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Conserved domains on  [gi|56849536|gb|AAW31630.1|]
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ABCB5beta [Homo sapiens]

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List of domain hits

Name Accession Description Interval E-value
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
571-809 5.58e-141

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


:

Pssm-ID: 213216 [Multi-domain]  Cd Length: 238  Bit Score: 418.87  E-value: 5.58e-141
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 571 EFREVSFFYPCRPDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRSQIAI 650
Cdd:cd03249   2 EFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 651 VPQEPVLFNCSIAENIAYGDNSRVVplDEIKEAANAANIHSFIEGPPEKYNTQVGLKGAQLSGGQKQRLAIARALLQKPK 730
Cdd:cd03249  82 VSQEPVLFDGTIAENIRYGKPDATD--EEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPK 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 56849536 731 ILLLDEATSALDNDSEKVVQHALDKARTGRTCLVVTHRLSAIQNADLIVVLHNGKIKEQGTHQELLRNRDIYFKLVNAQ 809
Cdd:cd03249 160 ILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
1-178 1.14e-102

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


:

Pssm-ID: 213216 [Multi-domain]  Cd Length: 238  Bit Score: 319.10  E-value: 1.14e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536   1 MVDENDIRALNVRHYRDHIGVVSQEPVLFGTTISNNIKYGRDDVTDEEMERAAREANAYDFIMEFPNKFNTLVGEKGAQM 80
Cdd:cd03249  61 LLDGVDIRDLNLRWLRSQIGLVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQL 140
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536  81 SGGQKQRIAIARALVRNPKILILDEATSALDSESESAVQAALEKASKGRTTIVVAHRLSTIRSADLIVTLKDGMLAEKGA 160
Cdd:cd03249 141 SGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGT 220
                       170
                ....*....|....*...
gi 56849536 161 HAELMAKRGLYYSLVMSQ 178
Cdd:cd03249 221 HDELMAQKGVYAKLVKAQ 238
ABC_membrane pfam00664
ABC transporter transmembrane region; This family represents a unit of six transmembrane ...
251-523 1.26e-49

ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.


:

Pssm-ID: 250039  Cd Length: 274  Bit Score: 175.94  E-value: 1.26e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536   251 TLASVLNGTVHPVFSIIFAKII-TMFGNNDKTTLKHDAEIYSMIFVILGVICFVSYFMQGLFYGraGEILTMRLRHLAFK 329
Cdd:pfam00664   1 LLIGILLLILAGATALVFPLLLgRFLDSLIDGNGDERSSLISLAILLIAVGVLQGLLLQGYFYL--GERLGQRIRKRLFR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536   330 AMLYQDIAWFDE--KENSTGGLTTILAIDIAQIQGATGSRIGVLTQNATNMGLSVIISFIYGWEMTFLILSIAPVLAVTG 407
Cdd:pfam00664  79 ALLRQILGLFMSffDTNSVGELTSRLTNDVSKIRDGLGDKLGLFFQSLATVVGGFIVMFYYGWKLTLVLLAILPLLILLS 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536   408 MIETAAMTGFANKDKQELKHAGKIATEALENIRTIVSLTREKAFEQMYEEMLQTQHRNTSKKAQIIGSCYAFSHAFIYFA 487
Cdd:pfam00664 159 AVLAKKLRKLNRKEQKAYAKAGSVAEESLSGIRTVKAFGREEYELERYDKALEDAEKAGIKKAIAAGLSFGITQFISYLS 238
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 56849536   488 YAAGFRFGAYLIQAGRMTPEGMFIVFTAIAYGAMAI 523
Cdd:pfam00664 239 YALALWFGGYLVISGGLSVGTVFAFLSLGLQLSGPL 274
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; ...
232-810 3.14e-130

ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; linked to 3D-structure


:

