd Length: 204  Bit Score: 51.45  E-value: 3.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 349 ALVGPNGCGKSTLIKLLL----GQLEPSRGLVKGGTKL-----EVAYFD-QYRDQLDPEQTVMDNVGEGKQEVMVRGrsr 418
Cdd:cd03240    26 LIVGQNGAGKTTIIEALKyaltGELPPNSKGGAHDPKLiregeVRAQVKlAFENANGKKYTITRSLAILENVIFCHQ--- 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 419 hilGYLQDFLFEPkrartpVKALSGGEKN------RLLLAKLFLKPSNLLILDEPTNDLDVETLELL-----EELLADYP 487
Cdd:cd03240   103 ---GESNWPLLDM------RGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEESlaeiiEERKSQKN 173
                         170
                  ....*....|....
gi 1411607396 488 GTLLLVSHDRRFID 501
Cdd:cd03240   174 FQLIVITHDEELVD 187
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
1-188 3.26e-07

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


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 52.92  E-value: 3.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   1 MALLTLHGACLSFS-DFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAG-------ELPLDDGRmvqqqdlkVTRLE 72
Cdd:PRK11650    1 MAGLKLQAVRKSYDgKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGleritsgEIWIGGRV--------VNELE 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  73 qdpPASSD-------------LTVFDYTAEGL--AGVGEllkkyHHIsmelahdpsdanirimsdlqeqldyqngwqfET 137
Cdd:PRK11650   73 ---PADRDiamvfqnyalyphMSVRENMAYGLkiRGMPK-----AEI-------------------------------EE 113
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1411607396 138 RISQVLTLLNLDPdaTLD----SLSGGWLRKVALARALACDPDLLLLDEPTNHLD 188
Cdd:PRK11650  114 RVAEAARILELEP--LLDrkprELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
19-468 3.56e-07

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 53.59  E-value: 3.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  19 LDNAELSIERGERLCLVGRNGAGKSTLMKIIAGElplddgRMVQQqdlkvtrleqdppasSDLTVFD------------- 85
Cdd:NF033858   17 LDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGA------RKIQQ---------------GRVEVLGgdmadarhrravc 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  86 ----YTAEGLagvGELLkkYHHISMElahdpsdanirimsdlqEQLDY------QNGWQFETRISQVLTLLNLDP--DAT 153
Cdd:NF033858   76 priaYMPQGL---GKNL--YPTLSVF-----------------ENLDFfgrlfgQDAAERRRRIDELLRATGLAPfaDRP 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 154 LDSLSGGWLRKVALARALACDPDLLLLDEPTNHLD----------IEAInwledflkdfRGA------IVfishdrefih 217
Cdd:NF033858  134 AGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDplsrrqfwelIDRI----------RAErpgmsvLV---------- 193
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 218 klATriidldrgvitswpgnydEYLqgkEEALRveelqhaeFDRKLAQeevwvrqgikarrtrNEGRVRALEAMR--MER 295
Cdd:NF033858  194 --AT------------------AYM---EEAER--------FDWLVAM---------------DAGRVLATGTPAelLAR 227
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 296 SQRREL-------------QGKAKLQMD--DVNRSGKLVFETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKST 360
Cdd:NF033858  228 TGADTLeaafiallpeekrRGHQPVVIPprPADDDDEPAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKST 307
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 361 LIKLLLGQLEPSRG-------LVKGG---TKLEVAYFDQ----YRdqldpEQTVMDN---------VGEGKQEVMVRgrs 417
Cdd:NF033858  308 TMKMLTGLLPASEGeawlfgqPVDAGdiaTRRRVGYMSQafslYG-----ELTVRQNlelharlfhLPAAEIAARVA--- 379
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1411607396 418 rhilGYLQDFLFEPKRARTPvKALSGGEKNRLLLAKLFL-KPSnLLILDEPT 468
Cdd:NF033858  380 ----EMLERFDLADVADALP-DSLPLGIRQRLSLAVAVIhKPE-LLILDEPT 425
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
319-471 3.68e-07

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 53.01  E-value: 3.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 319 VFETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGqLEPSrGLVKG-----GTKLEvayFDQYRDQ 393
Cdd:PRK13549    5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPH-GTYEGeiifeGEELQ---ASNIRDT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 394 -------------LDPEQTVMDNVGEGkQEVMVRGRSRHILGYL--QDFLFEPKRA---RTPVKALSGGEKNRLLLAKLF 455
Cdd:PRK13549   80 eragiaiihqelaLVKELSVLENIFLG-NEITPGGIMDYDAMYLraQKLLAQLKLDinpATPVGNLGLGQQQLVEIAKAL 158
                         170
                  ....*....|....*.
gi 1411607396 456 LKPSNLLILDEPTNDL 471
Cdd:PRK13549  159 NKQARLLILDEPTASL 174
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
349-472 3.93e-07

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: 52.42  E-value: 3.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 349 ALVGPNGCGKSTLIKLLLGQLEPSRG-LVKGGT--------------KLEVAY-FDQYRdqLDPEQTVMDNVGEGKQEVM 412
Cdd:TIGR02142  27 AIFGRSGSGKTTLIRLIAGLTRPDEGeIVLNGRtlfdsrkgiflppeKRRIGYvFQEAR--LFPHLSVRGNLRYGMKRAR 104
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 413 VRGRSRHILGYLQDFLFEPKRARTPVKaLSGGEKNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:TIGR02142 105 PSERRISFERVIELLGIGHLLGRLPGR-LSGGEKQRVAIGRALLSSPRLLLMDEPLAALD 163
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
1-184 4.16e-07

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


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 51.42  E-value: 4.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   1 MALLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMV-------QQQDLKVTRleq 73
Cdd:PRK11614    3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVfdgkditDWQTAKIMR--- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  74 dppassdltvfdytaEGLAGVGELLKKYHHISMElahdpsdANIRIMSDLQEQLDYQngwqfeTRISQVLTL---LNLDP 150
Cdd:PRK11614   80 ---------------EAVAIVPEGRRVFSRMTVE-------ENLAMGGFFAERDQFQ------ERIKWVYELfprLHERR 131
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1411607396 151 DATLDSLSGGWLRKVALARALACDPDLLLLDEPT 184
Cdd:PRK11614  132 IQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPS 165
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
19-191 4.21e-07

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: 52.90  E-value: 4.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  19 LDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPlddGRMVQQQDLKVTRLEQDPPASSdltvfdyTAEGLAGVGELL 98
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYP---GKFEGNVFINGKPVDIRNPAQA-------IRAGIAMVPEDR 345
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  99 KKYHHIS-MELAHDPSDANIRIMSDLQeQLDYQNGWQFETRISQVLTLLNLDPDATLDSLSGGWLRKVALARALACDPDL 177
Cdd:TIGR02633 346 KRHGIVPiLGVGKNITLSVLKSFCFKM-RIDAAAELQIIGSAIQRLKVKTASPFLPIGRLSGGNQQKAVLAKMLLTNPRV 424
                         170
                  ....*....|....
gi 1411607396 178 LLLDEPTNHLDIEA 191
Cdd:TIGR02633 425 LILDEPTRGVDVGA 438
ycf16 CHL00131
sulfate ABC transporter protein; Validated
317-474 4.22e-07

sulfate ABC transporter protein; Validated


Pssm-ID: 214372 [Multi-domain]  Cd Length: 252  Bit Score: 51.57  E-value: 4.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 317 KLVFETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQlePSRGLVKGgtklEVAYFDQYRDQLDP 396
Cdd:CHL00131    5 KPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGH--PAYKILEG----DILFKGESILDLEP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 397 EQTVMDNVGEGKQ-EVMVRGRSRhilgylQDFL---------FEPKRARTPVKAL------------------------- 441
Cdd:CHL00131   79 EERAHLGIFLAFQyPIEIPGVSN------ADFLrlaynskrkFQGLPELDPLEFLeiineklklvgmdpsflsrnvnegf 152
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1411607396 442 SGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVE 474
Cdd:CHL00131  153 SGGEKKRNEILQMALLDSELAILDETDSGLDID 185
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
136-231 4.40e-07

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 51.94  E-value: 4.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 136 ETRISQVLTLLNLDPDATLDS---LSGGWLRKVALARALACDPDLLLLDEPTNHLD----IEAINWLEDFLKDFRGAIVF 208
Cdd:PRK13634  122 KQKAREMIELVGLPEELLARSpfeLSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDpkgrKEMMEMFYKLHKEKGLTTVL 201
                          90       100
                  ....*....|....*....|...
gi 1411607396 209 ISHDREFIHKLATRIIDLDRGVI 231
Cdd:PRK13634  202 VTHSMEDAARYADQIVVMHKGTV 224
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
15-243 5.17e-07

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: 51.08  E-value: 5.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  15 DFPLLDNAELSIERGERLCLVGRNGAGKSTLMKII-------AGELPLD--DGRMVQQQDL--KVTRLEQDPPASSDlTV 83
Cdd:cd03253    13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLfrfydvsSGSILIDgqDIREVTLDSLrrAIGVVPQDTVLFND-TI 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  84 FDYTAEGLAGVGEllkkyhhISMELAHDPSDANIRIMSdLQEQLDYQNGwqfETRIsqvltllnldpdatldSLSGGWLR 163
Cdd:cd03253    92 GYNIRYGRPDATD-------EEVIEAAKAAQIHDKIMR-FPDGYDTIVG---ERGL----------------KLSGGEKQ 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 164 KVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRG--AIVFISHD-REFIHklATRIIDLDRGVITSwPGNYDE 240
Cdd:cd03253   145 RVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKgrTTIVIAHRlSTIVN--ADKIIVLKDGRIVE-RGTHEE 221

                  ...
gi 1411607396 241 YLQ 243
Cdd:cd03253   222 LLA 224
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
321-512 6.00e-07

methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]


Pssm-ID: 132313 [Multi-domain]  Cd Length: 520  Bit Score: 52.50  E-value: 6.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLG--QLEPSRGLV---------------------- 376
Cdd:TIGR03269   2 EVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIiyhvalcekcgyverpskvgep 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 377 --KGGTKLE--------------------VAYFDQYRDQLDPEQTVMDNVGEGKQEVMVRGRSRhiLGYLQDFLFEPK-- 432
Cdd:TIGR03269  82 cpVCGGTLEpeevdfwnlsdklrrrirkrIAIMLQRTFALYGDDTVLDNVLEALEEIGYEGKEA--VGRAVDLIEMVQls 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 433 -RARTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVETL----ELLEELLADYPGTLLLVSHDRRFIDNTVT-G 506
Cdd:TIGR03269 160 hRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAklvhNALEEAVKASGISMVLTSHWPEVIEDLSDkA 239

