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Conserved domains on  [gi|808356654|ref|NP_001293855|]
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ABC transporter domain-containing protein [Caenorhabditis elegans]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
P-loop_NTPase super family cl38936
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...
 411-590 5.06e-20

P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.


The actual alignment was detected with superfamily member cd03225:

Pssm-ID: 476819 [Multi-domain]  Cd Length: 211  Bit Score: 90.22  E-value: 5.06e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  411 KQVSLTVHLGEVVTLYGHHGCGSGEILSIIAGQMKPEYGEVMMEQSqrplmiskttdvpNVNYLNVIQYLRLIS------ 484
Cdd:cd03225    18 DDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGK-------------DLTKLSLKELRRKVGlvfqnp 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  485 -----------------KMRGVSASTSH--IDEMLEELDLIKVKNRSLDLLSTTQKERLRIAAVFVGQPDLVLIDFPTME 545
Cdd:cd03225    85 ddqffgptveeevafglENLGLPEEEIEerVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAG 164

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 808356654  546 CLPEWKFMVFRFIEK-RKEKRSIIVSSYDPEETEAISDKVVLMSEG 590
Cdd:cd03225   165 LDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLELADRVIVLEDG 210
rim_protein super family cl31083
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
 177-597 2.22e-18

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]


The actual alignment was detected with superfamily member TIGR01257:

Pssm-ID: 130324 [Multi-domain]  Cd Length: 2272  Bit Score: 92.00  E-value: 2.22e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654   177 LHARRFHYFIAKFVFWYGIALIISLIVFivnvlvvpAVFCSTYLQFVVCYAAC--IISFAIFLattfPGSPLFA------ 248
Cdd:TIGR01257  720 MHGRILHYSDPFILFLFLLAFSTATIMQ--------CFLLSTFFSKASLAAACsgVIYFTLYL----PHILCFAwqdrmt 787

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654   249 ----KIVGFLSMVAgeFGFGTVY------HGIGffqLCVRHFGKSEFDGPWIDAVCTL-CMTGNCVLLITVSIYFDTYFC 317
Cdd:TIGR01257  788 adlkTAVSLLSPVA--FGFGTEYlvrfeeQGLG---LQWSNIGNSPLEGDEFSFLLSMkMMLLDAALYGLLAWYLDQVFP 862

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654   318 LFTMEPLAFYFPLEKDYWMP-EARSPQLDTFFVKqiillkpgrSEITVKKAHDEILPA--KTSTGSKYIPPTpivkgVPL 394
Cdd:TIGR01257  863 GDYGTPLPWYFLLQESYWLGgEGCSTREERALEK---------TEPLTEEMEDPEHPEgiNDSFFERELPGL-----VPG 928

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654   395 VVLYGICKRIENHWR--VKQVSLTVHLGEVVTLYGHHGCGSGEILSIIAGQMKPEYGEVMMEQSQrplmISKTTDV---- 468
Cdd:TIGR01257  929 VCVKNLVKIFEPSGRpaVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKD----IETNLDAvrqs 1004

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654   469 ----PNVN----YLNVIQYLRLISKMRGVSASTSHID--EMLEELDLIKVKNRSLDLLSTTQKERLRIAAVFVGQPDLVL 538
Cdd:TIGR01257 1005 lgmcPQHNilfhHLTVAEHILFYAQLKGRSWEEAQLEmeAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVV 1084

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 808356654   539 IDFPTMECLPEWKFMVFRFIEKRKEKRSIIVSSYDPEETEAISDKVVLMSEGYVVLNGS 597
Cdd:TIGR01257 1085 LDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGT 1143
ABC2_membrane_3 super family cl38365
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ...
 901-1097 5.79e-04

ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter family pfam01061.


The actual alignment was detected with superfamily member pfam12698:

Pssm-ID: 463674 [Multi-domain]  Cd Length: 345  Bit Score: 43.92  E-value: 5.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654   901 SYSLMYITAVFQMFVYTFSVVLPLRLVSTNMGPQSMILPWPRYVYFGFIYVFQLVVFLVIAIILGFAVLSMGFFATNtts 980
Cdd:pfam12698  161 YYLVGLILMIIILIGAAIIAVSIVEEKESRIKERLLVSGVSPLQYWLGKILGDFLVGLLQLLIILLLLFGIGIPFGN--- 237

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654   981 cYLRFLSAWFLSYASTLPLIYFLVFNIQNTKSVIPIILAISSLSVTFpnLVASFSAENqvsLQSLIQFVSwscMLNPPSS 1060
Cdd:pfam12698  238 -LGLLLLLFLLYGLAYIALGYLLGSLFKNSEDAQSIIGIVILLLSGF--FGGLFPLED---PPSFLQWIF---SIIPFFS 308

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 808356654  1061 LQVLAAFLNAGESLEKNSGTITSLILFCGAQFWIIVI 1097
Cdd:pfam12698  309 PIDGLLRLIYGDSLWEIAPSLIILLLFAVVLLLLALL 345
 
Name Accession Description Interval E-value
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
 411-590 5.06e-20

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: 90.22  E-value: 5.06e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  411 KQVSLTVHLGEVVTLYGHHGCGSGEILSIIAGQMKPEYGEVMMEQSqrplmiskttdvpNVNYLNVIQYLRLIS------ 484
Cdd:cd03225    18 DDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGK-------------DLTKLSLKELRRKVGlvfqnp 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  485 -----------------KMRGVSASTSH--IDEMLEELDLIKVKNRSLDLLSTTQKERLRIAAVFVGQPDLVLIDFPTME 545
Cdd:cd03225    85 ddqffgptveeevafglENLGLPEEEIEerVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAG 164

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 808356654  546 CLPEWKFMVFRFIEK-RKEKRSIIVSSYDPEETEAISDKVVLMSEG 590
Cdd:cd03225   165 LDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLELADRVIVLEDG 210
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
 177-597 2.22e-18

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: 92.00  E-value: 2.22e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654   177 LHARRFHYFIAKFVFWYGIALIISLIVFivnvlvvpAVFCSTYLQFVVCYAAC--IISFAIFLattfPGSPLFA------ 248
Cdd:TIGR01257  720 MHGRILHYSDPFILFLFLLAFSTATIMQ--------CFLLSTFFSKASLAAACsgVIYFTLYL----PHILCFAwqdrmt 787

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654   249 ----KIVGFLSMVAgeFGFGTVY------HGIGffqLCVRHFGKSEFDGPWIDAVCTL-CMTGNCVLLITVSIYFDTYFC 317
Cdd:TIGR01257  788 adlkTAVSLLSPVA--FGFGTEYlvrfeeQGLG---LQWSNIGNSPLEGDEFSFLLSMkMMLLDAALYGLLAWYLDQVFP 862

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654   318 LFTMEPLAFYFPLEKDYWMP-EARSPQLDTFFVKqiillkpgrSEITVKKAHDEILPA--KTSTGSKYIPPTpivkgVPL 394
Cdd:TIGR01257  863 GDYGTPLPWYFLLQESYWLGgEGCSTREERALEK---------TEPLTEEMEDPEHPEgiNDSFFERELPGL-----VPG 928

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654   395 VVLYGICKRIENHWR--VKQVSLTVHLGEVVTLYGHHGCGSGEILSIIAGQMKPEYGEVMMEQSQrplmISKTTDV---- 468
Cdd:TIGR01257  929 VCVKNLVKIFEPSGRpaVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKD----IETNLDAvrqs 1004

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654   469 ----PNVN----YLNVIQYLRLISKMRGVSASTSHID--EMLEELDLIKVKNRSLDLLSTTQKERLRIAAVFVGQPDLVL 538
Cdd:TIGR01257 1005 lgmcPQHNilfhHLTVAEHILFYAQLKGRSWEEAQLEmeAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVV 1084

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 808356654   539 IDFPTMECLPEWKFMVFRFIEKRKEKRSIIVSSYDPEETEAISDKVVLMSEGYVVLNGS 597
Cdd:TIGR01257 1085 LDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGT 1143
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 410-543 2.39e-12

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: 66.13  E-value: 2.39e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654   410 VKQVSLTVHLGEVVTLYGHHGCGSGEILSIIAGQMKPEYGEV----------MMEQSQRPL-MIS-KTTDVPNV-NYLNV 476
Cdd:pfam00005    1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTIlldgqdltddERKSLRKEIgYVFqDPQLFPRLtVRENL 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 808356654   477 IQYLRLISKMRgvSASTSHIDEMLEELDLIKVKNRSLDL----LSTTQKERLRIAAVFVGQPDLVLIDFPT 543
Cdd:pfam00005   81 RLGLLLKGLSK--REKDARAEEALEKLGLGDLADRPVGErpgtLSGGQRQRVAIARALLTKPKLLLLDEPT 149
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
395-609 3.58e-12