Pssm-ID: 224055 [Multi-domain]  Cd Length: 567  Bit Score: 403.35  E-value: 3.14e-130
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 232 SLLKILKLNKPEWPFVvLGTLASVLNGTVHPVFSIIFAKIITMFGNNdkttlKHDAEIYSMIFVILGVICFVSYFMQGLF 311
Cdd:COG1132   2 SLLRRLLKYLKYKLLL-LAILLLLLSALLSLLLPLLIGRIIDALLAD-----LGELLELLLLLLLLALLGGVLRALQSYL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 312 YGRAGEILTMRLRHLAFKAMLYQDIAWFDEkeNSTGGLTTILAIDIAQIQGATGSRIGVLTQNATNMGLSVIISFIYGWE 391
Cdd:COG1132  76 GSRLGQKIVADLRRDLFEKLLRLPLSFFDK--AKSGDLISRLTNDVEAVSNLVSTVLVLVFTSILLLIGSLVLLFSLSWR 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 392 MTFLILSIAPVLAVTGMIETAAMTGFANKDKQELKHAGKIATEALENIRTIVSLTREKAFEQMYEEMLQTQHRNTSKKAQ 471
Cdd:COG1132 154 LALILLLILPLLALVLSLLARKSRKLSRRVREALGELNARLLESLSGIRVIKAFGAEDRELKRFEEANEELRRANLRASR 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 472 IIGSCYAFSHAFIYFAYAAGFRFGAYLIQAGRMTPEGMFIVFTAIAYGAMAIGKTLVLAPEYSKAKSGAAHLFALLEKKP 551
Cdd:COG1132 234 LEALLAPLMLLLSSLGTVLVLALGGFLVLSGSLTVGALAAFILYLLRLLTPILQLGEVVSLLQRASAAAERLFELLDEEP 313
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 552 NIDSrsqEGKKPDTCEGNLEFREVSFFYPcrPDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLF 631
Cdd:COG1132 314 EVED---PPDPLKDTIGSIEFENVSFSYP--GKKPVLKDISFSIEPGEKVAIVGPSGSGKSTLIKLLLRLYDPTSGEILI 388
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 632 DGVDAKELNVQWLRSQIAIVPQEPVLFNCSIAENIAYGDNSrvVPLDEIKEAANAANIHSFIEGPPEKYNTQVGLKGAQL 711
Cdd:COG1132 389 DGIDIRDISLDSLRKRIGIVSQDPLLFSGTIRENIALGRPD--ATDEEIEEALKLANAHEFIANLPDGYDTIVGERGVNL 466
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 712 SGGQKQRLAIARALLQKPKILLLDEATSALDNDSEKVVQHALDKARTGRTCLVVTHRLSAIQNADLIVVLHNGKIKEQGT 791
Cdd:COG1132 467 SGGQRQRLAIARALLRNPPILILDEATSALDTETEALIQDALKKLLKGRTTLIIAHRLSTIKNADRIIVLDNGRIVERGT 546
                       570
                ....*....|....*....
gi 56849536 792 HQELLRNRDIYFKLVNAQS 810
Cdd:COG1132 547 HEELLAKGGLYARLYQAQG 565
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; ...
1-178 1.26e-69

ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; linked to 3D-structure


:

Pssm-ID: 224055 [Multi-domain]  Cd Length: 567  Bit Score: 241.18  E-value: 1.26e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536   1 MVDENDIRALNVRHYRDHIGVVSQEPVLFGTTISNNIKYGRDDVTDEEMERAAREANAYDFIMEFPNKFNTLVGEKGAQM 80
Cdd:COG1132 387 LIDGIDIRDISLDSLRKRIGIVSQDPLLFSGTIRENIALGRPDATDEEIEEALKLANAHEFIANLPDGYDTIVGERGVNL 466
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536  81 SGGQKQRIAIARALVRNPKILILDEATSALDSESESAVQAALEKASKGRTTIVVAHRLSTIRSADLIVTLKDGMLAEKGA 160
Cdd:COG1132 467 SGGQRQRLAIARALLRNPPILILDEATSALDTETEALIQDALKKLLKGRTTLIIAHRLSTIKNADRIIVLDNGRIVERGT 546
                       170
                ....*....|....*...
gi 56849536 161 HAELMAKRGLYYSLVMSQ 178
Cdd:COG1132 547 HEELLAKGGLYARLYQAQ 564
 