                  ....*.
gi 1411607396 507 CWLFEG 512
Cdd:TIGR03269 240 IWLENG 245
PLN03232 PLN03232
ABC transporter C family member; Provisional
338-472 6.02e-07

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 53.06  E-value: 6.02e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  338 LDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSR--GLVKGGTkleVAYFDQYRDQLDpeQTVMDNVGEG-KQEVMVR 414
Cdd:PLN03232   636 INLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAEtsSVVIRGS---VAYVPQVSWIFN--ATVRENILFGsDFESERY 710
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1411607396  415 GRSRHILGYLQDFLFEPKRARTPVKA----LSGGEKNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:PLN03232   711 WRAIDVTALQHDLDLLPGRDLTEIGErgvnISGGQKQRVSMARAVYSNSDIYIFDDPLSALD 772
sufC TIGR01978
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ...
330-501 6.40e-07

FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 273907 [Multi-domain]  Cd Length: 243  Bit Score: 51.11  E-value: 6.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 330 GDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQlePSRGLVKGgtklEVAYFDQYRDQLDPEQtvmdnvgegkq 409
Cdd:TIGR01978  11 EDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGH--PSYEVTSG----TILFKGQDLLELEPDE----------- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 410 evmvRGRSRHILGY----------LQDFLFEPKRAR------TPVKAL----------------------------SGGE 445
Cdd:TIGR01978  74 ----RARAGLFLAFqypeeipgvsNLEFLRSALNARrsargeEPLDLLdfekllkeklalldmdeeflnrsvnegfSGGE 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 446 KNRL-LLAKLFLKPsNLLILDEPTNDLDVETLELLEELLADY--PGT-LLLVSHDRRFID 501
Cdd:TIGR01978 150 KKRNeILQMALLEP-KLAILDEIDSGLDIDALKIVAEGINRLrePDRsFLIITHYQRLLN 208
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
344-475 6.92e-07

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 50.58  E-value: 6.92e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 344 RGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLV--KGGT--KLEVAYFDQYRDQ----------LDPEQTVMDNVGE--- 406
Cdd:PRK11629   34 EGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVifNGQPmsKLSSAAKAELRNQklgfiyqfhhLLPDFTALENVAMpll 113
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1411607396 407 --GKQEVMVRGRSRHILGYLQdflfEPKRARTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVET 475
Cdd:PRK11629  114 igKKKPAEINSRALEMLAAVG----LEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARN 180
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
17-228 7.58e-07

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: 50.57  E-value: 7.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  17 PLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGR-MVQQQDLKVTRLE----------QDPpassdlTVFD 85
Cdd:cd03244    18 PVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSiLIDGVDISKIGLHdlrsrisiipQDP------VLFS 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  86 YTaeglagvgellkkyhhISMELahDP----SDAnirimsDLQEQLDYQNGWQFetrISQVLTLLNLDPDATLDSLSGGW 161
Cdd:cd03244    92 GT----------------IRSNL--DPfgeySDE------ELWQALERVGLKEF---VESLPGGLDTVVEEGGENLSVGQ 144
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1411607396 162 LRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKD-FRGAIVF-IShdrefiHKLATrIIDLDR 228
Cdd:cd03244   145 RQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIREaFKDCTVLtIA------HRLDT-IIDSDR 206
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
19-246 8.10e-07

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 51.00  E-value: 8.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  19 LDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMvqqqdlkvtrLEQDPPassdltvFDYTAEGL----AGV 94
Cdd:PRK13636   22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRI----------LFDGKP-------IDYSRKGLmklrESV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  95 GELLKKYHH--ISMELAHDPS--DANIRIMSDlqeqldyqngwQFETRISQVLTLLNLDP--DATLDSLSGGWLRKVALA 168
Cdd:PRK13636   85 GMVFQDPDNqlFSASVYQDVSfgAVNLKLPED-----------EVRKRVDNALKRTGIEHlkDKPTHCLSFGQKKRVAIA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 169 RALACDPDLLLLDEPTNHLD----IEAINWLEDFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVITsWPGNYDEYLQG 244
Cdd:PRK13636  154 GVLVMEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVI-LQGNPKEVFAE 232

                  ..
gi 1411607396 245 KE 246
Cdd:PRK13636  233 KE 234
YbjD COG3593
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ...
23-219 8.44e-07

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: 51.54  E-value: 8.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  23 ELSIERGERL-CLVGRNGAGKSTLMKIIAGELPLDDGRMVQQQDLKVTRLEQDPPASSDLTvFDYTAEGLAGVGELLKKY 101
Cdd:COG3593    16 DLSIELSDDLtVLVGENNSGKSSILEALRLLLGPSSSRKFDEEDFYLGDDPDLPEIEIELT-FGSLLSRLLRLLLKEEDK 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 102 HHISMELAHDPSDANIRImSDLQEQLD-YQNGWQFETRIS---------QVLTLLNL----DPDATLDSLSGG--WLRKV 165
Cdd:COG3593    95 EELEEALEELNEELKEAL-KALNELLSeYLKELLDGLDLElelsldeleDLLKSLSLriedGKELPLDRLGSGfqRLILL 173
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1411607396 166 ALARALA-----CDPDLLLLDEPTNHLDIEAINWLEDFLKDF--RGAIVFIS-HDREFIHKL 219
Cdd:COG3593   174 ALLSALAelkraPANPILLIEEPEAHLHPQAQRRLLKLLKELseKPNQVIITtHSPHLLSEV 235
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
340-475 9.10e-07

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 50.65  E-value: 9.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 340 LQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLV--------KGGTKLEVAYFDQyRDQLDPEQTVMdnvgegKQEV 411
Cdd:PRK15056   28 FTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKIsilgqptrQALQKNLVAYVPQ-SEEVDWSFPVL------VEDV 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 412 MVRGRSRHiLGYLQdflfEPK-RARTPVKA-----------------LSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDV 473
Cdd:PRK15056  101 VMMGRYGH-MGWLR----RAKkRDRQIVTAalarvdmvefrhrqigeLSGGQKKRVFLARAIAQQGQVILLDEPFTGVDV 175

                  ..
gi 1411607396 474 ET 475
Cdd:PRK15056  176 KT 177
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
319-472 9.53e-07

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 50.55  E-value: 9.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 319 VFETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLL--LGQLEPSrGLVKGgtklEVAYFDQ--YRDQL 394
Cdd:PRK14243   10 VLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrLNDLIPG-FRVEG----KVTFHGKnlYAPDV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 395 DP-----------------EQTVMDNVGEGKQevmvrgrsrhILGYLQDF--LFEP--KRA----------RTPVKALSG 443
Cdd:PRK14243   85 DPvevrrrigmvfqkpnpfPKSIYDNIAYGAR----------INGYKGDMdeLVERslRQAalwdevkdklKQSGLSLSG 154
                         170       180
                  ....*....|....*....|....*....
gi 1411607396 444 GEKNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:PRK14243  155 GQQQRLCIARAIAVQPEVILMDEPCSALD 183
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
19-231 1.02e-06

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 50.85  E-value: 1.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  19 LDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGR-MVQQQDLK------------VTRLEQDPpassDLTVFD 85
Cdd:PRK13639   18 LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEvLIKGEPIKydkksllevrktVGIVFQNP----DDQLFA 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  86 YTAEGLAGVGELlkkyhhiSMELAHDpsdanirimsdlqeqldyqngwQFETRISQVLTLLNLD--PDATLDSLSGGWLR 163
Cdd:PRK13639   94 PTVEEDVAFGPL-------NLGLSKE----------------------EVEKRVKEALKAVGMEgfENKPPHHLSGGQKK 144
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1411607396 164 KVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDF--RGAIVFIS-HDREFIHKLATRIIDLDRGVI 231
Cdd:PRK13639  145 RVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLnkEGITIIIStHDVDLVPVYADKVYVMSDGKI 215
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
344-513 1.14e-06

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: 49.11  E-value: 1.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 344 RGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKgGTKLEVAYFDQYRDqldpeqtvmdnvgegkqevmvrgrsrhilgy 423
Cdd:cd03222    24 EGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDE-WDGITPVYKPQYID------------------------------- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 424 lqdflfepkrartpvkaLSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVETLELLEELLADY----PGTLLLVSHDRRF 499
Cdd:cd03222    72 -----------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLseegKKTALVVEHDLAV 134
                         170
                  ....*....|....
gi 1411607396 500 IDNTVTGCWLFEGD 513
Cdd:cd03222   135 LDYLSDRIHVFEGE 148
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
338-472 1.31e-06

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 50.37  E-value: 1.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 338 LDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTKLEVAYFDQYRDQL-----DPEQ-----TVMDNVGE 406
Cdd:PRK13632   28 VSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKiDGITISKENLKEIRKKIgiifqNPDNqfigaTVEDDIAF 107
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1411607396 407 GKQEVMV-RGRSRHILGYL------QDFL-FEPKRartpvkaLSGGEKNRLLLAK-LFLKPSnLLILDEPTNDLD 472
Cdd:PRK13632  108 GLENKKVpPKKMKDIIDDLakkvgmEDYLdKEPQN-------LSGGQKQRVAIASvLALNPE-IIIFDESTSMLD 174
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
19-229 1.52e-06

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 49.49  E-value: 1.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  19 LDNAELSIERGERLCLVGRNGAGKSTLMKIIAG-ELPLDDGRMVQQQDlkVTRLE---------------QDPPASSDLT 82
Cdd:PRK10908   18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGiERPSAGKIWFSGHD--ITRLKnrevpflrrqigmifQDHHLLMDRT 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  83 VFDYTAEGLAGVGellkkyhhismelahdPSDANIRimsdlqeqldyqngwqfeTRISQVLTLLNLdpdatLD------- 155
Cdd:PRK10908   96 VYDNVAIPLIIAG----------------ASGDDIR------------------RRVSAALDKVGL-----LDkaknfpi 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 156 SLSGGWLRKVALARALACDPDLLLLDEPTNHLDiEAINwlEDFLKDFR-----GAIVFI-SHDREFIHKLATRIIDLDRG 229
Cdd:PRK10908  137 QLSGGEQQRVGIARAVVNKPAVLLADEPTGNLD-DALS--EGILRLFEefnrvGVTVLMaTHDIGLISRRSYRMLTLSDG 213
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
156-211 1.84e-06

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


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 49.65  E-value: 1.84e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1411607396 156 SLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRG--AIVFISH 211
Cdd:COG1117   154 GLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKdyTIVIVTH 211
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
3-236 2.14e-06