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 69.75  E-value: 3.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  395 VVLYGICKRIENHWRVKQVSLTVHLGEVVTLYGHHGCGSGEILSIIAGQMKPEYGEVMME---------QSQRPLMISKT 465
Cdd:PRK11432    7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDgedvthrsiQQRDICMVFQS 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  466 TDV-PNVNYLNVIQY-LrlisKMRGVSAS--TSHIDEMLEELDLIKVKNRSLDLLSTTQKERLRIAAVFVGQPDLVLIDF 541
Cdd:PRK11432   87 YALfPHMSLGENVGYgL----KMLGVPKEerKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDE 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 808356654  542 PtmecLPEWKFMVFRFI-EKRKE--KRSIIVSSY---DPEETEAISDKVVLMSEGYVVLNGSCEAFKHSINSVF 609
Cdd:PRK11432  163 P----LSNLDANLRRSMrEKIRElqQQFNITSLYvthDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRF 232
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
 410-601 9.85e-11

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: 66.08  E-value: 9.85e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  410 VKQVSLTVHLGEVVTLYGHHGCG-SGEILSI---------IAGQMKPEyGEVMMEQSQRPL-----MISKTTDVpNVNYL 474
Cdd:COG1123    22 VDGVSLTIAPGETVALVGESGSGkSTLALALmgllphggrISGEVLLD-GRDLLELSEALRgrrigMVFQDPMT-QLNPV 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  475 NVIQYLRLISKMRGVSASTSH--IDEMLEELDLIKVKNRSLDLLSTTQKERLRIAAVFVGQPDLVLIDFPTMECLPEWKF 552
Cdd:COG1123   100 TVGDQIAEALENLGLSRAEARarVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQA 179

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 808356654  553 MVFRFIEK--RKEKRSIIVSSYDPEETEAISDKVVLMSEGYVVLNGSCEAF 601
Cdd:COG1123   180 EILDLLRElqRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
 410-603 1.36e-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: 53.48  E-value: 1.36e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654   410 VKQVSLTVHLGEVVTLYGHHGCGSGEILSIIAGQMKPEYGEVMMEQSQrplMISKTTDV-PNVNY----------LNVIQ 478
Cdd:TIGR01257 1955 VDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKS---ILTNISDVhQNMGYcpqfdaiddlLTGRE 2031

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654   479 YLRLISKMRGVSAStsHIDEM----LEELDLIKVKNRSLDLLSTTQKERLRIAAVFVGQPDLVLIDFPTMECLPEWKFMV 554
Cdd:TIGR01257 2032 HLYLYARLRGVPAE--EIEKVanwsIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRML 2109

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 808356654   555 FRFIEK-RKEKRSIIVSSYDPEETEAISDKVVLMSEGYVVLNGSCEAFKH 603
Cdd:TIGR01257 2110 WNTIVSiIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKS 2159
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
497-605 1.48e-04

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 45.88  E-value: 1.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  497 DEMLEELDLIKVKNRSLDLLSTTQKERLRIAAVFVGQPDLVLIDFPTMECLPEWKFMVFRFIEKR-KEKRSIIVSSYDPE 575
Cdd:NF000106  126 DELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMvRDGATVLLTTQYME 205

                          90       100       110
                  ....*....|....*....|....*....|
gi 808356654  576 ETEAISDKVVLMSEGYVVLNGSCEAFKHSI 605
Cdd:NF000106  206 EAEQLAHELTVIDRGRVIADGKVDELKTKV 235
ABC2_membrane_3 pfam12698
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ...
 901-1097 5.79e-04

ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter family pfam01061.


Pssm-ID: 463674 [Multi-domain]  Cd Length: 345  Bit Score: 43.92  E-value: 5.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654   901 SYSLMYITAVFQMFVYTFSVVLPLRLVSTNMGPQSMILPWPRYVYFGFIYVFQLVVFLVIAIILGFAVLSMGFFATNtts 980
Cdd:pfam12698  161 YYLVGLILMIIILIGAAIIAVSIVEEKESRIKERLLVSGVSPLQYWLGKILGDFLVGLLQLLIILLLLFGIGIPFGN--- 237

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654   981 cYLRFLSAWFLSYASTLPLIYFLVFNIQNTKSVIPIILAISSLSVTFpnLVASFSAENqvsLQSLIQFVSwscMLNPPSS 1060
Cdd:pfam12698  238 -LGLLLLLFLLYGLAYIALGYLLGSLFKNSEDAQSIIGIVILLLSGF--FGGLFPLED---PPSFLQWIF---SIIPFFS 308

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 808356654  1061 LQVLAAFLNAGESLEKNSGTITSLILFCGAQFWIIVI 1097
Cdd:pfam12698  309 PIDGLLRLIYGDSLWEIAPSLIILLLFAVVLLLLALL 345
NosY COG1277
ABC-type transport system involved in multi-copper enzyme maturation, permease component ...
 160-254 2.72e-03

ABC-type transport system involved in multi-copper enzyme maturation, permease component [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440888 [Multi-domain]  Cd Length: 201  Bit Score: 40.57  E-value: 2.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  160 DLWNNDRSSGYYNMFLSLHARRFHYFIAKFVFWYGIALIISLIVFIVNVLVVPAVFCST------YLQFV---VCYAACI 230
Cdd:COG1277    71 DAISGERESGTLELLLTLPISRWEIVLGKFLGALLVLLLALLITFLLALLLGLLLFGSPppdlgaILGFYlglLLLGLAF 150

                          90       100
                  ....*....|....*....|....
gi 808356654  231 ISFAIFLATTFpGSPLFAKIVGFL 254
Cdd:COG1277   151 LAIGLFISALT-RNQIVAAILAIA 173
 
Name Accession Description Interval E-value
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
 411-590 5.06e-20

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: 90.22  E-value: 5.06e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  411 KQVSLTVHLGEVVTLYGHHGCGSGEILSIIAGQMKPEYGEVMMEQSqrplmiskttdvpNVNYLNVIQYLRLIS------ 484
Cdd:cd03225    18 DDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGK-------------DLTKLSLKELRRKVGlvfqnp 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  485 -----------------KMRGVSASTSH--IDEMLEELDLIKVKNRSLDLLSTTQKERLRIAAVFVGQPDLVLIDFPTME 545
Cdd:cd03225    85 ddqffgptveeevafglENLGLPEEEIEerVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAG 164

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 808356654  546 CLPEWKFMVFRFIEK-RKEKRSIIVSSYDPEETEAISDKVVLMSEG 590
Cdd:cd03225   165 LDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLELADRVIVLEDG 210
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
 177-597 2.22e-18

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: 92.00  E-value: 2.22e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654   177 LHARRFHYFIAKFVFWYGIALIISLIVFivnvlvvpAVFCSTYLQFVVCYAAC--IISFAIFLattfPGSPLFA------ 248
Cdd:TIGR01257  720 MHGRILHYSDPFILFLFLLAFSTATIMQ--------CFLLSTFFSKASLAAACsgVIYFTLYL----PHILCFAwqdrmt 787

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654   249 ----KIVGFLSMVAgeFGFGTVY------HGIGffqLCVRHFGKSEFDGPWIDAVCTL-CMTGNCVLLITVSIYFDTYFC 317
Cdd:TIGR01257  788 adlkTAVSLLSPVA--FGFGTEYlvrfeeQGLG---LQWSNIGNSPLEGDEFSFLLSMkMMLLDAALYGLLAWYLDQVFP 862

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654   318 LFTMEPLAFYFPLEKDYWMP-EARSPQLDTFFVKqiillkpgrSEITVKKAHDEILPA--KTSTGSKYIPPTpivkgVPL 394
Cdd:TIGR01257  863 GDYGTPLPWYFLLQESYWLGgEGCSTREERALEK---------TEPLTEEMEDPEHPEgiNDSFFERELPGL-----VPG 928

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654   395 VVLYGICKRIENHWR--VKQVSLTVHLGEVVTLYGHHGCGSGEILSIIAGQMKPEYGEVMMEQSQrplmISKTTDV---- 468
Cdd:TIGR01257  929 VCVKNLVKIFEPSGRpaVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKD----IETNLDAvrqs 1004

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654   469 ----PNVN----YLNVIQYLRLISKMRGVSASTSHID--EMLEELDLIKVKNRSLDLLSTTQKERLRIAAVFVGQPDLVL 538
Cdd:TIGR01257 1005 lgmcPQHNilfhHLTVAEHILFYAQLKGRSWEEAQLEmeAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVV 1084

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 808356654   539 IDFPTMECLPEWKFMVFRFIEKRKEKRSIIVSSYDPEETEAISDKVVLMSEGYVVLNGS 597
Cdd:TIGR01257 1085 LDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGT 1143
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
 395-619 9.47e-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: 81.13  E-value: 9.47e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  395 VVLYGICKRIENHWRVKQVSLTVHLGEVVTLYGHHGCGSGEILSIIAGQMKPEYGEVMMEqsQRPLmisktTDVP----N 470
Cdd:cd03300     1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLD--GKDI-----TNLPphkrP 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  471 VN----------YLNVIQYLRLISKMRGVSAST--SHIDEMLEELDLIKVKNRSLDLLSTTQKERLRIAAVFVGQPDLVL 538
Cdd:cd03300    74 VNtvfqnyalfpHLTVFENIAFGLRLKKLPKAEikERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  539 IDFPTMEC---LPEWKFMVFRFIEKRKEKRSIIVsSYDPEETEAISDKVVLMSEGYVVLNGSCEafkhsinsvfEIRIWP 615
Cdd:cd03300   154 LDEPLGALdlkLRKDMQLELKRLQKELGITFVFV-THDQEEALTMSDRIAVMNKGKIQQIGTPE----------EIYEEP 222