Name Accession Description Interval E-value
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
571-809 5.58e-141

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


Pssm-ID: 213216 [Multi-domain]  Cd Length: 238  Bit Score: 418.87  E-value: 5.58e-141
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 571 EFREVSFFYPCRPDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRSQIAI 650
Cdd:cd03249   2 EFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 651 VPQEPVLFNCSIAENIAYGDNSRVVplDEIKEAANAANIHSFIEGPPEKYNTQVGLKGAQLSGGQKQRLAIARALLQKPK 730
Cdd:cd03249  82 VSQEPVLFDGTIAENIRYGKPDATD--EEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPK 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 56849536 731 ILLLDEATSALDNDSEKVVQHALDKARTGRTCLVVTHRLSAIQNADLIVVLHNGKIKEQGTHQELLRNRDIYFKLVNAQ 809
Cdd:cd03249 160 ILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
1-178 1.14e-102

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


Pssm-ID: 213216 [Multi-domain]  Cd Length: 238  Bit Score: 319.10  E-value: 1.14e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536   1 MVDENDIRALNVRHYRDHIGVVSQEPVLFGTTISNNIKYGRDDVTDEEMERAAREANAYDFIMEFPNKFNTLVGEKGAQM 80
Cdd:cd03249  61 LLDGVDIRDLNLRWLRSQIGLVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQL 140
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536  81 SGGQKQRIAIARALVRNPKILILDEATSALDSESESAVQAALEKASKGRTTIVVAHRLSTIRSADLIVTLKDGMLAEKGA 160
Cdd:cd03249 141 SGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGT 220
                       170
                ....*....|....*...
gi 56849536 161 HAELMAKRGLYYSLVMSQ 178
Cdd:cd03249 221 HDELMAQKGVYAKLVKAQ 238
ABC_membrane pfam00664
ABC transporter transmembrane region; This family represents a unit of six transmembrane ...
251-523 1.26e-49

ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.


Pssm-ID: 250039  Cd Length: 274  Bit Score: 175.94  E-value: 1.26e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536   251 TLASVLNGTVHPVFSIIFAKII-TMFGNNDKTTLKHDAEIYSMIFVILGVICFVSYFMQGLFYGraGEILTMRLRHLAFK 329
Cdd:pfam00664   1 LLIGILLLILAGATALVFPLLLgRFLDSLIDGNGDERSSLISLAILLIAVGVLQGLLLQGYFYL--GERLGQRIRKRLFR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536   330 AMLYQDIAWFDE--KENSTGGLTTILAIDIAQIQGATGSRIGVLTQNATNMGLSVIISFIYGWEMTFLILSIAPVLAVTG 407
Cdd:pfam00664  79 ALLRQILGLFMSffDTNSVGELTSRLTNDVSKIRDGLGDKLGLFFQSLATVVGGFIVMFYYGWKLTLVLLAILPLLILLS 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536   408 MIETAAMTGFANKDKQELKHAGKIATEALENIRTIVSLTREKAFEQMYEEMLQTQHRNTSKKAQIIGSCYAFSHAFIYFA 487
Cdd:pfam00664 159 AVLAKKLRKLNRKEQKAYAKAGSVAEESLSGIRTVKAFGREEYELERYDKALEDAEKAGIKKAIAAGLSFGITQFISYLS 238
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 56849536   488 YAAGFRFGAYLIQAGRMTPEGMFIVFTAIAYGAMAI 523
Cdd:pfam00664 239 YALALWFGGYLVISGGLSVGTVFAFLSLGLQLSGPL 274
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
588-739 5.28e-43

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: 249501  Cd Length: 150  Bit Score: 153.57  E-value: 5.28e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536   588 LRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRSQIAIVPQEPVLFN-CSIAENI 666
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPGLFPrLTVRENL 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 56849536   667 AYG----DNSRVVPLDEIKEAANAANIhsfiegpPEKYNTQVGLKGAQLSGGQKQRLAIARALLQKPKILLLDEATS 739
Cdd:pfam00005  81 RLGlllkGLSKREKDARAEEALEKLGL-------GDLLDRPVGENPGTLSGGQKQRVAIARALLTKPKLLLLDEPTA 150
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
2-108 2.33e-24