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 49.62  E-value: 2.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   3 LLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMVQQQDlkvtrleqdppassdlt 82
Cdd:PRK13638    1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGK----------------- 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  83 VFDYTAEGLAGVGELLKKyhhismeLAHDPsDANI---RIMSDLQEQLDYQNGWQFET--RISQVLTLLNLD--PDATLD 155
Cdd:PRK13638   64 PLDYSKRGLLALRQQVAT-------VFQDP-EQQIfytDIDSDIAFSLRNLGVPEAEItrRVDEALTLVDAQhfRHQPIQ 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 156 SLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRGA---IVFISHDREFIHKLATRIIDLDRGVIT 232
Cdd:PRK13638  136 CLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQgnhVIISSHDIDLIYEISDAVYVLRQGQIL 215

                  ....*.
gi 1411607396 233 SW--PG 236
Cdd:PRK13638  216 THgaPG 221
cbiO PRK13649
energy-coupling factor transporter ATPase;
17-232 2.18e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 49.74  E-value: 2.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  17 PLLDNAELSIERGERLCLVGRNGAGKSTLMKII-------AGELPLDDGRMVQQ---QDLKVTR----LEQDPPASS--D 80
Cdd:PRK13649   21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLnglhvptQGSVRVDDTLITSTsknKDIKQIRkkvgLVFQFPESQlfE 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  81 LTVFDYTAEGLAGVGellkkyhhISMELAHDPSDANIRIMSdLQEQLDYQNgwQFEtrisqvltllnldpdatldsLSGG 160
Cdd:PRK13649  101 ETVLKDVAFGPQNFG--------VSQEEAEALAREKLALVG-ISESLFEKN--PFE--------------------LSGG 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1411607396 161 WLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRGA---IVFISHDREFIHKLATRIIDLDRGVIT 232
Cdd:PRK13649  150 QMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSgmtIVLVTHLMDDVANYADFVYVLEKGKLV 224
cbiO PRK13644
energy-coupling factor transporter ATPase;
335-475 2.18e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 49.60  E-value: 2.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 335 FQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRG--LVKGGTKLEVAYFDQYRDQL-----DPE-----QTVMD 402
Cdd:PRK13644   18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGkvLVSGIDTGDFSKLQGIRKLVgivfqNPEtqfvgRTVEE 97
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1411607396 403 NVGEGKQE-----VMVRGRSRHILGYLQdflFEPKRARTPvKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVET 475
Cdd:PRK13644   98 DLAFGPENlclppIEIRKRVDRALAEIG---LEKYRHRSP-KTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDS 171
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
13-213 2.23e-06

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127 [Multi-domain]  Cd Length: 200  Bit Score: 48.79  E-value: 2.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  13 FSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRM-VQQQDLKvtrleqdppasSDLTVFDytaEGL 91
Cdd:PRK13540   11 YHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEIlFERQSIK-----------KDLCTYQ---KQL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  92 AGVGellkkyHHISMelahdpsDANIRIMSDLQEQLDYQNGwqfETRISQVLTLLNLDP--DATLDSLSGGWLRKVALAR 169
Cdd:PRK13540   77 CFVG------HRSGI-------NPYLTLRENCLYDIHFSPG---AVGITELCRLFSLEHliDYPCGLLSSGQKRQVALLR 140
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1411607396 170 ALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFR---GAIVFISHDR 213
Cdd:PRK13540  141 LWMSKAKLWLLDEPLVALDELSLLTIITKIQEHRakgGAVLLTSHQD 187
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
22-232 2.38e-06

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 50.29  E-value: 2.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  22 AELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGR-MVQQQDLKVTRLEQDPPASSDLTVFDYTAEG---LAGVGEL 97
Cdd:PRK11288  272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQvYLDGKPIDIRSPRDAIRAGIMLCPEDRKAEGiipVHSVADN 351
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  98 LkkyhHISMELAHDPSDANIRimsdlqeqldyqNGWQFETRISQVlTLLNL---DPDATLDSLSGGWLRKVALARALACD 174
Cdd:PRK11288  352 I----NISARRHHLRAGCLIN------------NRWEAENADRFI-RSLNIktpSREQLIMNLSGGNQQKAILGRWLSED 414
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1411607396 175 PDLLLLDEPTNHLDIEAINWLEDFLKDF--RG-AIVFISHDREFIHKLATRIIDLDRGVIT 232
Cdd:PRK11288  415 MKVILLDEPTRGIDVGAKHEIYNVIYELaaQGvAVLFVSSDLPEVLGVADRIVVMREGRIA 475
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
337-475 2.41e-06

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


Pssm-ID: 213269 [Multi-domain]  Cd Length: 207  Bit Score: 48.56  E-value: 2.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 337 GLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKggtklevayFDQYRDQLDPEQTVMDNVGEGKQE-VMVRG 415
Cdd:cd03369    26 NVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIE---------IDGIDISTIPLEDLRSSLTIIPQDpTLFSG 96
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1411607396 416 RSRHILG----YLQDFLFEPKRARTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVET 475
Cdd:cd03369    97 TIRSNLDpfdeYSDEEIYGALRVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYAT 160
PvdE COG4615
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...
24-237 2.93e-06

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


Pssm-ID: 443659 [Multi-domain]  Cd Length: 547  Bit Score: 50.18  E-value: 2.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  24 LSIERGERLCLVGRNGAGKSTLMKII-------AGELPLdDGRMVQQQDLkvtrleqdppAS---------SDLTVFD-- 85
Cdd:COG4615   353 LTIRRGELVFIVGGNGSGKSTLAKLLtglyrpeSGEILL-DGQPVTADNR----------EAyrqlfsavfSDFHLFDrl 421
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  86 YTAEGLAG---VGELLKKyhhisMELAHdpsdanirimsdlqeQLDYQNGwqfetRISqvltllnldpdaTLDsLSGGWL 162
Cdd:COG4615   422 LGLDGEADparARELLER-----LELDH---------------KVSVEDG-----RFS------------TTD-LSQGQR 463
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 163 RKVALARALACDPDLLLLDEptnhldieainWLED--------F-------LKDfRG-AIVFISHDREFIHkLATRIIDL 226
Cdd:COG4615   464 KRLALLVALLEDRPILVFDE-----------WAADqdpefrrvFytellpeLKA-RGkTVIAISHDDRYFD-LADRVLKM 530
                         250
                  ....*....|.
gi 1411607396 227 DRGVITSWPGN 237
Cdd:COG4615   531 DYGKLVELTGP 541
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
339-496 2.95e-06

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: 49.18  E-value: 2.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 339 DLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRG--LVKGG--TKLEVAYFDQYRDQ----------LDPEQTVMDNV 404
Cdd:cd03294    44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGkvLIDGQdiAAMSRKELRELRRKkismvfqsfaLLPHRTVLENV 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 405 -------GEGKQEvmvrgRSRHILGYLQDFLFEPKRARTPvKALSGGEKNRLLLAK-LFLKPSnLLILDEPTNDLD---- 472
Cdd:cd03294   124 afglevqGVPRAE-----REERAAEALELVGLEGWEHKYP-DELSGGMQQRVGLARaLAVDPD-ILLMDEAFSALDplir 196
                         170       180
                  ....*....|....*....|....
gi 1411607396 473 VETLELLEELLADYPGTLLLVSHD 496
Cdd:cd03294   197 REMQDELLRLQAELQKTIVFITHD 220
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
315-496 3.09e-06

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


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 50.03  E-value: 3.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 315 SGKLVFETEGLGLDFGDRTLfqgldlQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRG--LVKGG--TKLEVAYFDQY 390
Cdd:PRK10070   30 SKEQILEKTGLSLGVKDASL------AIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGqvLIDGVdiAKISDAELREV 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 391 RDQ----------LDPEQTVMDNVGEGKQ--EVMVRGRSRHILGYLQDFLFEPKRARTPvKALSGGEKNRLLLAKLFLKP 458
Cdd:PRK10070  104 RRKkiamvfqsfaLMPHMTVLDNTAFGMElaGINAEERREKALDALRQVGLENYAHSYP-DELSGGMRQRVGLARALAIN 182
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1411607396 459 SNLLILDEPTNDLD----VETLELLEELLADYPGTLLLVSHD 496
Cdd:PRK10070  183 PDILLMDEAFSALDplirTEMQDELVKLQAKHQRTIVFISHD 224
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
319-475 3.12e-06

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 49.24  E-value: 3.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 319 VFETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKL----------------LLGQLEPSRGLVKGGTKL 382
Cdd:PRK09984    4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHlsglitgdksagshieLLGRTVQREGRLARDIRK 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 383 EVAY----FDQYrdQLDPEQTVMDNVGEG-------------------KQEVMvRGRSRHILGYLqdflfepkrARTPVK 439
Cdd:PRK09984   84 SRANtgyiFQQF--NLVNRLSVLENVLIGalgstpfwrtcfswftreqKQRAL-QALTRVGMVHF---------AHQRVS 151
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1411607396 440 ALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVET 475
Cdd:PRK09984  152 TLSGGQQQRVAIARALMQQAKVILADEPIASLDPES 187
PvdE COG4615
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...
338-393 3.55e-06

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


Pssm-ID: 443659 [Multi-domain]  Cd Length: 547  Bit Score: 50.18  E-value: 3.55e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1411607396 338 LDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTKLEVAYFDQYRDQ 393
Cdd:COG4615   351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILlDGQPVTADNREAYRQL 407
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
17-241 3.67e-06

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


Pssm-ID: 213269 [Multi-domain]  Cd Length: 207  Bit Score: 48.18  E-value: 3.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  17 PLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRM-VQQQDLKVTRLEQdppASSDLTVfdytaeglagvg 95
Cdd:cd03369    22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIeIDGIDISTIPLED---LRSSLTI------------ 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  96 ellkkyhhismeLAHDPsdanIRIMSDLQEQLDYQNGWQFEtrisQVLTLLNLDPDAtlDSLSGGWLRKVALARALACDP 175
Cdd:cd03369    87 ------------IPQDP----TLFSGTIRSNLDPFDEYSDE----EIYGALRVSEGG--LNLSQGQRQLLCLARALLKRP 144
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1411607396 176 DLLLLDEPTNHLDIEAINWLEDFL-KDFRGAIVFIshdreFIHKLATrIIDLDRGVITSwPGNYDEY 241
Cdd:cd03369   145 RVLVLDEATASIDYATDALIQKTIrEEFTNSTILT-----IAHRLRT-IIDYDKILVMD-AGEVKEY 204
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
11-253 3.77e-06