                  ....
gi 808356654  616 NNRF 619
Cdd:cd03300   223 ANRF 226
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
 399-596 5.07e-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: 78.48  E-value: 5.07e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  399 GICKRIENHWRVKQVSLTVHLGEVVTLYGHHGCGSGEILSIIAGQMKPEYGEVMMEQSqrPLMISKTTDvpnVNYL---- 474
Cdd:cd03269     5 NVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGK--PLDIAARNR---IGYLpeer 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  475 ------NVIQYLRLISKMRGVSAS--TSHIDEMLEELDLIKVKNRSLDLLSTTQKERLRIAAVFVGQPDLVLIDFPTMEC 546
Cdd:cd03269    80 glypkmKVIDQLVYLAQLKGLKKEeaRRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGL 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 808356654  547 LPEWKFMVFRFI-EKRKEKRSIIVSSYDPEETEAISDKVVLMSEGYVVLNG 596
Cdd:cd03269   160 DPVNVELLKDVIrELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
 395-596 5.19e-16

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: 78.33  E-value: 5.19e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  395 VVLYGICKRIENHWRVKQVSLTVHLGEVVTLYGHHGCGSGEILSIIAGQMKPEYGEVMMeqSQRPLmisktTDVP----N 470
Cdd:cd03259     1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILI--DGRDV-----TGVPperrN 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  471 VNY----------LNVIQYLRLISKMRGVSASTSH--IDEMLEELDLIKVKNRSLDLLSTTQKERLRIAAVFVGQPDLVL 538
Cdd:cd03259    74 IGMvfqdyalfphLTVAENIAFGLKLRGVPKAEIRarVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLL 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 808356654  539 IDFP--------TMECLPEWKfmvfRFIekRKEKRSIIVSSYDPEETEAISDKVVLMSEGYVVLNG 596
Cdd:cd03259   154 LDEPlsaldaklREELREELK----ELQ--RELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
 399-590 6.61e-16

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: 77.05  E-value: 6.61e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  399 GICKRIENHWRVKQVSLTVHLGEVVTLYGHHGCGSGEILSIIAGQMKPEYGEVMMEQSQrplMISKTTDVP-NVNYlnVI 477
Cdd:cd03230     5 NLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKD---IKKEPEEVKrRIGY--LP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  478 QYLRLISKMRGvsastshiDEMLEeldlikvknrsldlLSTTQKERLRIAAVFVGQPDLVLIDFPTMECLPEWKFMVFRF 557
Cdd:cd03230    80 EEPSLYENLTV--------RENLK--------------LSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWEL 137

                         170       180       190
                  ....*....|....*....|....*....|....
gi 808356654  558 IEK-RKEKRSIIVSSYDPEETEAISDKVVLMSEG 590
Cdd:cd03230   138 LRElKKEGKTILLSSHILEEAERLCDRVAILNNG 171
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
 399-590 5.46e-13

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


Pssm-ID: 213179 [Multi-domain]  Cd Length: 157  Bit Score: 68.04  E-value: 5.46e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  399 GICKRIENHWRVKQVSLTVHLGEVVTLYGHHGCGSGEILSIIAGQMKPEYGEVMMeqsqrplmiskttDVPNVNYLNVIQ 478
Cdd:cd00267     4 NLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILI-------------DGKDIAKLPLEE 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  479 YLRLISkmrgvsastshidemleeldlikvknrSLDLLSTTQKERLRIAAVFVGQPDLVLIDFPT--MEclPEWKFMVFR 556
Cdd:cd00267    71 LRRRIG---------------------------YVPQLSGGQRQRVALARALLLNPDLLLLDEPTsgLD--PASRERLLE 121

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 808356654  557 FIEK-RKEKRSIIVSSYDPEETEAISDKVVLMSEG 590
Cdd:cd00267   122 LLRElAEEGRTVIIVTHDPELAELAADRVIVLKDG 156
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
 399-592 8.92e-13

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: 69.06  E-value: 8.92e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  399 GICKR----IENHWRVKQVSLTVHLGEVVTLYGHHGCGSGEILSIIAGQMKPEYGEV-MMEQSQRPLMISKTTDVPN--- 470
Cdd:cd03255     5 NLSKTygggGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVrVDGTDISKLSEKELAAFRRrhi 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  471 ---------VNYLNVIQYLRLISKMRGVSASTSH--IDEMLEELDLIKVKNRSLDLLSTTQKERLRIAAVFVGQPDLVLI 539
Cdd:cd03255    85 gfvfqsfnlLPDLTALENVELPLLLAGVPKKERRerAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILA 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 808356654  540 DFPTMECLPEWKFMVFRFIEK--RKEKRSIIVSSYDPEETEaISDKVVLMSEGYV 592
Cdd:cd03255   165 DEPTGNLDSETGKEVMELLRElnKEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
 397-599 1.07e-12

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: 69.11  E-value: 1.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  397 LYGICKRIENHWRVKQVSLTVHLGEVVTLYGHHGCGSGEILSIIAGQMKPEYGEVMMEQSQrplmiskTTDVP------- 469
Cdd:cd03218     3 AENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQD-------ITKLPmhkrarl 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  470 NVNYL----------NVIQYLRLISKMRGVSASTSH--IDEMLEELDLIKVKNRSLDLLSTTQKERLRIAAVFVGQPDLV 537
Cdd:cd03218    76 GIGYLpqeasifrklTVEENILAVLEIRGLSKKEREekLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFL 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 808356654  538 LIDFPTMECLPEWKFMVFRFIEKRKEKR-SIIVSSYDPEETEAISDKVVLMSEGYVVLNGSCE 599
Cdd:cd03218   156 LLDEPFAGVDPIAVQDIQKIIKILKDRGiGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPE 218
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
 410-587 1.10e-12

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: 68.71  E-value: 1.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  410 VKQVSLTVHLGEVVTLYGHHGCGSGEILSIIAGQMKPEYGEVMM---EQSQRPLMISKttdVP---NVNY---LNVIQY- 479
Cdd:cd03235    15 LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVfgkPLEKERKRIGY---VPqrrSIDRdfpISVRDVv 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  480 -LRLISKM---RGVSASTSH-IDEMLEELDLIKVKNRSLDLLSTTQKERLRIAAVFVGQPDLVLIDFPTMECLPEWKFMV 554
Cdd:cd03235    92 lMGLYGHKglfRRLSKADKAkVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDI 171

                         170       180       190
                  ....*....|....*....|....*....|....
gi 808356654  555 FRFIEK-RKEKRSIIVSSYDPEETEAISDKVVLM 587
Cdd:cd03235   172 YELLRElRREGMTILVVTHDLGLVLEYFDRVLLL 205
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 410-543 2.39e-12

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: 66.13  E-value: 2.39e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654   410 VKQVSLTVHLGEVVTLYGHHGCGSGEILSIIAGQMKPEYGEV----------MMEQSQRPL-MIS-KTTDVPNV-NYLNV 476
Cdd:pfam00005    1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTIlldgqdltddERKSLRKEIgYVFqDPQLFPRLtVRENL 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 808356654   477 IQYLRLISKMRgvSASTSHIDEMLEELDLIKVKNRSLDL----LSTTQKERLRIAAVFVGQPDLVLIDFPT 543
Cdd:pfam00005   81 RLGLLLKGLSK--REKDARAEEALEKLGLGDLADRPVGErpgtLSGGQRQRVAIARALLTKPKLLLLDEPT 149
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
395-609 3.58e-12

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 69.75  E-value: 3.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  395 VVLYGICKRIENHWRVKQVSLTVHLGEVVTLYGHHGCGSGEILSIIAGQMKPEYGEVMME---------QSQRPLMISKT 465
Cdd:PRK11432    7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDgedvthrsiQQRDICMVFQS 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  466 TDV-PNVNYLNVIQY-LrlisKMRGVSAS--TSHIDEMLEELDLIKVKNRSLDLLSTTQKERLRIAAVFVGQPDLVLIDF 541
Cdd:PRK11432   87 YALfPHMSLGENVGYgL----KMLGVPKEerKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDE 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 808356654  542 PtmecLPEWKFMVFRFI-EKRKE--KRSIIVSSY---DPEETEAISDKVVLMSEGYVVLNGSCEAFKHSINSVF 609
Cdd:PRK11432  163 P----LSNLDANLRRSMrEKIRElqQQFNITSLYvthDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRF 232
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
 410-596 5.19e-12

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: 67.36  E-value: 5.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  410 VKQVSLTVHLGEVVTLYGHHGCGSGEILSIIAGQMKPEYGEV----MMEQSQRP--------LMISKTT---DVPnvnyl 474
Cdd:cd03267    37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVrvagLVPWKRRKkflrrigvVFGQKTQlwwDLP----- 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  475 nVIQYLRLISKMRGVSAS--TSHIDEMLEELDLIKVKNRSLDLLSTTQKERLRIAAVFVGQPDLVLIDFPTMECLPEWKF 552
Cdd:cd03267   112 -VIDSFYLLAAIYDLPPArfKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQE 190