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: 249501  Cd Length: 150  Bit Score: 100.80  E-value: 2.33e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536     2 VDENDIRALNVRHYRDHIGVVSQEPVLF-GTTISNNIKYGRDDvtdEEMERAAREANAYDFI--MEFPNKFNTLVGEKGA 78
Cdd:pfam00005  44 LDGQDLTDDERKSLRKEIGYVFQDPGLFpRLTVRENLRLGLLL---KGLSKREKDARAEEALekLGLGDLLDRPVGENPG 120
                          90       100       110
                  ....*....|....*....|....*....|
gi 56849536    79 QMSGGQKQRIAIARALVRNPKILILDEATS 108
Cdd:pfam00005 121 TLSGGQKQRVAIARALLTKPKLLLLDEPTA 150
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
587-778 1.69e-16

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


Pssm-ID: 273491  Cd Length: 198  Bit Score: 78.55  E-value: 1.69e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536   587 ILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRsQIAIVPQEPVLFN-CSIAEN 665
Cdd:TIGR01189  15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHE-NILYLGHLPGLKPeLSALEN 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536   666 IAYgdnsrvvpldeikeaanAANIHSFIEGPPEKYNTQVGLKG------AQLSGGQKQRLAIARALLQKPKILLLDEATS 739
Cdd:TIGR01189  94 LHF-----------------WAAIHGGAQRTIEDALAAVGLTGfedlpaAQLSAGQQRRLALARLWLSRRPLWILDEPTT 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 56849536   740 ALDNDSEKVVQHALDkARTGRTCLVV--THRLSAIQNADLI 778
Cdd:TIGR01189 157 ALDKAGVALLAGLLR-AHLARGGIVLltTHQDLGLVEAREL 196
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
570-776 1.81e-10

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127  Cd Length: 200  Bit Score: 59.96  E-value: 1.81e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536  570 LEFREVSFFYPCRPdvfILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRSQIA 649
Cdd:PRK13540   2 LDVIELDFDYHDQP---LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536  650 IVPQEPVLFNCSIAENIAYGDNSRVVPLdEIKEAANAANIHSFIEGPpekyntqVGLkgaqLSGGQKQRLAIARALLQKP 729
Cdd:PRK13540  79 VGHRSGINPYLTLRENCLYDIHFSPGAV-GITELCRLFSLEHLIDYP-------CGL----LSSGQKRQVALLRLWMSKA 146
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 56849536  730 KILLLDEATSALDNDSEKVVQHALDKART-GRTCLVVTHRLSAIQNAD 776
Cdd:PRK13540 147 KLWLLDEPLVALDELSLLTIITKIQEHRAkGGAVLLTSHQDLPLNKAD 194
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
78-135 8.72e-06

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


Pssm-ID: 273491  Cd Length: 198  Bit Score: 45.81  E-value: 8.72e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 56849536    78 AQMSGGQKQRIAIARALVRNPKILILDEATSALDSESEsAVQAALEKASKGRTTIVVA 135
Cdd:TIGR01189 126 AQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGV-ALLAGLLRAHLARGGIVLL 182
PRK13541 PRK13541
cytochrome c biogenesis protein CcmA; Provisional
68-151 3.84e-03

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184128  Cd Length: 195  Bit Score: 37.93  E-value: 3.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536   68 KFNTLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSALDSESESAVQAALE-KASKGRTTIVVAHRLSTIRSAdL 146
Cdd:PRK13541 112 KLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVmKANSGGIVLLSSHLESSIKSA-Q 190

                 ....*
gi 56849536  147 IVTLK 151
Cdd:PRK13541 191 ILQLD 195
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; ...
232-810 3.14e-130

ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; linked to 3D-structure


Pssm-ID: 224055 [Multi-domain]  Cd Length: 567  Bit Score: 403.35  E-value: 3.14e-130
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 232 SLLKILKLNKPEWPFVvLGTLASVLNGTVHPVFSIIFAKIITMFGNNdkttlKHDAEIYSMIFVILGVICFVSYFMQGLF 311
Cdd:COG1132   2 SLLRRLLKYLKYKLLL-LAILLLLLSALLSLLLPLLIGRIIDALLAD-----LGELLELLLLLLLLALLGGVLRALQSYL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 312 YGRAGEILTMRLRHLAFKAMLYQDIAWFDEkeNSTGGLTTILAIDIAQIQGATGSRIGVLTQNATNMGLSVIISFIYGWE 391
Cdd:COG1132  76 GSRLGQKIVADLRRDLFEKLLRLPLSFFDK--AKSGDLISRLTNDVEAVSNLVSTVLVLVFTSILLLIGSLVLLFSLSWR 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 392 MTFLILSIAPVLAVTGMIETAAMTGFANKDKQELKHAGKIATEALENIRTIVSLTREKAFEQMYEEMLQTQHRNTSKKAQ 471
Cdd:COG1132 154 LALILLLILPLLALVLSLLARKSRKLSRRVREALGELNARLLESLSGIRVIKAFGAEDRELKRFEEANEELRRANLRASR 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 472 IIGSCYAFSHAFIYFAYAAGFRFGAYLIQAGRMTPEGMFIVFTAIAYGAMAIGKTLVLAPEYSKAKSGAAHLFALLEKKP 551
Cdd:COG1132 234 LEALLAPLMLLLSSLGTVLVLALGGFLVLSGSLTVGALAAFILYLLRLLTPILQLGEVVSLLQRASAAAERLFELLDEEP 313
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 552 NIDSrsqEGKKPDTCEGNLEFREVSFFYPcrPDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLF 631
Cdd:COG1132 314 EVED---PPDPLKDTIGSIEFENVSFSYP--GKKPVLKDISFSIEPGEKVAIVGPSGSGKSTLIKLLLRLYDPTSGEILI 388
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 632 DGVDAKELNVQWLRSQIAIVPQEPVLFNCSIAENIAYGDNSrvVPLDEIKEAANAANIHSFIEGPPEKYNTQVGLKGAQL 711
Cdd:COG1132 389 DGIDIRDISLDSLRKRIGIVSQDPLLFSGTIRENIALGRPD--ATDEEIEEALKLANAHEFIANLPDGYDTIVGERGVNL 466
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 712 SGGQKQRLAIARALLQKPKILLLDEATSALDNDSEKVVQHALDKARTGRTCLVVTHRLSAIQNADLIVVLHNGKIKEQGT 791
Cdd:COG1132 467 SGGQRQRLAIARALLRNPPILILDEATSALDTETEALIQDALKKLLKGRTTLIIAHRLSTIKNADRIIVLDNGRIVERGT 546
                       570
                ....*....|....*....
gi 56849536 792 HQELLRNRDIYFKLVNAQS 810
Cdd:COG1132 547 HEELLAKGGLYARLYQAQG 565
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
3-806 3.80e-131