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 50.41  E-value: 3.77e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   11 LSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMV-----QQQDLKVTRLEQDPPASS----DL 81
Cdd:PTZ00265  1176 ISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNDHHIvfkneHTNDMTNEQDYQGDEEQNvgmkNV 1255
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   82 TVFDYTAEGLAGVGELLKKYHHISMELAHDPSDANIRIMSDL-----QEQL-----DYQN---GWQFETR---------- 138
Cdd:PTZ00265  1256 NEFSLTKEGGSGEDSTVFKNSGKILLDGVDICDYNLKDLRNLfsivsQEPMlfnmsIYENikfGKEDATRedvkrackfa 1335
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  139 -ISQVLTLLNLDPDATL----DSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRGaivfiSHDR 213
Cdd:PTZ00265  1336 aIDEFIESLPNKYDTNVgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKD-----KADK 1410
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1411607396  214 EFI---HKLATrIIDLDRGVITSWPGNYDEYLQGK---EEALRVEE 253
Cdd:PTZ00265  1411 TIItiaHRIAS-IKRSDKIVVFNNPDRTGSFVQAHgthEELLSVQD 1455
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
18-219 4.48e-06

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 48.27  E-value: 4.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  18 LLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGelplddgrmvqqqdlkvtrleQDPPASSD-------LTVFDYTAEG 90
Cdd:PRK11629   24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGG---------------------LDTPTSGDvifngqpMSKLSSAAKA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  91 LAGVGEL--LKKYHHismeLAHDPSDANIRIMSDLqeqLDYQNGWQFETRISQVLTLLNLDPDATLDS--LSGGWLRKVA 166
Cdd:PRK11629   83 ELRNQKLgfIYQFHH----LLPDFTALENVAMPLL---IGKKKPAEINSRALEMLAAVGLEHRANHRPseLSGGERQRVA 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1411607396 167 LARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFR----GAIVFISHDREFIHKL 219
Cdd:PRK11629  156 IARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNrlqgTAFLVVTHDLQLAKRM 212
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
349-472 4.53e-06

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


Pssm-ID: 130324 [Multi-domain]  Cd Length: 2272  Bit Score: 50.01  E-value: 4.53e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  349 ALVGPNGCGKSTLIKLLLGQLEPSRGLV-KGGTKLEVAyFDQYRDQLD--PEQTVMDNVGEGKQEVM----VRGRSR--- 418
Cdd:TIGR01257  960 AFLGHNGAGKTTTLSILTGLLPPTSGTVlVGGKDIETN-LDAVRQSLGmcPQHNILFHHLTVAEHILfyaqLKGRSWeea 1038
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1411607396  419 --HILGYLQDFLFEPKRaRTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:TIGR01257 1039 qlEMEAMLEDTGLHHKR-NEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVD 1093
cbiO PRK13650
energy-coupling factor transporter ATPase;
341-496 4.74e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 48.57  E-value: 4.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 341 QVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRG-LVKGGTKLEVAYFDQYRDQL-----DPEQ-----TVMDNVG---- 405
Cdd:PRK13650   29 HVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGqIIIDGDLLTEENVWDIRHKIgmvfqNPDNqfvgaTVEDDVAfgle 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 406 -EGKQEVMVRGRSRHILGY--LQDFlfepkRARTPVKaLSGGEKNRLLLAKLFLKPSNLLILDEPTNDLD----VETLEL 478
Cdd:PRK13650  109 nKGIPHEEMKERVNEALELvgMQDF-----KEREPAR-LSGGQKQRVAIAGAVAMRPKIIILDEATSMLDpegrLELIKT 182
                         170
                  ....*....|....*...
gi 1411607396 479 LEELLADYPGTLLLVSHD 496
Cdd:PRK13650  183 IKGIRDDYQMTVISITHD 200
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
323-468 5.24e-06

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 49.74  E-value: 5.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 323 EGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGqlepSRGLVKGgtKLEV------------------ 384
Cdd:NF033858    5 EGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAG----ARKIQQG--RVEVlggdmadarhrravcpri 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 385 AYFDQ------YrdqldPEQTVMDNV-------GEGKQEvmvrgRSRHILGYLQDFLFEPKRARtPVKALSGGEKNRL-L 450
Cdd:NF033858   79 AYMPQglgknlY-----PTLSVFENLdffgrlfGQDAAE-----RRRRIDELLRATGLAPFADR-PAGKLSGGMKQKLgL 147
                         170
                  ....*....|....*...
gi 1411607396 451 LAKLFLKPsNLLILDEPT 468
Cdd:NF033858  148 CCALIHDP-DLLILDEPT 164
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
34-216 5.44e-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: 47.60  E-value: 5.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  34 LVGRNGAGKSTLMKIIA----GELPLD-DGRmvqQQDLKVTRlEQDPPASSDLTVfdYTAEGlagvgellKKYHhISMEL 108
Cdd:cd03240    27 IVGQNGAGKTTIIEALKyaltGELPPNsKGG---AHDPKLIR-EGEVRAQVKLAF--ENANG--------KKYT-ITRSL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 109 AHDPSDANIRimsdlQEQLDyqngwqfetrisqvlTLLnLDPdatLDSLSGGW-------LRkVALARALACDPDLLLLD 181
Cdd:cd03240    92 AILENVIFCH-----QGESN---------------WPL-LDM---RGRCSGGEkvlasliIR-LALAETFGSNCGILALD 146
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1411607396 182 EPTNHLDIEAINW-LEDFLKDFRGAIVF----ISHDREFI 216
Cdd:cd03240   147 EPTTNLDEENIEEsLAEIIEERKSQKNFqlivITHDEELV 186
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
20-210 5.48e-06

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 49.16  E-value: 5.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  20 DNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPlddGR-----MVQQQDLKVTRleqdpPAssdltvfDYTAEGLAGV 94
Cdd:PRK13549  279 DDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYP---GRwegeiFIDGKPVKIRN-----PQ-------QAIAQGIAMV 343
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  95 GELLKKYHHIS-MELAHDPSDANIRIMS-----DLQEQLDYqngwqfetrISQVLTLLNL---DPDATLDSLSGGWLRKV 165
Cdd:PRK13549  344 PEDRKRDGIVPvMGVGKNITLAALDRFTggsriDDAAELKT---------ILESIQRLKVktaSPELAIARLSGGNQQKA 414
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1411607396 166 ALARALACDPDLLLLDEPTNHLDIEA-------INWLEDflkdfRG-AIVFIS 210
Cdd:PRK13549  415 VLAKCLLLNPKILILDEPTRGIDVGAkyeiyklINQLVQ-----QGvAIIVIS 462
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
8-229 5.83e-06

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 49.34  E-value: 5.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   8 GACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMV---QQQDLK---------VTRLEQDP 75
Cdd:PRK10982    3 NISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILfqgKEIDFKsskealengISMVHQEL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  76 PASSDLTVFDytaeglagvGELLKKYHHISMELAHDPS-DANIRIMSDLQeqldyqngwqfetrisqvltlLNLDPDATL 154
Cdd:PRK10982   83 NLVLQRSVMD---------NMWLGRYPTKGMFVDQDKMyRDTKAIFDELD---------------------IDIDPRAKV 132
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1411607396 155 DSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDF---LKDFRGAIVFISHDREFIHKLATRIIDLDRG 229
Cdd:PRK10982  133 ATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHLFTIirkLKERGCGIVYISHKMEEIFQLCDEITILRDG 210
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
336-501 7.04e-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: 46.93  E-value: 7.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 336 QGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRgLVKGGTKlevaYFDQYRDQLDPEQTVMDnVGegkqevmvrg 415
Cdd:cd03238    12 QNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYASGKAR-LISFLPK----FSRNKLIFIDQLQFLID-VG---------- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 416 rsrhiLGYLqdflfepkRARTPVKALSGGEKNRLLLAK-LFLKPSN-LLILDEPTNDL---DVETLELLEELLADYPGTL 490
Cdd:cd03238    76 -----LGYL--------TLGQKLSTLSGGELQRVKLASeLFSEPPGtLFILDEPSTGLhqqDINQLLEVIKGLIDLGNTV 142
                         170
                  ....*....|.
gi 1411607396 491 LLVSHDRRFID 501
Cdd:cd03238   143 ILIEHNLDVLS 153
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
157-222 7.49e-06

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 48.17  E-value: 7.49e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1411607396 157 LSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDF--RGAIVFISHDREFIHKLATR 222
Cdd:PRK14271  164 LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLadRLTVIIVTHNLAQAARISDR 231
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
156-245 8.21e-06

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: 46.80  E-value: 8.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 156 SLSGGWLRKVALARALACDPDLLLLDEPTNHLDIE----AINWLEDFLKDFRGAIVFISHDREFIHKLATRIIdldrgVI 231
Cdd:cd03222    71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEqrlnAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIH-----VF 145
                          90
                  ....*....|....
gi 1411607396 232 TSWPGNYDEYLQGK 245
Cdd:cd03222   146 EGEPGVYGIASQPK 159
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
13-211 9.00e-06

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 47.53  E-value: 9.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  13 FSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDD-----------GRMVQQQDL-------KVTRLEQD 74
Cdd:PRK14267   14 YGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearvegevrlfGRNIYSPDVdpievrrEVGMVFQY 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  75 PPASSDLTVFDYTAEGLAgVGELLKKyhhismelahdpsdanirimsdlQEQLDYQNGWQFE--TRISQVLTLLNLDPDa 152
Cdd:PRK14267   94 PNPFPHLTIYDNVAIGVK-LNGLVKS-----------------------KKELDERVEWALKkaALWDEVKDRLNDYPS- 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1411607396 153 tldSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRG--AIVFISH 211
Cdd:PRK14267  149 ---NLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKeyTIVLVTH 206
PRK10522 PRK10522
multidrug transporter membrane component/ATP-binding component; Provisional
24-232 9.75e-06

multidrug transporter membrane component/ATP-binding component; Provisional


Pssm-ID: 236707 [Multi-domain]  Cd Length: 547  Bit Score: 48.43  E-value: 9.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  24 LSIERGERLCLVGRNGAGKSTLMKII-------AGELPLdDGRMVQQQDLKVTRlEQDPPASSDLTVFDYT--AEGLAGV 94
Cdd:PRK10522  344 LTIKRGELLFLIGGNGSGKSTLAMLLtglyqpqSGEILL-DGKPVTAEQPEDYR-KLFSAVFTDFHLFDQLlgPEGKPAN 421
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  95 GELLKKYhhismeLAHdpsdanirimSDLQEQLDYQNGwqfetrisqvlTLLNLDpdatldsLSGGWLRKVALARALACD 174
Cdd:PRK10522  422 PALVEKW------LER----------LKMAHKLELEDG-----------RISNLK-------LSKGQKKRLALLLALAEE 467
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1411607396 175 PDLLLLDEptnhldieainWLEDFLKDFR--------------GAIVF-ISHDRE-FIHklATRIIDLDRGVIT 232
Cdd:PRK10522  468 RDILLLDE-----------WAADQDPHFRrefyqvllpllqemGKTIFaISHDDHyFIH--ADRLLEMRNGQLS 528
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
337-475 9.92e-06