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 808356654  553 MVFRFI--EKRKEKRSIIVSSYDPEETEAISDKVVLMSEGYVVLNG 596
Cdd:cd03267   191 NIRNFLkeYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
 410-588 1.90e-11

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: 65.19  E-value: 1.90e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  410 VKQVSLTVHLGEVVTLYGHHGCGSGEILSIIAGQMKPEYGEVMME-------QSQRPLMISKTTDVPnvnYLNVIQYLRL 482
Cdd:cd03293    20 LEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDgepvtgpGPDRGYVFQQDALLP---WLTVLDNVAL 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  483 ISKMRGVSAS--TSHIDEMLEELDLIKVKNRSLDLLSTTQKERLRIAAVFVGQPDLVLIDFP-------TMECLPEWkfm 553
Cdd:cd03293    97 GLELQGVPKAeaRERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPfsaldalTREQLQEE--- 173

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 808356654  554 vfrfIEK--RKEKRSIIVSSYDPEETEAISDKVVLMS 588
Cdd:cd03293   174 ----LLDiwRETGKTVLLVTHDIDEAVFLADRVVVLS 206
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
 395-593 2.18e-11

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: 64.97  E-value: 2.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  395 VVLYGICKRIENHWRVKQVSLTVHLGEVVTLYGHHGCGSGEILSIIAGQMKPEYGEVMMEQsqrplmiSKTTDVP----N 470
Cdd:cd03301     1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGG-------RDVTDLPpkdrD 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  471 V-----NY-----LNVIQYLRLISKMRGVSASTshIDEMLEE----LDLIKVKNRSLDLLSTTQKERLRIAAVFVGQPDL 536
Cdd:cd03301    74 IamvfqNYalyphMTVYDNIAFGLKLRKVPKDE--IDERVREvaelLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKV 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 808356654  537 VLIDFP--------TMECLPEWKFMvfrfieKRKEKRSIIVSSYDPEETEAISDKVVLMSEGYVV 593
Cdd:cd03301   152 FLMDEPlsnldaklRVQMRAELKRL------QQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQ 210
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
 410-601 9.85e-11

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: 66.08  E-value: 9.85e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  410 VKQVSLTVHLGEVVTLYGHHGCG-SGEILSI---------IAGQMKPEyGEVMMEQSQRPL-----MISKTTDVpNVNYL 474
Cdd:COG1123    22 VDGVSLTIAPGETVALVGESGSGkSTLALALmgllphggrISGEVLLD-GRDLLELSEALRgrrigMVFQDPMT-QLNPV 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  475 NVIQYLRLISKMRGVSASTSH--IDEMLEELDLIKVKNRSLDLLSTTQKERLRIAAVFVGQPDLVLIDFPTMECLPEWKF 552
Cdd:COG1123   100 TVGDQIAEALENLGLSRAEARarVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQA 179

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 808356654  553 MVFRFIEK--RKEKRSIIVSSYDPEETEAISDKVVLMSEGYVVLNGSCEAF 601
Cdd:COG1123   180 EILDLLRElqRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
 399-590 2.18e-10

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: 61.05  E-value: 2.18e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  399 GICKRIENHWRVKQVSLTVHLGEVVTLYGHHGCGSGEILSIIAGQMKPEYGEVMMEQsqRPLMISKTTDVP---NVNYln 475
Cdd:cd03229     5 NVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDG--EDLTDLEDELPPlrrRIGM-- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  476 VIQYLRLISKMrgvsastshidEMLEeldlikvkNRSLdLLSTTQKERLRIAAVFVGQPDLVLIDFPTMECLPEWKFMVF 555
Cdd:cd03229    81 VFQDFALFPHL-----------TVLE--------NIAL-GLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVR 140

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 808356654  556 RFIEKRKEK--RSIIVSSYDPEETEAISDKVVLMSEG 590
Cdd:cd03229   141 ALLKSLQAQlgITVVLVTHDLDEAARLADRVVVLRDG 177
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
393-624 3.60e-10

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 63.70  E-value: 3.60e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  393 PLVVLYGICKRIENHWRVKQVSLTVHLGEVVTLYGHHGCGSGEILSIIAGQMKPEYGEVMMEQS--------QRP--LMI 462
Cdd:PRK11607   18 PLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVdlshvppyQRPinMMF 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  463 SKTTDVPnvnYLNVIQYLRLISKMRGVSAS--TSHIDEMLEELDLIKVKNRSLDLLSTTQKERLRIAAVFVGQPDLVLID 540
Cdd:PRK11607   98 QSYALFP---HMTVEQNIAFGLKQDKLPKAeiASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLD 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  541 FPtMECLPE-----WKFMVFRFIEKRKEkrSIIVSSYDPEETEAISDKVVLMSEGYVVLNGSCEafkhsinsvfEIRIWP 615
Cdd:PRK11607  175 EP-MGALDKklrdrMQLEVVDILERVGV--TCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPE----------EIYEHP 241


                  ....*....
gi 808356654  616 NNRFTDEQI 624
Cdd:PRK11607  242 TTRYSAEFI 250
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
 399-593 4.17e-10

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: 60.13  E-value: 4.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  399 GICKRIENHWRVKQVSLTVHLGEVVTLYGHHGCGSGEILSIIAGQMKPEYGEVMMEQSQrplmiskttdvpnVNYLNVIQ 478
Cdd:cd03216     5 GITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKE-------------VSFASPRD 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  479 YLRLiskmrGVsaSTSHidemleeldlikvknrsldLLSTTQKERLRIAAVFVGQPDLVLIDFPTMECLPEWKFMVFRFI 558
Cdd:cd03216    72 ARRA-----GI--AMVY-------------------QLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVI 125

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 808356654  559 EK-RKEKRSIIVSSYDPEETEAISDKVVLMSEGYVV 593
Cdd:cd03216   126 RRlRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
403-597 5.07e-10

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 61.95  E-value: 5.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  403 RIENHWRVKQVSLTVHLGEVVTLYGHHGCGSGEILSIIAGQMKPEYGEVM-----MEQSQRPLM-----ISKTTDVPN-- 470
Cdd:PRK13638   10 RYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLwqgkpLDYSKRGLLalrqqVATVFQDPEqq 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  471 VNYLNVIQYLRLISKMRGVSAS--TSHIDEMLEELDLIKVKNRSLDLLSTTQKERLRIAAVFVGQPDLVLIDFPTMECLP 548
Cdd:PRK13638   90 IFYTDIDSDIAFSLRNLGVPEAeiTRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDP 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 808356654  549 EWKFMVFRFIEK-RKEKRSIIVSSYDPEETEAISDKVVLMSEGYVVLNGS 597
Cdd:PRK13638  170 AGRTQMIAIIRRiVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGA 219
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
 405-543 6.25e-10

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


Pssm-ID: 213198 [Multi-domain]  Cd Length: 201  Bit Score: 60.58  E-value: 6.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  405 ENHWRV--KQVSLTVHLGEVVTLYGHHGCGSGEILSIIAGQMKPEYGEVMMEqsQRPLMISKTTDVPNVNY--------- 473
Cdd:cd03231     9 ERDGRAlfSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLN--GGPLDFQRDSIARGLLYlghapgikt 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 808356654  474 -LNVIQYLRLISKMrgvsASTSHIDEMLEELDLIKVKNRSLDLLSTTQKERLRIAAVFVGQPDLVLIDFPT 543
Cdd:cd03231    87 tLSVLENLRFWHAD----HSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPT 153
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
 410-596 2.21e-09

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


Pssm-ID: 213201 [Multi-domain]  Cd Length: 226  Bit Score: 59.21  E-value: 2.21e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  410 VKQVSLTVHLGEVVTLYGHHGCGSGEILSIIAGQM---KPEYGEVMM--EQSQRPLMISKTTDVP----NVNYLNVIQYL 480
Cdd:cd03234    23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVeggGTTSGQILFngQPRKPDQFQKCVAYVRqddiLLPGLTVRETL 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  481 RLISKMRGVSASTSHIDEMLEELDLIK------VKNRSLDLLSTTQKERLRIAAVFVGQPDLVLIDFPT--MECLPEWKF 552
Cdd:cd03234   103 TYTAILRLPRKSSDAIRKKRVEDVLLRdlaltrIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTsgLDSFTALNL 182

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 808356654  553 MVFrFIEKRKEKRSIIVSSYDP-EETEAISDKVVLMSEGYVVLNG 596
Cdd:cd03234   183 VST-LSQLARRNRIVILTIHQPrSDLFRLFDRILLLSSGEIVYSG 226
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
393-597 4.80e-09

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 59.96  E-value: 4.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  393 PLVVLYGICKRIENHWRVKQVSLTVHLGEVVTLYGHHGCGSGEILSIIAGQMKPEYGEVMMEQSQrplmiskTTDVP--- 469
Cdd:PRK09452   13 PLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQD-------ITHVPaen 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  470 -NVN--------------YLNVIQYLRliskMRGVSAS--TSHIDEMLEELDLIKVKNRSLDLLSTTQKERLRIAAVFVG 532
Cdd:PRK09452   86 rHVNtvfqsyalfphmtvFENVAFGLR----MQKTPAAeiTPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVN 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 808356654  533 QPDLVLIDfptmECLP--EWKFmvfrfiekRKEKRS------------IIVSSYDPEETEAISDKVVLMSEGYVVLNGS 597
Cdd:PRK09452  162 KPKVLLLD----ESLSalDYKL--------RKQMQNelkalqrklgitFVFVTHDQEEALTMSDRIVVMRDGRIEQDGT 228
cbiO PRK13650
energy-coupling factor transporter ATPase;
405-592 1.33e-08