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 427.52  E-value: 3.80e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536     3 DENDIRALNVRHYRDHIGVVSQEPVLFGTTISNNIKYG---------------------RDD------------------ 43
Cdd:PTZ00265  446 DSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSlyslkdlealsnyynedgndsQENknkrnscrakcagdlndm 525
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536    44 ------------------VTDEEMERAAREANAYDFIMEFPNKFNTLVGEKGAQMSGGQKQRIAIARALVRNPKILILDE 105
Cdd:PTZ00265  526 snttdsneliemrknyqtIKDSEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDE 605
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536   106 ATSALDSESESAVQAALE--KASKGRTTIVVAHRLSTIRSADLIVTL------------------------------KDG 153
Cdd:PTZ00265  606 ATSSLDNKSEYLVQKTINnlKGNENRITIIIAHRLSTIRYANTIFVLsnrergstvdvdiigedptkdnkennnknnKDD 685
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536   154 -----------------MLAEKGAHAELMA-KRGLYYSLVMSQDIKKA---------DEQMESMTYS-TER-----KTNS 200
Cdd:PTZ00265  686 nnnnnnnnnnkinnagsYIIEQGTHDALMKnKNGIYYTMINNQKVSSKkssnndndkDSDMKSSAYKdSERgydpdEMNG 765
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536   201 LPLHSVKSIKSDFIDKAEESTQSKEISLPEVSLLKILKLNKPEWPF---------------VVLGTLASVLNGTVHPVFS 265
Cdd:PTZ00265  766 NSKHENESASNKKSCKMSDENASENNAGGKLPFLRNLFKRKPKAPNnlrivyreifsykkdVTIIALSILVAGGLYPVFA 845
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536   266 IIFAKII-TMFgnnDKTTLKHDAEIYSMIFVILGVICFVSYFMQGLFYGRAGEILTMRLRHLAFKAMLYQDIAWFDEKEN 344
Cdd:PTZ00265  846 LLYAKYVsTLF---DFANLEANSNKYSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMKRRLFENILYQEISFFDQDKH 922
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536   345 STGGLTTILAIDIAQIQGATGSRIGVLTQNATNMGLSVIISF----IYGWEMTFL------ILSIAPVLAVTGMIETAAM 414
Cdd:PTZ00265  923 APGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSMVMSFyfcpIVAAVLTGTyfifmrVFAIRARLTANKDVEKKEI 1002
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536   415 ----TGFA-NKDKQELKHAGKIATEALENIRTIVSLTREKAFEQMYEEMLQTQHRNTSKKAQIIGSCYAFSHAFIYFAYA 489
Cdd:PTZ00265 1003 nqpgTVFAyNSDDEIFKDPSFLIQEAFYNMNTVIIYGLEDYFCNLIEKAIDYSNKGQKRKTLVNSMLWGFSQSAQLFINS 1082
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536   490 AGFRFGAYLIQAGRMTPEG-MFIVFTAIAYGAMAiGKTLVLAPEYSKAKSGAAHLFALLEKKPNIDSRSQEG---KKPDT 565
Cdd:PTZ00265 1083 FAYWFGSFLIRRGTILVDDfMKSLFTFLFTGSYA-GKLMSLKGDSENAKLSFEKYYPLIIRKSNIDVRDNGGiriKNKND 1161
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536   566 CEGNLEFREVSFFYPCRPDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYD---------------------- 623
Cdd:PTZ00265 1162 IKGKIEIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqd 1241
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536   624 --------------------------------PVQGQVLFDGVDAKELNVQWLRSQIAIVPQEPVLFNCSIAENIAYGDN 671
Cdd:PTZ00265 1242 yqgdeeqnvgmknvnefsltkeggsgedstvfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKE 1321
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536   672 SrvVPLDEIKEAANAANIHSFIEGPPEKYNTQVGLKGAQLSGGQKQRLAIARALLQKPKILLLDEATSALDNDSEKVVQH 751
Cdd:PTZ00265 1322 D--ATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEK 1399
                         970       980       990      1000      1010      1020
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 56849536   752 AL----DKArtGRTCLVVTHRLSAIQNADLIVVLHNGK-----IKEQGTHQELLRNRD-IYFKLV 806
Cdd:PTZ00265 1400 TIvdikDKA--DKTIITIAHRIASIKRSDKIVVFNNPDrtgsfVQAHGTHEELLSVQDgVYKKYV 1462
MsbA_rel TIGR02204
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ...
288-809 9.35e-113

ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.