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: 47.10  E-value: 9.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 337 GLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTKLEVAYFDQYRDQL-----DP---EQTVMDNV--- 404
Cdd:cd03244    22 NISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILiDGVDISKIGLHDLRSRIsiipqDPvlfSGTIRSNLdpf 101
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1411607396 405 GEGKQEVMVRGRSR-HILGYLQDFlfePKRARTPVKA----LSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVET 475
Cdd:cd03244   102 GEYSDEELWQALERvGLKEFVESL---PGGLDTVVEEggenLSVGQRQLLCLARALLRKSKILVLDEATASVDPET 174
SufC COG0396
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ...
321-474 1.21e-05

Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440165 [Multi-domain]  Cd Length: 245  Bit Score: 46.98  E-value: 1.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLG--QLEPSRG--LVKGG--TKLEV---------- 384
Cdd:COG0396     2 EIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGhpKYEVTSGsiLLDGEdiLELSPderaragifl 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 385 AYfdQY---------RDQLdpeQTVMDNVGEGKQEVM-----VRGRSRhILGYLQDFLfepKRartPVKA-LSGGEKNRL 449
Cdd:COG0396    82 AF--QYpveipgvsvSNFL---RTALNARRGEELSAReflklLKEKMK-ELGLDEDFL---DR---YVNEgFSGGEKKRN 149
                         170       180
                  ....*....|....*....|....*.
gi 1411607396 450 -LLAKLFLKPSnLLILDEPTNDLDVE 474
Cdd:COG0396   150 eILQMLLLEPK-LAILDETDSGLDID 174
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
338-500 1.30e-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: 46.56  E-value: 1.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 338 LDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKGGTKLE---------------VAYFDQYRDQLDPeqTVMD 402
Cdd:cd03290    20 INIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNEsepsfeatrsrnrysVAYAAQKPWLLNA--TVEE 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 403 NVGEGKQEVMVRGRSRHILGYLQ-DFLFEPKRARTPVKA----LSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVETLE 477
Cdd:cd03290    98 NITFGSPFNKQRYKAVTDACSLQpDIDLLPFGDQTEIGErginLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSD 177
                         170       180
                  ....*....|....*....|....*...
gi 1411607396 478 LLEEL-----LADYPGTLLLVSHDRRFI 500
Cdd:cd03290   178 HLMQEgilkfLQDDKRTLVLVTHKLQYL 205
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
337-516 1.41e-05

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 47.39  E-value: 1.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 337 GLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLV-----------KGGTKLEVAY------------------- 386
Cdd:PRK13651   25 NVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkKTKEKEKVLEklviqktrfkkikkikeir 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 387 --------FDQYrdQLDpEQTVMDNV-------GEGKQEVMVRGRSR-HILGYLQDFLfepkrARTPVkALSGGEKNRLL 450
Cdd:PRK13651  105 rrvgvvfqFAEY--QLF-EQTIEKDIifgpvsmGVSKEEAKKRAAKYiELVGLDESYL-----QRSPF-ELSGGQKRRVA 175
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1411607396 451 LAKLFLKPSNLLILDEPTNDLD---VETLELLEELLADYPGTLLLVSHDrrfIDNTV--TGCWLFEGDGRI 516
Cdd:PRK13651  176 LAGILAMEPDFLVFDEPTAGLDpqgVKEILEIFDNLNKQGKTIILVTHD---LDNVLewTKRTIFFKDGKI 243
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
5-195 1.45e-05

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


Pssm-ID: 213200 [Multi-domain]  Cd Length: 202  Bit Score: 46.49  E-value: 1.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   5 TLHGACLSF------SDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPlddgrmvqqQDLKVTRleqdppas 78
Cdd:cd03233     3 TLSWRNISFttgkgrSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTE---------GNVSVEG-------- 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  79 sDLTVFDYTAEglagvgELLKKYHH-ISMELAHDPSDANIRImsdlQEQLDYQngwqfetrisqvltlLNLDPDATLDSL 157
Cdd:cd03233    66 -DIHYNGIPYK------EFAEKYPGeIIYVSEEDVHFPTLTV----RETLDFA---------------LRCKGNEFVRGI 119
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1411607396 158 SGGWLRKVALARALACDPDLLLLDEPTNHLD-IEAINWL 195
Cdd:cd03233   120 SGGERKRVSIAEALVSRASVLCWDNSTRGLDsSTALEIL 158
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
138-226 1.51e-05

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: 45.78  E-value: 1.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 138 RISQVLTLLN-----LDPDATLDSLSGGWLRKVALARALACDPD--LLLLDEPTNHLDIEAINWLEDFLKDFRG---AIV 207
Cdd:cd03238    64 FIDQLQFLIDvglgyLTLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDlgnTVI 143
                          90
                  ....*....|....*....
gi 1411607396 208 FISHDREFIhKLATRIIDL 226
Cdd:cd03238   144 LIEHNLDVL-SSADWIIDF 161
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
18-226 1.53e-05

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 46.95  E-value: 1.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  18 LLDNAELSIERGERLCLVGRNGAGKSTLMKII------AGELPLDD-----GRMVQQQDLKVTRLEQD------PPASSD 80
Cdd:PRK14258   22 ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLnrmnelESEVRVEGrveffNQNIYERRVNLNRLRRQvsmvhpKPNLFP 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  81 LTVFDYTAEGLAGVGellkkyHHISMELaHDPSDANIRiMSDLQEQLdyqngwqfETRISQvltllnldpdATLDsLSGG 160
Cdd:PRK14258  102 MSVYDNVAYGVKIVG------WRPKLEI-DDIVESALK-DADLWDEI--------KHKIHK----------SALD-LSGG 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 161 WLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFR----GAIVFISHDrefIHKLaTRIIDL 226
Cdd:PRK14258  155 QQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlrseLTMVIVSHN---LHQV-SRLSDF 220
cbiO PRK13645
energy-coupling factor transporter ATPase;
339-472 1.55e-05

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 47.31  E-value: 1.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 339 DLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRG-LVKGGTKL---------------EVAYFDQYRD-QLDPEQTVM 401
Cdd:PRK13645   31 SLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGqTIVGDYAIpanlkkikevkrlrkEIGLVFQFPEyQLFQETIEK 110
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1411607396 402 D------NVGEGKQEVMVRgrsrhiLGYLQDFLFEPKR--ARTPVKaLSGGEKNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:PRK13645  111 DiafgpvNLGENKQEAYKK------VPELLKLVQLPEDyvKRSPFE-LSGGQKRRVALAGIIAMDGNTLVLDEPTGGLD 182
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
15-240 1.94e-05

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 47.47  E-value: 1.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  15 DFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMVqqqdLKVTRLEQDPPassdltvFDYTAEGLAGV 94
Cdd:PRK09700  275 DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIR----LNGKDISPRSP-------LDAVKKGMAYI 343
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  95 GELLKK---YHHISMElahdpsdANIRIMSDLQEQlDYQNGWQF-----ETRISQ----VLTLLNLDPDATLDSLSGGWL 162
Cdd:PRK09700  344 TESRRDngfFPNFSIA-------QNMAISRSLKDG-GYKGAMGLfhevdEQRTAEnqreLLALKCHSVNQNITELSGGNQ 415
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 163 RKVALARALACDPDLLLLDEPTNHLDIEA---INWLEDFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVITSWPGNYD 239
Cdd:PRK09700  416 QKVLISKWLCCCPEVIIFDEPTRGIDVGAkaeIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRD 495

                  .
gi 1411607396 240 E 240
Cdd:PRK09700  496 D 496
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
336-472 2.13e-05

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


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 47.15  E-value: 2.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 336 QGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGqLEPsrglVKGG---------TKLEVA------YFDQYrdQLDPEQTV 400
Cdd:PRK11650   21 KGIDLDVADGEFIVLVGPSGCGKSTLLRMVAG-LER----ITSGeiwiggrvvNELEPAdrdiamVFQNY--ALYPHMSV 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 401 MDNVGEG-------KQEVMVR-GRSRHILGyLQDFLfepkrARTPvKALSGGEKNRLLLA-------KLFLkpsnlliLD 465
Cdd:PRK11650   94 RENMAYGlkirgmpKAEIEERvAEAARILE-LEPLL-----DRKP-RELSGGQRQRVAMGraivrepAVFL-------FD 159

                  ....*..
gi 1411607396 466 EPTNDLD 472
Cdd:PRK11650  160 EPLSNLD 166
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
3-229 2.50e-05

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


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 46.14  E-value: 2.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396   3 LLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKII-------AGELPLDDGRMVQQQDLKVTRLE--- 72
Cdd:PRK11300    5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLtgfykptGGTILLRGQHIEGLPGHQIARMGvvr 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  73 --QDPPASSDLTVFdytaEGLagvgeLLKKYHHIsmelahdpsdaNIRIMSDL----------QEQLDYQNGWqfetris 140
Cdd:PRK11300   85 tfQHVRLFREMTVI----ENL-----LVAQHQQL-----------KTGLFSGLlktpafrraeSEALDRAATW------- 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 141 qvLTLLNLDPDATLDS--LSGGWLRKVALARALACDPDLLLLDEPT---NHLDIEAINWLEDFLKD-FRGAIVFISHDRE 214
Cdd:PRK11300  138 --LERVGLLEHANRQAgnLAYGQQRRLEIARCMVTQPEILMLDEPAaglNPKETKELDELIAELRNeHNVTVLLIEHDMK 215
                         250
                  ....*....|....*
gi 1411607396 215 FIHKLATRIIDLDRG 229
Cdd:PRK11300  216 LVMGISDRIYVVNQG 230
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
11-188 2.74e-05

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


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 47.02  E-value: 2.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  11 LSFS---DFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLD------DGRMVQQQDLKVTR-----LEQDPP 76
Cdd:PRK10790  346 VSFAyrdDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTegeirlDGRPLSSLSHSVLRqgvamVQQDPV 425
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  77 ASSDlTVFdytaeglagvgellkkyhhismelahdpsdANIRIMSDLQEqldyQNGWQ-FETriSQVLTLLNLDPDA--T 153
Cdd:PRK10790  426 VLAD-TFL------------------------------ANVTLGRDISE----EQVWQaLET--VQLAELARSLPDGlyT 468
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1411607396 154 L-----DSLSGGWLRKVALARALACDPDLLLLDEPTNHLD 188
Cdd:PRK10790  469 PlgeqgNNLSVGQKQLLALARVLVQTPQILILDEATANID 508
CeuD COG4604
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ...
321-472 2.95e-05