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 57.82  E-value: 1.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  405 ENHWRVKQVSLTVHLGEVVTLYGHHGCGSGEILSIIAGQMKPEYGEVMMEQSQRplmiskTTDvpnvnylNVIQYLRLIS 484
Cdd:PRK13650   18 QEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLL------TEE-------NVWDIRHKIG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  485 KM-----------------------RGVSAST--SHIDEMLEELDLIKVKNRSLDLLSTTQKERLRIAAVFVGQPDLVLI 539
Cdd:PRK13650   85 MVfqnpdnqfvgatveddvafglenKGIPHEEmkERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIIL 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 808356654  540 DFPTMECLPEWKFMVFRFIEKRKEKRSIIVSS--YDPEETeAISDKVVLMSEGYV 592
Cdd:PRK13650  165 DEATSMLDPEGRLELIKTIKGIRDDYQMTVISitHDLDEV-ALSDRVLVMKNGQV 218
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
 395-597 2.03e-08

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: 56.58  E-value: 2.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  395 VVLYGICKRIENHWRVKQVSLTVHLGEVVTLYGHHGCGSGEILSIIAGQMKPEYGEVMMEQSQrplmiskTTDVP----N 470
Cdd:cd03296     3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGED-------ATDVPvqerN 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  471 VNYL--------------NVIQYLRLISKMRGVSAST--SHIDEMLEELDLIKVKNRSLDLLSTTQKERLRIAAVFVGQP 534
Cdd:cd03296    76 VGFVfqhyalfrhmtvfdNVAFGLRVKPRSERPPEAEirAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEP 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 808356654  535 DLVLIDFPtmeclpewkfmvFRFIEK--RKEKR-------------SIIVsSYDPEETEAISDKVVLMSEGYVVLNGS 597
Cdd:cd03296   156 KVLLLDEP------------FGALDAkvRKELRrwlrrlhdelhvtTVFV-THDQEEALEVADRVVVMNKGRIEQVGT 220
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
 384-595 2.06e-08

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 56.99  E-value: 2.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  384 PPTPIVKGVPLVvLYGICKRIENHWRVKQVSLTVHLGEVVTLYGHHGCGSGEILSIIAGQMKPEYGEV------------ 451
Cdd:PRK11247    3 NTARLNQGTPLL-LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELlagtaplaeare 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  452 ---MMEQSQRPLMISKTTDvpNVNylnviqyLRLISKMRgvsastshiDEMLEELDLIKVKNRSLD---LLSTTQKERLR 525
Cdd:PRK11247   82 dtrLMFQDARLLPWKKVID--NVG-------LGLKGQWR---------DAALQALAAVGLADRANEwpaALSGGQKQRVA 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  526 IAAVFVGQPDLVLIDFP----------TMECLPE--WkfmvfrfiekRKEKRSIIVSSYDPEETEAISDKVVLMSEGYVV 593
Cdd:PRK11247  144 LARALIHRPGLLLLDEPlgaldaltriEMQDLIEslW----------QQHGFTVLLVTHDVSEAVAMADRVLLIEEGKIG 213


                  ..
gi 808356654  594 LN 595
Cdd:PRK11247  214 LD 215
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
 410-625 3.99e-08

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 56.06  E-value: 3.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  410 VKQVSLTVHLGEVVTLYGHHGCGSGEILSIIAGQMKPEYGEVMMEQSQRPLMISKTTDVPNVNYL----------NVIQY 479
Cdd:PRK10895   19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGYLpqeasifrrlSVYDN 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  480 LRLISKMRGVSASTSHID---EMLEELDLIKVKNRSLDLLSTTQKERLRIAAVFVGQPDLVLIDFPTMECLPEWKFMVFR 556
Cdd:PRK10895   99 LMAVLQIRDDLSAEQREDranELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKR 178

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  557 FIEK-RKEKRSIIVSSYDPEETEAISDKVVLMSEGYVVLNGSceafkhsinsvfeiriwPNNRFTDEQIK 625
Cdd:PRK10895  179 IIEHlRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGT-----------------PTEILQDEHVK 231
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
 401-596 6.98e-08

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: 54.85  E-value: 6.98e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  401 CKRIENHWRVKQVSLTVHLGEVVTLYGHHGCGSGEILSIIAGQMKPEYGEVMMEQSQRPLMiskttdvpNVNY-----LN 475
Cdd:cd03220    29 KGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLL--------GLGGgfnpeLT 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  476 VIQYLRLISKMRGVsaSTSHIDEMLEE----------LDLiKVKNrsldlLSTTQKERLRIAAVFVGQPDLVLIDfptme 545
Cdd:cd03220   101 GRENIYLNGRLLGL--SRKEIDEKIDEiiefselgdfIDL-PVKT-----YSSGMKARLAFAIATALEPDILLID----- 167

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  546 clpEW------KFM---VFRFIEKRKEKRSIIVSSYDPEETEAISDKVVLMSEGYVVLNG 596
Cdd:cd03220   168 ---EVlavgdaAFQekcQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
 410-601 9.11e-08

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 55.24  E-value: 9.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  410 VKQVSLTVHLGEVVTLYGHHGCGSGEILSIIAGQMKPEYGEV-------------MMEQSQRPLMISKTTDvpnvNYL-- 474
Cdd:PRK13636   22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRIlfdgkpidysrkgLMKLRESVGMVFQDPD----NQLfs 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  475 -NVIQYLRLISKMRGVSASTSH--IDEMLEELDLIKVKNRSLDLLSTTQKERLRIAAVFVGQPDLVLIDFPTMECLPEWK 551
Cdd:PRK13636   98 aSVYQDVSFGAVNLKLPEDEVRkrVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGV 177

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 808356654  552 FMVFRFIEKRKEKR--SIIVSSYDPEETEAISDKVVLMSEGYVVLNGSC-EAF 601
Cdd:PRK13636  178 SEIMKLLVEMQKELglTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPkEVF 230
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
405-602 1.20e-07

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 55.09  E-value: 1.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  405 ENHWRVKQVSLTVHLGEVVTLYGHHGCGSgeilSIIAGQMK----PEYGEVMMEQ------------SQRPLMISKTTDV 468
Cdd:PRK13633   21 TEKLALDDVNLEVKKGEFLVILGRNGSGK----STIAKHMNalliPSEGKVYVDGldtsdeenlwdiRNKAGMVFQNPDN 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  469 PNVNYLnVIQYLRLISKMRGVSAST--SHIDEMLEELDLIKVKNRSLDLLSTTQKERLRIAAVFVGQPDLVLIDFPTMEC 546
Cdd:PRK13633   97 QIVATI-VEEDVAFGPENLGIPPEEirERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAML 175

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  547 LPEWKFMVFRFIEKRKEKRSI---IVSSYDPEETEAisDKVVLMSEGYVVLNGSC-EAFK 602
Cdd:PRK13633  176 DPSGRREVVNTIKELNKKYGItiiLITHYMEEAVEA--DRIIVMDSGKVVMEGTPkEIFK 233
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
 411-606 1.66e-07

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


Pssm-ID: 213228 [Multi-domain]  Cd Length: 235  Bit Score: 54.04  E-value: 1.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  411 KQVSLTVHLGEVVTLYGHHGCGSGEILSIIAGQMKPEYGEVMMEQSQRPLMISKTTDVPNVNY------------LNVIQ 478
Cdd:cd03261    17 KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRRRMgmlfqsgalfdsLTVFE 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  479 ----YLRLISKMrgvsaSTSHIDEM----LEELDLIKVKNRSLDLLSTTQKERLRIAAVFVGQPDLVLIDFPTMECLPEW 550
Cdd:cd03261    97 nvafPLREHTRL-----SEEEIREIvlekLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDPIA 171

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 808356654  551 KFMVFRFIE--KRKEKRSIIVSSYDPEETEAISDKVVLMSEGYVVLNGSCEAFKHSIN 606
Cdd:cd03261   172 SGVIDDLIRslKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASDD 229
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
393-596 1.77e-07

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 55.56  E-value: 1.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  393 PLVVLYGICKRIENHWRVKQVSLTVHLGEVVTLYGHHGCGSGEILSIIAGQMKPEYGEVMMEQSQRPLMISKTT------ 466
Cdd:PRK09700    4 PYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAaqlgig 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  467 ----DVPNVNYLNVIQYL----RLISKMRGV-----SASTSHIDEMLEELDLIKVKNRSLDLLSTTQKERLRIAAVFVGQ 533
Cdd:PRK09700   84 iiyqELSVIDELTVLENLyigrHLTKKVCGVniidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLD 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 808356654  534 PDLVLIDFPTMECLP---EWKFMVFRfiEKRKEKRSIIVSSYDPEETEAISDKVVLMSEGYVVLNG 596
Cdd:PRK09700  164 AKVIIMDEPTSSLTNkevDYLFLIMN--QLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
cbiO PRK13644
energy-coupling factor transporter ATPase;
410-599 1.86e-07

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 54.22  E-value: 1.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  410 VKQVSLTVHLGEVVTLYGHHGCGSGEILSIIAGQMKPEYGEVMMeqsqRPLMISKTTDVPNVNYLNVIQYLRLISKMRGV 489
Cdd:PRK13644   18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLV----SGIDTGDFSKLQGIRKLVGIVFQNPETQFVGR 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  490 SAST-----------------SHIDEMLEELDLIKVKNRSLDLLSTTQKERLRIAAVFVGQPDLVLIDFPTMECLPEWKF 552
Cdd:PRK13644   94 TVEEdlafgpenlclppieirKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGI 173

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 808356654  553 MVFRFIEKRKEK-RSIIVSSYDPEETEAiSDKVVLMSEGYVVLNGSCE 599
Cdd:PRK13644  174 AVLERIKKLHEKgKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPE 220
cbiO PRK13646
energy-coupling factor transporter ATPase;
407-597 2.29e-07

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 54.02  E-value: 2.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  407 HWRVKQVSLTVHLGEVVTLYGHHGCGSGEILSIIAGQMKPEYGEVMMEQSQrplMISKTTDvpnvnylnviQYLRLISKM 486
Cdd:PRK13646   20 HQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDIT---ITHKTKD----------KYIRPVRKR 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  487 RGV----SASTSHIDEMLEE---------LDLIKVKNRSLDLL-----------------STTQKERLRIAAVFVGQPDL 536
Cdd:PRK13646   87 IGMvfqfPESQLFEDTVEREiifgpknfkMNLDEVKNYAHRLLmdlgfsrdvmsqspfqmSGGQMRKIAIVSILAMNPDI 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 808356654  537 VLIDFPTMECLPEWKFMVFRFIEK--RKEKRSIIVSSYDPEETEAISDKVVLMSEGYVVLNGS 597
Cdd:PRK13646  167 IVLDEPTAGLDPQSKRQVMRLLKSlqTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTS 229
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
 413-543 5.74e-07

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 52.09  E-value: 5.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  413 VSLTVHLGEVVTLYGHHGCGSGEILSIIAGQMKPEYGEVM--------MEQSQRPLMISKTTD--------VPNVNYLNV 476
Cdd:PRK10584   29 VELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSlvgqplhqMDEEARAKLRAKHVGfvfqsfmlIPTLNALEN 108

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 808356654  477 IQylrLISKMRGVSASTSHID--EMLEELDLIKVKNRSLDLLSTTQKERLRIAAVFVGQPDLVLIDFPT 543
Cdd:PRK10584  109 VE---LPALLRGESSRQSRNGakALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPT 174
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
413-590 1.16e-06

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 51.62  E-value: 1.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  413 VSLTVHLGEVVTLYGHHGCGSGEILSIIAGQMKPEYGEVMMEQ-------SQRPLMISKTTDVPNVNYL-NVIQYLRLIS 484
Cdd:PRK11248   20 INLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGkpvegpgAERGVVFQNEGLLPWRNVQdNVAFGLQLAG 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  485 KMRGVSASTSHidEMLEELDLIKVKNRSLDLLSTTQKERLRIAAVFVGQPDLVLIDFP-------TMECLPEWKFMVFrf 557
Cdd:PRK11248  100 VEKMQRLEIAH--QMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPfgaldafTREQMQTLLLKLW-- 175

                         170       180       190
                  ....*....|....*....|....*....|...
gi 808356654  558 iekRKEKRSIIVSSYDPEETEAISDKVVLMSEG 590
Cdd:PRK11248  176 ---QETGKQVLLITHDIEEAVFMATELVLLSPG 205
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
 410-603 1.36e-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: 53.48  E-value: 1.36e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654   410 VKQVSLTVHLGEVVTLYGHHGCGSGEILSIIAGQMKPEYGEVMMEQSQrplMISKTTDV-PNVNY----------LNVIQ 478
Cdd:TIGR01257 1955 VDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKS---ILTNISDVhQNMGYcpqfdaiddlLTGRE 2031

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654   479 YLRLISKMRGVSAStsHIDEM----LEELDLIKVKNRSLDLLSTTQKERLRIAAVFVGQPDLVLIDFPTMECLPEWKFMV 554
Cdd:TIGR01257 2032 HLYLYARLRGVPAE--EIEKVanwsIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRML 2109

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 808356654   555 FRFIEK-RKEKRSIIVSSYDPEETEAISDKVVLMSEGYVVLNGSCEAFKH 603
Cdd:TIGR01257 2110 WNTIVSiIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKS 2159
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
 405-596 3.23e-06

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: 49.23  E-value: 3.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  405 ENHWRVKQVSLTVHLGEVVTLYGHHGCGSGEILSIIAGQMKPEYGEVMMEQSqrplmiskttdvpnvnylNVIQYLRLIS 484
Cdd:cd03247    13 QEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGV------------------PVSDLEKALS 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  485 KmrgvsastshidemleeldLIKVKNRSLDLLSTT------------QKERLRIAAVFVGQPDLVLIDFPTMECLPEWKF 552
Cdd:cd03247    75 S-------------------LISVLNQRPYLFDTTlrnnlgrrfsggERQRLALARILLQDAPIVLLDEPTVGLDPITER 135

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 808356654  553 MVFRFIEKRKEKRSIIVSSYDPEETEAIsDKVVLMSEGYVVLNG 596
Cdd:cd03247   136 QLLSLIFEVLKDKTLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
392-597 4.27e-06

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 50.57  E-value: 4.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  392 VPLVVLYGICKRIENHWRVKQVSLTVHLGEVVTLYGHHGCGSGEILSIIAGQMKPEYGEVMM------EQSQRPLMisKT 465
Cdd:PRK13537    5 VAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLcgepvpSRARHARQ--RV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  466 TDVPNVNYLN----VIQYLRLISKMRGVSASTshIDEMLEEL-DLIKVKNRS---LDLLSTTQKERLRIAAVFVGQPDLV 537
Cdd:PRK13537   83 GVVPQFDNLDpdftVRENLLVFGRYFGLSAAA--ARALVPPLlEFAKLENKAdakVGELSGGMKRRLTLARALVNDPDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 808356654  538 LIDFPTMECLPEWKFMVF-RFIEKRKEKRSIIVSSYDPEETEAISDKVVLMSEGYVVLNGS 597
Cdd:PRK13537  161 VLDEPTTGLDPQARHLMWeRLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGA 221
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
 389-596 5.38e-06

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: 48.80  E-value: 5.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  389 VKGVPLVVLYGICKRIENHWRVKQVSLTVHLGEVVTLYGHHGCGSGEILSIIAGQMKPEYGevmmeqsqrplmISKTTDV 468
Cdd:cd03233     2 STLSWRNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVS------------VEGDIHY 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  469 PNVNYLNVIQYLRLISKMrgVSASTSHIDEML--EELDL-IKVK-NRSLDLLSTTQKERLRIAAVFVGQPDLVLIDFPT- 543
Cdd:cd03233    70 NGIPYKEFAEKYPGEIIY--VSEEDVHFPTLTvrETLDFaLRCKgNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTr 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 808356654  544 -------MECLPEWKFMVfrfiekRKEKRSIIVSSYDP-EETEAISDKVVLMSEGYVVLNG 596
Cdd:cd03233   148 gldsstaLEILKCIRTMA------DVLKTTTFVSLYQAsDEIYDLFDKVLVLYEGRQIYYG 202
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
409-593 5.45e-06

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 50.79  E-value: 5.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  409 RVKQVSLTVHLGEVVTLYGHHGCGSGEILSIIAGQMKPEYGEVMMEqsQRPLMISKTTD--------VP----------- 469
Cdd:COG1129   267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLD--GKPVRIRSPRDairagiayVPedrkgeglvld 344

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  470 -----NVNYLNviqyLRLISKMRGVS--ASTSHIDEMLEELDlikVKNRSLDLLSTT------QKerLRIAAVFVGQPDL 536
Cdd:COG1129   345 lsireNITLAS----LDRLSRGGLLDrrRERALAEEYIKRLR---IKTPSPEQPVGNlsggnqQK--VVLAKWLATDPKV 415

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 808356654  537 VLIDFPT--------MEclpewkfmVFRFIEK-RKEKRSIIVSSYDPEETEAISDKVVLMSEGYVV 593
Cdd:COG1129   416 LILDEPTrgidvgakAE--------IYRLIRElAAEGKAVIVISSELPELLGLSDRILVMREGRIV 473
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
 420-585 5.52e-06

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: 49.33  E-value: 5.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  420 GEVVTLYGHHGCGSGEILSIIAGQMKPEYGEVMMEQ---SQRPLMISKTTDVpNVNYLnviqylrLISKMRGVSASTSHI 496
Cdd:cd03237    25 SEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELdtvSYKPQYIKADYEG-TVRDL-------LSSITKDFYTHPYFK 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  497 DEMLEELDLIKVKNRSLDLLSTTQKERLRIAAVFVGQPDLVLIDFPTMECLPEWKFMVFRFIeKR---KEKRSIIVSSYD 573
Cdd:cd03237    97 TEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVI-RRfaeNNEKTAFVVEHD 175