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


Pssm-ID: 443654 [Multi-domain]  Cd Length: 252  Bit Score: 45.84  E-value: 2.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRG--LVKGgtkLEVAYFDQyRD------ 392
Cdd:COG4604     3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGevLVDG---LDVATTPS-RElakrla 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 393 ------QLDPEQTVMDNVGEGkqevmvR-----GR-----SRHI--------LGYLQD-FLFEpkrartpvkaLSGGEKN 447
Cdd:COG4604    79 ilrqenHINSRLTVRELVAFG------RfpyskGRltaedREIIdeaiayldLEDLADrYLDE----------LSGGQRQ 142
                         170       180
                  ....*....|....*....|....*
gi 1411607396 448 RLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:COG4604   143 RAFIAMVLAQDTDYVLLDEPLNNLD 167
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
348-473 3.32e-05

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 45.94  E-value: 3.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 348 IALVGPNGCGKSTLIKLLLGQLEPSRG-LVKGGTKLEVAYFdQYRDQ------------LDPEQTV---MDNVGEGKQEV 411
Cdd:PRK15112   42 LAIIGENGSGKSTLAKMLAGMIEPTSGeLLIDDHPLHFGDY-SYRSQrirmifqdpstsLNPRQRIsqiLDFPLRLNTDL 120
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1411607396 412 MVRGRSRHILGYLQDFLFEPKRARTPVKALSGGEKNRLLLAK-LFLKPsNLLILDEPTNDLDV 473
Cdd:PRK15112  121 EPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQKQRLGLARaLILRP-KVIIADEALASLDM 182
cbiO PRK13640
energy-coupling factor transporter ATPase;
338-472 4.78e-05

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 45.56  E-value: 4.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 338 LDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEP-----SRGLVKGGTKLEVAYFDqYRDQL-----DPEQ-----TVMD 402
Cdd:PRK13640   26 ISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnpnSKITVDGITLTAKTVWD-IREKVgivfqNPDNqfvgaTVGD 104
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1411607396 403 NVGEGKQEvmvRGRSR-HILGYLQDFLFE---PKRARTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:PRK13640  105 DVAFGLEN---RAVPRpEMIKIVRDVLADvgmLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLD 175
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
156-188 5.48e-05

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 45.15  E-value: 5.48e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1411607396 156 SLSGGWLRKVALARALACDPDLLLLDEPTNHLD 188
Cdd:PRK14239  148 GLSGGQQQRVCIARVLATSPKIILLDEPTSALD 180
GguA NF040905
sugar ABC transporter ATP-binding protein;
19-210 5.83e-05

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 45.94  E-value: 5.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  19 LDNAELSIERGERLCLVGRNGAGKSTL-MKI--------IAGELpLDDGRMVqqqDLKvtrleqdppassdlTVFDYTAE 89
Cdd:NF040905  276 VDDVSLNVRRGEIVGIAGLMGAGRTELaMSVfgrsygrnISGTV-FKDGKEV---DVS--------------TVSDAIDA 337
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  90 GLAGVGELLKKYHHISME-LAHDPSDANIRIMS-----DLQEQLDYQNGWQFETRI--SQVltllnldpDATLDSLSGGW 161
Cdd:NF040905  338 GLAYVTEDRKGYGLNLIDdIKRNITLANLGKVSrrgviDENEEIKVAEEYRKKMNIktPSV--------FQKVGNLSGGN 409
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1411607396 162 LRKVALARALACDPDLLLLDEPTNHLDIEA-------INWLEDFLKdfrgAIVFIS 210
Cdd:NF040905  410 QQKVVLSKWLFTDPDVLILDEPTRGIDVGAkyeiytiINELAAEGK----GVIVIS 461
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
335-467 5.87e-05

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: 45.86  E-value: 5.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 335 FQGLDLQV---LRGDKI-ALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTKLevayFDQYRDQ---------------- 393
Cdd:COG4148    11 RGGFTLDVdftLPGRGVtALFGPSGSGKTTLLRAIAGLERPDSGRIRlGGEVL----QDSARGIflpphrrrigyvfqea 86
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1411607396 394 -LDPEQTVMDNVGEGkQEVMVRGRSRHILGYLQDFL-FEPKRARTPVkALSGGEKNRLLLAK-LFLKPSnLLILDEP 467
Cdd:COG4148    87 rLFPHLSVRGNLLYG-RKRAPRAERRISFDEVVELLgIGHLLDRRPA-TLSGGERQRVAIGRaLLSSPR-LLLMDEP 160
ABCG_PDR_domain2 cd03232
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...
17-191 7.25e-05

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: 44.16  E-value: 7.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  17 PLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGelplddgrmvqqqdlkvtrleqdppassdltvfdytaEGLAGV-- 94
Cdd:cd03232    21 QLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAG-------------------------------------RKTAGVit 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  95 GELLkkyhhismeLAHDPSDANIRIMSDLQEQLDYQNGwqfETRISQVLTLlnldpDATLDSLSGGWLRKVALARALACD 174
Cdd:cd03232    64 GEIL---------INGRPLDKNFQRSTGYVEQQDVHSP---NLTVREALRF-----SALLRGLSVEQRKRLTIGVELAAK 126
                         170
                  ....*....|....*..
gi 1411607396 175 PDLLLLDEPTNHLDIEA 191
Cdd:cd03232   127 PSILFLDEPTSGLDSQA 143
PLN03211 PLN03211
ABC transporter G-25; Provisional
329-472 7.47e-05

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 46.03  E-value: 7.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 329 FGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPS----RGLVKGG--TK--LEVAYFDQYRDQLDPEQTV 400
Cdd:PLN03211   78 IQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnftgTILANNRkpTKqiLKRTGFVTQDDILYPHLTV 157
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 401 MDNV----------GEGKQEVMVRGRS-----------RHILGylqdflfepkraRTPVKALSGGEKNRLLLA-KLFLKP 458
Cdd:PLN03211  158 RETLvfcsllrlpkSLTKQEKILVAESviselgltkceNTIIG------------NSFIRGISGGERKRVSIAhEMLINP 225
                         170
                  ....*....|....
gi 1411607396 459 SnLLILDEPTNDLD 472
Cdd:PLN03211  226 S-LLILDEPTSGLD 238
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
345-472 7.98e-05

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


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 45.81  E-value: 7.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 345 GDKIALVGPNGCGKSTLIKLLLGQLEPsrGLVKGGTKL------------EVAYFDQYRDQLDPEQTV-----------M 401
Cdd:TIGR00955  51 GELLAVMGSSGAGKTTLMNALAFRSPK--GVKGSGSVLlngmpidakemrAISAYVQQDDLFIPTLTVrehlmfqahlrM 128
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1411607396 402 DNVGEGKQEvmvRGRSRHILGYL-----QDFLF-EPKRartpVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:TIGR00955 129 PRRVTKKEK---RERVDEVLQALglrkcANTRIgVPGR----VKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLD 198
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
25-189 8.70e-05

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 44.78  E-value: 8.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  25 SIERGERLCLVGRNGAGKSTLMKIIAGelplddgrMVqqqdlkvtrleqdPPASSDLTVFDYTAEglagVGELLKKYHHI 104
Cdd:PRK15112   35 TLREGQTLAIIGENGSGKSTLAKMLAG--------MI-------------EPTSGELLIDDHPLH----FGDYSYRSQRI 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 105 SMeLAHDPS-------------DANIRIMSDLQEQldyqngwQFETRISQVLTLLNLDPDATL---DSLSGGWLRKVALA 168
Cdd:PRK15112   90 RM-IFQDPStslnprqrisqilDFPLRLNTDLEPE-------QREKQIIETLRQVGLLPDHASyypHMLAPGQKQRLGLA 161
                         170       180
                  ....*....|....*....|.
gi 1411607396 169 RALACDPDLLLLDEPTNHLDI 189
Cdd:PRK15112  162 RALILRPKVIIADEALASLDM 182
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
337-473 1.12e-04

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 44.57  E-value: 1.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 337 GLDLQVLRGDKIALVGPNGCGKSTLIKLL-------------LGQ--LEPSRGLVKG-GTKLEVAYFDQYrDQLDPEQTV 400
Cdd:PRK11308   33 GVSFTLERGKTLAVVGESGCGKSTLARLLtmietptggelyyQGQdlLKADPEAQKLlRQKIQIVFQNPY-GSLNPRKKV 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 401 MDNVGE--------GKQEvmvrgRSRHILGYLQDFLFEPKRA-RTPvKALSGGEKNRLLLAK-LFLKPsNLLILDEPTND 470
Cdd:PRK11308  112 GQILEEpllintslSAAE-----RREKALAMMAKVGLRPEHYdRYP-HMFSGGQRQRIAIARaLMLDP-DVVVADEPVSA 184

                  ...
gi 1411607396 471 LDV 473
Cdd:PRK11308  185 LDV 187
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
7-59 1.40e-04

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 45.12  E-value: 1.40e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1411607396   7 HGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGR 59
Cdd:NF033858  270 RGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGE 322
sufC PRK09580
cysteine desulfurase ATPase component; Reviewed
331-474 1.61e-04

cysteine desulfurase ATPase component; Reviewed


Pssm-ID: 181965 [Multi-domain]  Cd Length: 248  Bit Score: 43.63  E-value: 1.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 331 DRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSrglVKGGtklEVAYFDQYRDQLDPEqtvmDNVGEG--- 407
Cdd:PRK09580   13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYE---VTGG---TVEFKGKDLLELSPE----DRAGEGifm 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 408 --KQEVMVRGRSRHIL---------GY----------LQDFLFEPKR---------ARTPVKALSGGEKNRLLLAKLFLK 457
Cdd:PRK09580   83 afQYPVEIPGVSNQFFlqtalnavrSYrgqepldrfdFQDLMEEKIAllkmpedllTRSVNVGFSGGEKKRNDILQMAVL 162
                         170
                  ....*....|....*..
gi 1411607396 458 PSNLLILDEPTNDLDVE 474
Cdd:PRK09580  163 EPELCILDESDSGLDID 179
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
156-212 1.72e-04

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 43.62  E-value: 1.72e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1411607396 156 SLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDF--RGAIVFISHD 212
Cdd:PRK14243  151 SLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELkeQYTIIIVTHN 209
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
344-472 2.49e-04