                         170
                  ....*....|..
gi 808356654  574 PEETEAISDKVV 585
Cdd:cd03237   176 IIMIDYLADRLI 187
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
 411-599 7.64e-06

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 49.31  E-value: 7.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  411 KQVSLTVHLGEVVTLYGHHGCGSGEILSIIAGQMKPEYGEVMMEQ-----SQRPLM-ISKTTDV-----------PNVNY 473
Cdd:PRK13639   19 KGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepikyDKKSLLeVRKTVGIvfqnpddqlfaPTVEE 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  474 LNVIQYLRLISKMRGVSastSHIDEMLEELDLIKVKNRSLDLLSTTQKERLRIAAVFVGQPDLVLIDFPTMECLPEWKFM 553
Cdd:PRK13639   99 DVAFGPLNLGLSKEEVE---KRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQ 175

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 808356654  554 VFRFI-EKRKEKRSIIVSSYDPEETEAISDKVVLMSEGYVVLNGSCE 599
Cdd:PRK13639  176 IMKLLyDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPK 222
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
410-604 9.38e-06

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 49.24  E-value: 9.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  410 VKQVSLTVHLGEVVTLYGHHGCGSGEILSIIAGQMKPEYGEVmmEQSQRPLMISKTTDV----------PNVNYL----- 474
Cdd:PRK13635   23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTI--TVGGMVLSEETVWDVrrqvgmvfqnPDNQFVgatvq 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  475 -NVIQYLrlisKMRGVSAstshiDEMLEELD--LIKVK-----NRSLDLLSTTQKERLRIAAVFVGQPDLVLIDFPTMEC 546
Cdd:PRK13635  101 dDVAFGL----ENIGVPR-----EEMVERVDqaLRQVGmedflNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSML 171

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 808356654  547 LPEWKFMVFRFIEKRKEKRSIIVSS--YDPEETeAISDKVVLMSEGYVVLNGS-CEAFKHS 604
Cdd:PRK13635  172 DPRGRREVLETVRQLKEQKGITVLSitHDLDEA-AQADRVIVMNKGEILEEGTpEEIFKSG 231
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
 408-597 1.02e-05

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 48.83  E-value: 1.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  408 WRVKQVSLTVHLGEVVTLYGHHGCGSGEILSIIAGQMKPEYGEVMMEqsqrplmiSKTTDVPNVNYLN----VI------ 477
Cdd:PRK13632   23 NALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKID--------GITISKENLKEIRkkigIIfqnpdn 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  478 QYL--------------RLIS--KMRGVsastshIDEMLEELDLIKVKNRSLDLLSTTQKERLRIAAVFVGQPDLVLIDF 541
Cdd:PRK13632   95 QFIgatveddiafglenKKVPpkKMKDI------IDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDE 168

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 808356654  542 PTMECLPEWKFMVFRFIEKRKEKRSIIVSSYDPEETEAI-SDKVVLMSEGYVVLNGS 597
Cdd:PRK13632  169 STSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAIlADKVIVFSEGKLIAQGK 225
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
 410-604 1.27e-05

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


Pssm-ID: 213225 [Multi-domain]  Cd Length: 233  Bit Score: 48.35  E-value: 1.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  410 VKQVSLTVHLGEVVTLYGHHGCGSGEILSIIAGQMKPEYGEV--------------MMEQSQRPLMISKttdvpNVNYLN 475
Cdd:cd03258    21 LKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVlvdgtdltllsgkeLRKARRRIGMIFQ-----HFNLLS 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  476 ---VIQYLRLISKMRGVSAS--TSHIDEMLEELDLIKVKNRSLDLLSTTQKERLRIAAVFVGQPDLVLIDFPTMECLPEW 550
Cdd:cd03258    96 srtVFENVALPLEIAGVPKAeiEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPET 175

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 808356654  551 KFMVFRFIEKRKEKR--SIIVSSYDPEETEAISDKVVLMSEGYVVLNGSC-EAFKHS 604
Cdd:cd03258   176 TQSILALLRDINRELglTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVeEVFANP 232
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
410-672 1.77e-05

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


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 48.88  E-value: 1.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  410 VKQVSLTVHLGEVVTLYGHHGCGSGEILSIIAGQMKPEYGEVMMEQSQrplmISKTTD-----VPNVNYLNVIQYLRLIS 484
Cdd:PRK10070   44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVD----IAKISDaelreVRRKKIAMVFQSFALMP 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  485 KMR------------GVSASTSHiDEMLEELDLIKVKNRSL---DLLSTTQKERLRIAAVFVGQPDLVLID--FPTMECL 547
Cdd:PRK10070  120 HMTvldntafgmelaGINAEERR-EKALDALRQVGLENYAHsypDELSGGMRQRVGLARALAINPDILLMDeaFSALDPL 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  548 PEWKFMVFRFIEKRKEKRSIIVSSYDPEETEAISDKVVLMSEGYVVLNGSCEafkhsinsvfEIRIWPNNRFTDEQIKGM 627
Cdd:PRK10070  199 IRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPD----------EILNNPANDYVRTFFRGV 268

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 808356654  628 MKTLTLgdnQMKNDARffETPNGKIRVTlPILYRRSIPLILRELD 672
Cdd:PRK10070  269 DISQVF---SAKDIAR--RTPNGLIRKT-PGFGPRSALKLLQDED 307
cbiO PRK13642
energy-coupling factor transporter ATPase;
496-593 1.92e-05

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 48.17  E-value: 1.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  496 IDEMLEELDLIKVKNRSLDLLSTTQKERLRIAAVFVGQPDLVLIDFPTMECLPEWKFMVFRFIEKRKEKRSIIVSS--YD 573
Cdd:PRK13642  121 VDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSitHD 200

                          90       100
                  ....*....|....*....|
gi 808356654  574 PEETeAISDKVVLMSEGYVV 593
Cdd:PRK13642  201 LDEA-ASSDRILVMKAGEII 219
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
 409-597 3.62e-05

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 46.85  E-value: 3.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  409 RVKQVSLTVHLGEVVTLYGHHGCGSGEILSIIAGqMKPEYGEVMME--------------------QSQRPLMIskttdV 468
Cdd:PRK03695   11 RLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAG-LLPGSGSIQFAgqpleawsaaelarhraylsQQQTPPFA-----M 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  469 PnvnylnVIQYLRL-ISKMRGVSASTSHIDEMLEELDLIKVKNRSLDLLSTTQKERLRIAAVF-----VGQPD--LVLID 540
Cdd:PRK03695   85 P------VFQYLTLhQPDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqvwpDINPAgqLLLLD 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 808356654  541 FPTMECLPEWKFMVFRFIEKRKEK-RSIIVSSYDPEETEAISDKVVLMSEGYVVLNGS 597
Cdd:PRK03695  159 EPMNSLDVAQQAALDRLLSELCQQgIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGR 216
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
393-543 4.63e-05

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 46.35  E-value: 4.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  393 PLVVLYGICKRIEN---HWRV-KQVSLTVHLGEVVTLYGHHGCGSGEILSIIAGQMKPEYGEVMME-QSQRPLMISKTTD 467
Cdd:PRK11629    4 ILLQCDNLCKRYQEgsvQTDVlHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNgQPMSKLSSAAKAE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  468 V---------------PNVNYLNVIQYLRLISKMRGVSASTSHIdEMLEELDLIKVKNRSLDLLSTTQKERLRIAAVFVG 532
Cdd:PRK11629   84 LrnqklgfiyqfhhllPDFTALENVAMPLLIGKKKPAEINSRAL-EMLAAVGLEHRANHRPSELSGGERQRVAIARALVN 162

                         170
                  ....*....|.
gi 808356654  533 QPDLVLIDFPT 543
Cdd:PRK11629  163 NPRLVLADEPT 173
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
 410-596 7.87e-05

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 46.06  E-value: 7.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  410 VKQVSLTVHLGEVVTLYGHHGCGSGEILSIIAG--QMKPE---YGEVMM-----------EQSQRPLMISKTTD-VPNVN 472
Cdd:PRK14247   19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRliELYPEarvSGEVYLdgqdifkmdviELRRRVQMVFQIPNpIPNLS 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  473 -YLNVIQYLRLISKMRGVSASTSHIDEMLEELDLI-KVKNRsLDL----LSTTQKERLRIAAVFVGQPDLVLIDFPTMEC 546
Cdd:PRK14247   99 iFENVALGLKLNRLVKSKKELQERVRWALEKAQLWdEVKDR-LDApagkLSGGQQQRLCIARALAFQPEVLLADEPTANL 177

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 808356654  547 LPEWKFMVFR-FIEKRKEKRSIIVSSYdPEETEAISDKVVLMSEGYVVLNG 596
Cdd:PRK14247  178 DPENTAKIESlFLELKKDMTIVLVTHF-PQQAARISDYVAFLYKGQIVEWG 227
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
497-605 1.48e-04

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 45.88  E-value: 1.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  497 DEMLEELDLIKVKNRSLDLLSTTQKERLRIAAVFVGQPDLVLIDFPTMECLPEWKFMVFRFIEKR-KEKRSIIVSSYDPE 575
Cdd:NF000106  126 DELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMvRDGATVLLTTQYME 205