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 43.20  E-value: 2.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 344 RGDKIALVGPNGCGKSTLIKLLLGQLEPSRGlvkggtklEVAYFDQYRDQLD--------------PEQ-----TVMDNV 404
Cdd:PRK13648   34 KGQWTSIVGHNGSGKSTIAKLMIGIEKVKSG--------EIFYNNQAITDDNfeklrkhigivfqnPDNqfvgsIVKYDV 105
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1411607396 405 GEGKQEVMVRGRSRH--ILGYLQDFLFEPKRARTPvKALSGGEKNRLLLAK-LFLKPSnLLILDEPTNDLD 472
Cdd:PRK13648  106 AFGLENHAVPYDEMHrrVSEALKQVDMLERADYEP-NALSGGQKQRVAIAGvLALNPS-VIILDEATSMLD 174
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
331-475 3.11e-04

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


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 43.93  E-value: 3.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 331 DRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTKLEVAYFDQYRDQL-----DP---EQTVM 401
Cdd:PRK10789  327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRfHDIPLTKLQLDSWRSRLavvsqTPflfSDTVA 406
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 402 DNVGEGKQ-------EVMVRGRSRHilgylQDFLFEPKRARTPVKA----LSGGEKNRLLLAKLFLKPSNLLILDEPTND 470
Cdd:PRK10789  407 NNIALGRPdatqqeiEHVARLASVH-----DDILRLPQGYDTEVGErgvmLSGGQKQRISIARALLLNAEILILDDALSA 481

                  ....*
gi 1411607396 471 LDVET 475
Cdd:PRK10789  482 VDGRT 486
hmuV PRK13547
heme ABC transporter ATP-binding protein;
332-473 3.19e-04

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 42.89  E-value: 3.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 332 RTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLepSRGLVKGGTKL--EVAYFDQYRDQLDPEQ-----TVMDNV 404
Cdd:PRK13547   14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDL--TGGGAPRGARVtgDVTLNGEPLAAIDAPRlarlrAVLPQA 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 405 GE-----GKQEVMVRGRSRHIL---------GYLQDFLFEPKRA----RTPVKALSGGEKNRL----LLAKLF-----LK 457
Cdd:PRK13547   92 AQpafafSAREIVLLGRYPHARragalthrdGEIAWQALALAGAtalvGRDVTTLSGGELARVqfarVLAQLWpphdaAQ 171
                         170
                  ....*....|....*.
gi 1411607396 458 PSNLLILDEPTNDLDV 473
Cdd:PRK13547  172 PPRYLLLDEPTAALDL 187
RNA_helicase pfam00910
RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding ...
350-413 3.34e-04

RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding during viral RNA replication. Members of this family are found in a variety of single stranded RNA viruses.


Pssm-ID: 459992  Cd Length: 102  Bit Score: 40.28  E-value: 3.34e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1411607396 350 LVGPNGCGKSTLIKLLLGQLEPSRGLVKGGTKL---EVAYFDQYRDQldpEQTVMDNVGEGKQEVMV 413
Cdd:pfam00910   3 LYGPPGCGKSTLAKYLARALLKKLGLPKDSVYSrnpDDDFWDGYTGQ---PVVIIDDFGQNPDGPDE 66
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
319-472 4.83e-04

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 42.46  E-value: 4.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 319 VFETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLL--LGQLEPS---RGLVK-GGTKLEVAYFD--QY 390
Cdd:PRK14239    5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVyNGHNIYSPRTDtvDL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 391 R-------DQLDP-EQTVMDNV-------GEGKQEVM-------VRGRSrhILGYLQDFLFEPkrartpVKALSGGEKNR 448
Cdd:PRK14239   85 RkeigmvfQQPNPfPMSIYENVvyglrlkGIKDKQVLdeaveksLKGAS--IWDEVKDRLHDS------ALGLSGGQQQR 156
                         170       180
                  ....*....|....*....|....
gi 1411607396 449 LLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:PRK14239  157 VCIARVLATSPKIILLDEPTSALD 180
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
307-475 5.10e-04

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 43.08  E-value: 5.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 307 LQMDDVNRSGKLVFETEGLGLDFGDRTL-FQGLDLQVLR--------GDKIALVGPNGCGKSTLIKLLLGQLEPSRG-LV 376
Cdd:PRK11176  322 LDLEQEKDEGKRVIERAKGDIEFRNVTFtYPGKEVPALRninfkipaGKTVALVGRSGSGKSTIANLLTRFYDIDEGeIL 401
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 377 KGGTKLEVAYFDQYRDQ--LDPEQ------TVMDNVGEGKQEVMVRGRSRHI--LGYLQDFLFEPKRARTPV-----KAL 441
Cdd:PRK11176  402 LDGHDLRDYTLASLRNQvaLVSQNvhlfndTIANNIAYARTEQYSREQIEEAarMAYAMDFINKMDNGLDTVigengVLL 481
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1411607396 442 SGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVET 475
Cdd:PRK11176  482 SGGQRQRIAIARALLRDSPILILDEATSALDTES 515
PLN03130 PLN03130
ABC transporter C family member; Provisional
330-472 6.21e-04

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 43.19  E-value: 6.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  330 GDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRG--LVKGGTkleVAYFDQYRDQLDpeQTVMDNVGEG 407
Cdd:PLN03130   628 AERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDasVVIRGT---VAYVPQVSWIFN--ATVRDNILFG 702
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  408 KQEVMVR-GRSRHILGYLQDFLFEPKRARTPVKA----LSGGEKNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:PLN03130   703 SPFDPERyERAIDVTALQHDLDLLPGGDLTEIGErgvnISGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
135-229 6.31e-04

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 43.28  E-value: 6.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  135 FETRISQV--LTLLNLDPDATLDSLSGGWLRKVALARALACDPD--LLLLDEPTNHLDIEAINWLEDFLKDFR---GAIV 207
Cdd:PRK00635   453 LKSRLSILidLGLPYLTPERALATLSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRdqgNTVL 532
                           90       100
                   ....*....|....*....|..
gi 1411607396  208 FISHDREFIhKLATRIIDLDRG 229
Cdd:PRK00635   533 LVEHDEQMI-SLADRIIDIGPG 553
PRK13546 PRK13546
teichoic acids export ABC transporter ATP-binding subunit TagH;
15-278 7.77e-04

teichoic acids export ABC transporter ATP-binding subunit TagH;


Pssm-ID: 184131 [Multi-domain]  Cd Length: 264  Bit Score: 41.73  E-value: 7.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  15 DFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMVQQQDLKVTRLeqDPPASSDLTVFDYTAEGLAGV 94
Cdd:PRK13546   36 TFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAI--SAGLSGQLTGIENIEFKMLCM 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  95 GELLKKYHHISMELAHdpsdaniriMSDLQEQLdYQngwqfetrisqvltllnldpdaTLDSLSGGWLRKVALARALACD 174
Cdd:PRK13546  114 GFKRKEIKAMTPKIIE---------FSELGEFI-YQ----------------------PVKKYSSGMRAKLGFSINITVN 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 175 PDLLLLDEPTNHLDIEAINWLEDFLKDFRGA---IVFISHDREFIHKLATRIIDLDRGVITSWpGNYDEYLQGKEEALRv 251
Cdd:PRK13546  162 PDILVIDEALSVGDQTFAQKCLDKIYEFKEQnktIFFVSHNLGQVRQFCTKIAWIEGGKLKDY-GELDDVLPKYEAFLN- 239
                         250       260
                  ....*....|....*....|....*..
gi 1411607396 252 eelqhaEFDRKLAQEEVWVRQGIKARR 278
Cdd:PRK13546  240 ------DFKKKSKAEQKEFRNKLDESR 260
PRK01156 PRK01156
chromosome segregation protein; Provisional
154-214 7.88e-04

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 42.58  E-value: 7.88e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1411607396 154 LDSLSGG------WLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDF----LKDFRG--AIVFISHDRE 214
Cdd:PRK01156  799 IDSLSGGektavaFALRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKDIieysLKDSSDipQVIMISHHRE 871
PRK13541 PRK13541
cytochrome c biogenesis protein CcmA; Provisional
36-227 8.86e-04

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184128 [Multi-domain]  Cd Length: 195  Bit Score: 41.01  E-value: 8.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  36 GRNGAGKSTLMKIIAGELPLDDGRMVQQ-------QDLKVTRLEQDPPASSDLTVFDYtaeglagvgelLKKYHHISMEL 108
Cdd:PRK13541   33 GANGCGKSSLLRMIAGIMQPSSGNIYYKncninniAKPYCTYIGHNLGLKLEMTVFEN-----------LKFWSEIYNSA 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 109 AHDPSDANIRIMSDLQEQLDYqngwqfetrisqvltllnldpdatldSLSGGWLRKVALARALACDPDLLLLDEPTNHLD 188
Cdd:PRK13541  102 ETLYAAIHYFKLHDLLDEKCY--------------------------SLSSGMQKIVAIARLIACQSDLWLLDEVETNLS 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1411607396 189 IEAINWLEDF--LKDFRGAIVFISHDREFIHKLAtRIIDLD 227
Cdd:PRK13541  156 KENRDLLNNLivMKANSGGIVLLSSHLESSIKSA-QILQLD 195
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
321-377 9.39e-04

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


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 41.51  E-value: 9.39e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1411607396 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK 377
Cdd:PRK11300    7 SVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIL 63
COG3950 COG3950
Predicted ATP-binding protein involved in virulence [General function prediction only];
11-187 2.11e-03

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


Pssm-ID: 443150 [Multi-domain]  Cd Length: 276  Bit Score: 40.37  E-value: 2.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  11 LSFSDFPLLDNAELSIERGERL-CLVGRNGAGKSTLMKIIA---------------GELPLDDGRMVQQQDL----KVTR 70
Cdd:COG3950     6 LTIENFRGFEDLEIDFDNPPRLtVLVGENGSGKTTLLEAIAlalsgllsrlddvkfRKLLIRNGEFGDSAKLilyyGTSR 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  71 LEQDPPASSDLTVFDYTAEGLAGVGELLKkyhhismelahdpSDANIR----IMSDLQEQLDYQNGWQFETRISQVLTLL 146
Cdd:COG3950    86 LLLDGPLKKLERLKEEYFSRLDGYDSLLD-------------EDSNLRefleWLREYLEDLENKLSDELDEKLEAVREAL 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1411607396 147 N-LDPDA----------------------TLDSLSGG------W----LRKVALARALACDPD----LLLLDEPTNHL 187
Cdd:COG3950   153 NkLLPDFkdiridrdpgrlvildkngeelPLNQLSDGersllaLvgdlARRLAELNPALENPLegegIVLIDEIDLHL 230
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
158-261 2.19e-03

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 40.87  E-value: 2.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 158 SGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDF--RGAIVFISHD-REFIHKLATRIIDLDRGVITSw 234
Cdd:NF000106  146 SGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMvrDGATVLLTTQyMEEAEQLAHELTVIDRGRVIA- 224
                          90       100
                  ....*....|....*....|....*....
gi 1411607396 235 PGNYDEyLQGK--EEALRVEELQHAEFDR 261
Cdd:NF000106  225 DGKVDE-LKTKvgGRTLQIRPAHAAELDR 252
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
309-377 2.23e-03

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 40.80  E-value: 2.23e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1411607396 309 MDDVNRSGKLVFETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK 377
Cdd:PRK15439    1 MQTSDTTAPPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLE 69
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
331-473 2.42e-03

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 40.84  E-value: 2.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 331 DRTLFQGLDLQVLRGDKIALVGPNGCGKS----TLIKLL--------------LGQ--LEPSRGLVKG--GTKLEVAyFD 388
Cdd:PRK15134   21 VRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLpsppvvypsgdirfHGEslLHASEQTLRGvrGNKIAMI-FQ 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 389 QYRDQLDPEQTVMdnvgegKQ--EVMV--RGRSR-----HILGYLQDFLFE--PKRARTPVKALSGGEKNRLLLAKLFLK 457
Cdd:PRK15134  100 EPMVSLNPLHTLE------KQlyEVLSlhRGMRReaargEILNCLDRVGIRqaAKRLTDYPHQLSGGERQRVMIAMALLT 173
                         170
                  ....*....|....*.
gi 1411607396 458 PSNLLILDEPTNDLDV 473
Cdd:PRK15134  174 RPELLIADEPTTALDV 189
AAA_21 pfam13304
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ...
33-268 2.94e-03

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: 40.07  E-value: 2.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  33 CLVGRNGAGKSTLMKII---------AGELPLDDGRMVQQQDLKVTRLEQDPPASSDLTVFDYTAEGLAGVGELLKKYHH 103
Cdd:pfam13304   3 VLIGPNGSGKSNLLEALrfladfdalVIGLTDERSRNGGIGGIPSLLNGIDPKEPIEFEISEFLEDGVRYRYGLDLERED 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 104 ISMELAHDPSDANIRIMSDLQEQLDYQNGWQFETRISQVLTLLNLDPDAtldslsggwlrkVALARALACDPDLLLLDEP 183
Cdd:pfam13304  83 VEEKLSSKPTLLEKRLLLREDSEEREPKFPPEAEELRLGLDVEERIELS------------LSELSDLISGLLLLSIISP 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 184 TNHLDIEAINWLEDFLKDFRGA--IVFISHDREFIHKLATRIIDLDRGVITSWPGNYDEYLQGKEEALRVEELQHAEFDR 261
Cdd:pfam13304 151 LSFLLLLDEGLLLEDWAVLDLAadLALFPDLKELLQRLVRGLKLADLNLSDLGEGIEKSLLVDDRLRERGLILLENGGGG 230

                  ....*..
gi 1411607396 262 KLAQEEV 268
Cdd:pfam13304 231 ELPAFEL 237
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
156-226 3.42e-03

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


Pssm-ID: 273184 [Multi-domain]  Cd Length: 925  Bit Score: 40.77  E-value: 3.42e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1411607396 156 SLSGGWLRKVALARAL---ACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRGA---IVFISHDREFIhKLATRIIDL 226
Cdd:TIGR00630 829 TLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKgntVVVIEHNLDVI-KTADYIIDL 904
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
349-471 3.46e-03

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 40.48  E-value: 3.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 349 ALVGPNGCGKSTLIKLLLGQLEPSRG--LVKG------GTK--LE--VAYFDQYRDQLDpEQTVMDNVGEGK-------- 408
Cdd:PRK10982   28 ALMGENGAGKSTLLKCLFGIYQKDSGsiLFQGkeidfkSSKeaLEngISMVHQELNLVL-QRSVMDNMWLGRyptkgmfv 106
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1411607396 409 -QEVMVRgRSRHILGYLqDFLFEPkraRTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDL 471
Cdd:PRK10982  107 dQDKMYR-DTKAIFDEL-DIDIDP---RAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL 165
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
325-475 3.63e-03

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 39.69  E-value: 3.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 325 LGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGL-VKGGTKLEVAYFDQYRDQLDPEQ----- 398
Cdd:PRK14271   27 LTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYrYSGDVLLGGRSIFNYRDVLEFRRrvgml 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 399 ---------TVMDNVGEGKQEVMVRGRsRHILGYLQDFLFE--------PKRARTPVKaLSGGEKNRLLLAKLFLKPSNL 461
Cdd:PRK14271  107 fqrpnpfpmSIMDNVLAGVRAHKLVPR-KEFRGVAQARLTEvglwdavkDRLSDSPFR-LSGGQQQLLCLARTLAVNPEV 184
                         170
                  ....*....|....
gi 1411607396 462 LILDEPTNDLDVET 475
Cdd:PRK14271  185 LLLDEPTSALDPTT 198
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
152-191 4.01e-03

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 40.10  E-value: 4.01e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1411607396 152 ATLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEA 191
Cdd:PRK10982  387 TQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGA 426
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
437-471 4.61e-03

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


Pssm-ID: 273184 [Multi-domain]  Cd Length: 925  Bit Score: 40.00  E-value: 4.61e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1411607396 437 PVKALSGGEKNRLLLAKLFLKPSN---LLILDEPTNDL 471
Cdd:TIGR00630 826 PATTLSGGEAQRIKLAKELSKRSTgrtLYILDEPTTGL 863
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
439-472 4.74e-03

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 40.40  E-value: 4.74e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1411607396  439 KALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:PTZ00265  1357 KSLSGGQKQRIAIARALLREPKILLLDEATSSLD 1390
cbiO PRK13646
energy-coupling factor transporter ATPase;
338-504 4.86e-03

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 39.38  E-value: 4.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 338 LDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKGG-----TKLEVAYFDQYRDQLD-----PE-QTVMDNVge 406
Cdd:PRK13646   26 VNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDdititHKTKDKYIRPVRKRIGmvfqfPEsQLFEDTV-- 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 407 gKQEVM------------VRGRSRHIL---GYLQDFLfepkrARTPVKaLSGGEKNRLLLAKLFLKPSNLLILDEPTNDL 471
Cdd:PRK13646  104 -EREIIfgpknfkmnldeVKNYAHRLLmdlGFSRDVM-----SQSPFQ-MSGGQMRKIAIVSILAMNPDIIVLDEPTAGL 176
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1411607396 472 D----VETLELLEELLADYPGTLLLVSHDR----RFIDNTV 504
Cdd:PRK13646  177 DpqskRQVMRLLKSLQTDENKTIILVSHDMnevaRYADEVI 217
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
157-231 4.87e-03

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: 39.80  E-value: 4.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 157 LSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAinwlEdflKDFRGAIVFISHDREFI---HKLAT-----RIIDLDR 228
Cdd:COG5265   495 LSGGEKQRVAIARTLLKNPPILIFDEATSALDSRT----E---RAIQAALREVARGRTTLviaHRLSTivdadEILVLEA 567

                  ...
gi 1411607396 229 GVI 231
Cdd:COG5265   568 GRI 570
PRK13546 PRK13546
teichoic acids export ABC transporter ATP-binding subunit TagH;
336-466 5.79e-03

teichoic acids export ABC transporter ATP-binding subunit TagH;


Pssm-ID: 184131 [Multi-domain]  Cd Length: 264  Bit Score: 39.03  E-value: 5.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 336 QGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKGGTKLEVAYFDQyrdQLDPEQTVMDNVgEGKQEVM--- 412
Cdd:PRK13546   41 DDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAISA---GLSGQLTGIENI-EFKMLCMgfk 116
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1411607396 413 ---VRGRSRHILGY--LQDFLFEpkrartPVKALSGGEKNRLLLAKLFLKPSNLLILDE 466
Cdd:PRK13546  117 rkeIKAMTPKIIEFseLGEFIYQ------PVKKYSSGMRAKLGFSINITVNPDILVIDE 169
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
349-473 5.85e-03

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 39.47  E-value: 5.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 349 ALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTKLevayFDQYRD-QLDPEQ----------------TVMDNVGEGKQE 410
Cdd:PRK11144   28 AIFGRSGAGKTSLINAISGLTRPQKGRIVlNGRVL----FDAEKGiCLPPEKrrigyvfqdarlfphyKVRGNLRYGMAK 103
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1411607396 411 VMvRGRSRHILGYLQdflFEPKRARTPVkALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDV 473
Cdd:PRK11144  104 SM-VAQFDKIVALLG---IEPLLDRYPG-SLSGGEKQRVAIGRALLTAPELLLMDEPLASLDL 161
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
14-188 7.32e-03

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


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 39.31  E-value: 7.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  14 SDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGrMVQQQDLKVTRLEQDP----PASSDLTVF---DY 86
Cdd:PRK10789  326 TDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEG-DIRFHDIPLTKLQLDSwrsrLAVVSQTPFlfsDT 404
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396  87 TAEGLAgvgelLKKYHHISMELAHDPSDANIRimsdlQEQLDYQNGWQFETRISQVLtllnldpdatldsLSGGWLRKVA 166
Cdd:PRK10789  405 VANNIA-----LGRPDATQQEIEHVARLASVH-----DDILRLPQGYDTEVGERGVM-------------LSGGQKQRIS 461
                         170       180
                  ....*....|....*....|..
gi 1411607396 167 LARALACDPDLLLLDEPTNHLD 188
Cdd:PRK10789  462 IARALLLNAEILILDDALSAVD 483
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
437-471 7.72e-03

ATP-binding cassette domain II 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: 213238 [Multi-domain]  Cd Length: 261  Bit Score: 38.75  E-value: 7.72e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1411607396 437 PVKALSGGEKNRLLLAKLFLKPSN---LLILDEPTNDL 471
Cdd:cd03271   166 PATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGL 203
AAA_21 pfam13304
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ...
153-216 8.63e-03

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: 38.52  E-value: 8.63e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 153 TLDSLSGGWLRKVALARALACD---PDLLLLDEPTNHLDIEAINWLEDFLKDF---RGAIVFISHDREFI 216
Cdd:pfam13304 233 PAFELSDGTKRLLALLAALLSAlpkGGLLLIDEPESGLHPKLLRRLLELLKELsrnGAQLILTTHSPLLL 302
 
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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