                          90       100       110
                  ....*....|....*....|....*....|
gi 808356654  576 ETEAISDKVVLMSEGYVVLNGSCEAFKHSI 605
Cdd:NF000106  206 EAEQLAHELTVIDRGRVIADGKVDELKTKV 235
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
 409-590 2.08e-04

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


Pssm-ID: 131681 [Multi-domain]  Cd Length: 500  Bit Score: 45.59  E-value: 2.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654   409 RVKQVSLTVHLGEVVTLYGHHGCGSGEILSIIAGQMKPEY-GEVMMEqsQRPLMISKTTD--------VPN-------VN 472
Cdd:TIGR02633  275 RVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKFeGNVFIN--GKPVDIRNPAQairagiamVPEdrkrhgiVP 352

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654   473 YLNVIQYLRLIS----KMRGVSASTSHIDEMLEELDLIKVKNRSLDL----LSTTQKERLRIAAVFVGQPDLVLIDFPTM 544
Cdd:TIGR02633  353 ILGVGKNITLSVlksfCFKMRIDAAAELQIIGSAIQRLKVKTASPFLpigrLSGGNQQKAVLAKMLLTNPRVLILDEPTR 432

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 808356654   545 ECLPEWKFMVFRFIEK-RKEKRSIIVSSYDPEETEAISDKVVLMSEG 590
Cdd:TIGR02633  433 GVDVGAKYEIYKLINQlAQEGVAIIVVSSELAEVLGLSDRVLVIGEG 479
cbiO PRK13640
energy-coupling factor transporter ATPase;
410-597 2.64e-04

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 44.79  E-value: 2.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  410 VKQVSLTVHLGEVVTLYGHHGCGSGEILSIIAGQMKPE--------------YGEVMMEQSQRPLMISKTTDVPNVNyLN 475
Cdd:PRK13640   23 LNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDdnpnskitvdgitlTAKTVWDIREKVGIVFQNPDNQFVG-AT 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  476 VIQYLRLISKMRGVSAS--TSHIDEMLEELDLIKVKNRSLDLLSTTQKERLRIAAVFVGQPDLVLIDFPTMECLPEWKFM 553
Cdd:PRK13640  102 VGDDVAFGLENRAVPRPemIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQ 181

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 808356654  554 VFRFIEKRKEKRSIIVSS--YDPEETEaISDKVVLMSEGYVVLNGS 597
Cdd:PRK13640  182 ILKLIRKLKKKNNLTVISitHDIDEAN-MADQVLVLDDGKLLAQGS 226
ABC2_membrane_3 pfam12698
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ...
 901-1097 5.79e-04

ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter family pfam01061.


Pssm-ID: 463674 [Multi-domain]  Cd Length: 345  Bit Score: 43.92  E-value: 5.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654   901 SYSLMYITAVFQMFVYTFSVVLPLRLVSTNMGPQSMILPWPRYVYFGFIYVFQLVVFLVIAIILGFAVLSMGFFATNtts 980
Cdd:pfam12698  161 YYLVGLILMIIILIGAAIIAVSIVEEKESRIKERLLVSGVSPLQYWLGKILGDFLVGLLQLLIILLLLFGIGIPFGN--- 237

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654   981 cYLRFLSAWFLSYASTLPLIYFLVFNIQNTKSVIPIILAISSLSVTFpnLVASFSAENqvsLQSLIQFVSwscMLNPPSS 1060
Cdd:pfam12698  238 -LGLLLLLFLLYGLAYIALGYLLGSLFKNSEDAQSIIGIVILLLSGF--FGGLFPLED---PPSFLQWIF---SIIPFFS 308

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 808356654  1061 LQVLAAFLNAGESLEKNSGTITSLILFCGAQFWIIVI 1097
Cdd:pfam12698  309 PIDGLLRLIYGDSLWEIAPSLIILLLFAVVLLLLALL 345
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
416-585 6.16e-04

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 44.41  E-value: 6.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  416 TVHLGEVVTLYGHHGCGSGEILSIIAGQMKPEYGEVMMEQ--SQRPLMISKTTDVPnvnylnVIQYLRLISKMrgvsAST 493
Cdd:PRK13409  361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELkiSYKPQYIKPDYDGT------VEDLLRSITDD----LGS 430

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  494 SHID-EMLEELDLIKVKNRSLDLLSTTQKERLRIAAVFVGQPDLVLIDFPTMECLPEWKFMVFRFIEKRKEKR--SIIVS 570
Cdd:PRK13409  431 SYYKsEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEReaTALVV 510

                         170
                  ....*....|....*
gi 808356654  571 SYDPEETEAISDKVV 585
Cdd:PRK13409  511 DHDIYMIDYISDRLM 525
tagH PRK13545
teichoic acids export protein ATP-binding subunit; Provisional
 405-540 1.27e-03

teichoic acids export protein ATP-binding subunit; Provisional


Pssm-ID: 184130 [Multi-domain]  Cd Length: 549  Bit Score: 43.34  E-value: 1.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  405 ENHWRVKQVSLTVHLGEVVTLYGHHGCGSGEILSIIAGQMKPEYGEVMMEQSQRPLMISKTTDvpnvNYLNVIQYLRLIS 484
Cdd:PRK13545   35 EYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLN----GQLTGIENIELKG 110

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 808356654  485 KMRGVSASTSH--IDEMLEELDLIKVKNRSLDLLSTTQKERLRIAAVFVGQPDLVLID 540
Cdd:PRK13545  111 LMMGLTKEKIKeiIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVID 168
DUF1189 pfam06691
Protein of unknown function (DUF1189); This family consists of several hypothetical bacterial ...
 937-1020 2.65e-03

Protein of unknown function (DUF1189); This family consists of several hypothetical bacterial proteins of around 260 residues in length. The function of this family is unknown.


Pssm-ID: 429073  Cd Length: 240  Bit Score: 41.07  E-value: 2.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654   937 ILPWPRYVYFGFIYVFQLVVFLVIAIILGFavlsMGFFATNTTSCYLRFLSAWFLS-YASTLPLIYFLVFNIQNTK---- 1011
Cdd:pfam06691  153 ILKIILPIIFIVLFLFSLASKLIGALILAL----IGLILARILKIKLSYGQLWNISaYALTLPTILFAIMNILNFTvpyf 228


                   ....*....
gi 808356654  1012 SVIPIILAI 1020
Cdd:pfam06691  229 FLIYWIIAI 237
NosY COG1277
ABC-type transport system involved in multi-copper enzyme maturation, permease component ...
 160-254 2.72e-03

ABC-type transport system involved in multi-copper enzyme maturation, permease component [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440888 [Multi-domain]  Cd Length: 201  Bit Score: 40.57  E-value: 2.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  160 DLWNNDRSSGYYNMFLSLHARRFHYFIAKFVFWYGIALIISLIVFIVNVLVVPAVFCST------YLQFV---VCYAACI 230
Cdd:COG1277    71 DAISGERESGTLELLLTLPISRWEIVLGKFLGALLVLLLALLITFLLALLLGLLLFGSPppdlgaILGFYlglLLLGLAF 150

                          90       100
                  ....*....|....*....|....
gi 808356654  231 ISFAIFLATTFpGSPLFAKIVGFL 254
Cdd:COG1277   151 LAIGLFISALT-RNQIVAAILAIA 173
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 416-569 2.88e-03

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: 42.08  E-value: 2.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  416 TVHLGEVVTLYGHHGCGSGEILSIIAGQMKPEYGEVMMEQ--SQRPLMISKTTDVPnvnylnVIQYLRliskmrgvSAST 493
Cdd:COG1245   362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLkiSYKPQYISPDYDGT------VEEFLR--------SANT 427

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  494 SHID------EMLEELDLIKVKNRSLDLLSTTQKERLRIAAVFVGQPDLVLIDFPTMECLPEWKFMVFRFIEK--RKEKR 565
Cdd:COG1245   428 DDFGssyyktEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRfaENRGK 507


                  ....
gi 808356654  566 SIIV 569
Cdd:COG1245   508 TAMV 511
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
 496-599 5.48e-03

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 40.56  E-value: 5.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  496 IDEMLEELDLIKVKNRSLDLLSTTQKERLRIAAVFVGQPDLVLIDFPTMECLPEWKFMVFRFIEKRKEK--RSIIVSSYD 573
Cdd:PRK13652  118 VSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETygMTVIFSTHQ 197

                          90       100
                  ....*....|....*....|....*.
gi 808356654  574 PEETEAISDKVVLMSEGYVVLNGSCE 599
Cdd:PRK13652  198 LDLVPEMADYIYVMDKGRIVAYGTVE 223
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
 494-596 5.57e-03

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 40.49  E-value: 5.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356654  494 SHIDEMLEELDLIKVKNRSLDLLSTTQKERLRIAAVFVGQPDLVLIDFPTMECLPEWKFMVFRFIEK-RKEKRSIIVSSY 572
Cdd:PRK13647  117 RRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRlHNQGKTVIVATH 196

                          90       100
                  ....*....|....*....|....
gi 808356654  573 DPEETEAISDKVVLMSEGYVVLNG 596
Cdd:PRK13647  197 DVDLAAEWADQVIVLKEGRVLAEG 220
 
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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