Pssm-ID: 131259 [Multi-domain]  Cd Length: 576  Bit Score: 357.86  E-value: 9.35e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536   288 EIYSMIFVILGVICFVSyFMQGLFYGRAGEILTMRLRHLAFKAMLYQDIAWFDEkeNSTGGLTTILAIDIAQIQGATGSR 367
Cdd:TIGR02204  59 RYFAFLLVVALVLALGT-AARFYLVTWLGERVVADIRRAVFAHLISLSPSFFDK--NRSGEVVSRLTTDTTLLQSVIGSS 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536   368 IGVLTQNATNMGLSVIISFIYGWEMTFLILS-----IAPVLAVTGMIETAAMTgfaNKDKqeLKHAGKIATEALENIRTI 442
Cdd:TIGR02204 136 LSMALRNALMCIGGLIMMFITSPKLTSLVLLavplvLLPILLFGRRVRKLSRE---SQDR--IADAGSYAGETLGAIRTV 210
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536   443 VSLTREKAFEQMYEEMLQTQHRNTSKKAQIIGSCYAFSHAFIYFAYAAGFRFGAYLIQAGRMTPE--GMFIVFTAIAygA 520
Cdd:TIGR02204 211 QAFGHEDAERSRFGGAVEKAYEAARQRIRTRALLTAIVIVLVFGAIVGVLWVGAHDVIAGKMSAGtlGQFVFYAVMV--A 288
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536   521 MAIGKTLVLAPEYSKAKSGAAHLFALLEKKPNIDSRSQEGKKPDTCEGNLEFREVSFFYPCRPDVFILRGLSLSIERGKT 600
Cdd:TIGR02204 289 GSIGTLSEVWGELQRAAGAAERLIELLQAEPDIKAPAHPKTLPVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGET 368
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536   601 VAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRSQIAIVPQEPVLFNCSIAENIAYG--DNSRvvplD 678
Cdd:TIGR02204 369 VALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGrpDATD----E 444
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536   679 EIKEAANAANIHSFIEGPPEKYNTQVGLKGAQLSGGQKQRLAIARALLQKPKILLLDEATSALDNDSEKVVQHALDKART 758
Cdd:TIGR02204 445 EVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMK 524
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 56849536   759 GRTCLVVTHRLSAIQNADLIVVLHNGKIKEQGTHQELLRNRDIYFKLVNAQ 809
Cdd:TIGR02204 525 GRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGGLYARLARLQ 575
PRK11176 PRK11176
lipid transporter ATP-binding/permease protein; Provisional
275-809 3.79e-91

lipid transporter ATP-binding/permease protein; Provisional


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 300.40  E-value: 3.79e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536  275 FGNNDKTTLKHDAEIYSMIFVILGVICFVS-YFMQGLfygrAGEILtMRLRHLAFKAMLYQDIAWFDEkeNSTGGLTTIL 353
Cdd:PRK11176  56 FGKADRSVLKWMPLVVIGLMILRGITSFISsYCISWV----SGKVV-MTMRRRLFGHMMGMPVSFFDK--QSTGTLLSRI 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536  354 AIDIAQIQGAT-GSRIGVLTQNATNMGLsVIISFIYGWEMTFLILSIAPVLAVTgmIETAAmTGFANKDKQELKHAGKIA 432
Cdd:PRK11176 129 TYDSEQVASSSsGALITVVREGASIIGL-FIMMFYYSWQLSLILIVIAPIVSIA--IRVVS-KRFRNISKNMQNTMGQVT 204
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536  433 TEA---LENIRTIVSL----TREKAFEQMYEEMLQTQHRNTSKKA------QIIGScyaFSHAFIYfaYAAGFRFGAYLI 499
Cdd:PRK11176 205 TSAeqmLKGHKEVLIFggqeVETKRFDKVSNRMRQQGMKMVSASSisdpiiQLIAS---LALAFVL--YAASFPSVMDTL 279
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536  500 QAGRMTpegmfIVFTAIaYGAMAIGKTLV-LAPEYSKAKSGAAHLFALLEKKPNIDsrsqEGK-KPDTCEGNLEFREVSF 577
Cdd:PRK11176 280 TAGTIT-----VVFSSM-IALMRPLKSLTnVNAQFQRGMAACQTLFAILDLEQEKD----EGKrVIERAKGDIEFRNVTF 349
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536  578 FYPCRpDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRSQIAIVPQEPVL 657
Cdd:PRK11176 350 TYPGK-EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHL 428
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536  658 FNCSIAENIAYGDN---SRvvplDEIKEAANAANIHSFIEGPPEKYNTQVGLKGAQLSGGQKQRLAIARALLQKPKILLL 734
Cdd:PRK11176 429 FNDTIANNIAYARTeqySR----EQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILIL 504
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 56849536  735 DEATSALDNDSEKVVQHALDKARTGRTCLVVTHRLSAIQNADLIVVLHNGKIKEQGTHQELLRNRDIYFKLVNAQ 809
Cdd:PRK11176 505 DEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQLHKMQ 579
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; ...
1-178 1.26e-69

ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; linked to 3D-structure


Pssm-ID: 224055 [Multi-domain]  Cd Length: 567  Bit Score: 241.18  E-value: 1.26e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536   1 MVDENDIRALNVRHYRDHIGVVSQEPVLFGTTISNNIKYGRDDVTDEEMERAAREANAYDFIMEFPNKFNTLVGEKGAQM 80
Cdd:COG1132 387 LIDGIDIRDISLDSLRKRIGIVSQDPLLFSGTIRENIALGRPDATDEEIEEALKLANAHEFIANLPDGYDTIVGERGVNL 466
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536  81 SGGQKQRIAIARALVRNPKILILDEATSALDSESESAVQAALEKASKGRTTIVVAHRLSTIRSADLIVTLKDGMLAEKGA 160
Cdd:COG1132 467 SGGQRQRLAIARALLRNPPILILDEATSALDTETEALIQDALKKLLKGRTTLIIAHRLSTIKNADRIIVLDNGRIVERGT 546
                       170
                ....*....|....*...
gi 56849536 161 HAELMAKRGLYYSLVMSQ 178
Cdd:COG1132 547 HEELLAKGGLYARLYQAQ 564
PRK13657 PRK13657
cyclic beta-1,2-glucan ABC transporter; Provisional
1-196 2.14e-66

cyclic beta-1,2-glucan ABC transporter; Provisional


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 232.54  E-value: 2.14e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536    1 MVDENDIRALNVRHYRDHIGVVSQEPVLFGTTISNNIKYGRDDVTDEEMERAAREANAYDFIMEFPNKFNTLVGEKGAQM 80
Cdd:PRK13657 393 LIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQL 472
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536   81 SGGQKQRIAIARALVRNPKILILDEATSALDSESESAVQAALEKASKGRTTIVVAHRLSTIRSADLIVTLKDGMLAEKGA 160
Cdd:PRK13657 473 SGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGS 552
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 56849536  161 HAELMAKRGLYYSLVMSQDIKKADEQMESMTYSTER 196
Cdd:PRK13657 553 FDELVARGGRFAALLRAQGMLQEDERRKQPAAEGAN 588
MsbA_rel TIGR02204
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ...
1-178 3.03e-64

ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.


Pssm-ID: 131259 [Multi-domain]  Cd Length: 576  Bit Score: 226.12  E-value: 3.03e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536     1 MVDENDIRALNVRHYRDHIGVVSQEPVLFGTTISNNIKYGRDDVTDEEMERAAREANAYDFIMEFPNKFNTLVGEKGAQM 80
Cdd:TIGR02204 398 LLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTL 477
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536    81 SGGQKQRIAIARALVRNPKILILDEATSALDSESESAVQAALEKASKGRTTIVVAHRLSTIRSADLIVTLKDGMLAEKGA 160
Cdd:TIGR02204 478 SGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGT 557
                         170
                  ....*....|....*...
gi 56849536   161 HAELMAKRGLYYSLVMSQ 178
Cdd:TIGR02204 558 HAELIAKGGLYARLARLQ 575
PLN03232 PLN03232
ABC transporter C family member; Provisional
16-808 2.65e-54

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 203.67  E-value: 2.65e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536    16 RDHIGVVSQEPVLFGTTISNNIKYGrddvTDEEMERAAREANA----YDFIMeFPNKFNTLVGEKGAQMSGGQKQRIAIA 91
Cdd:PLN03232  678 RGSVAYVPQVSWIFNATVRENILFG----SDFESERYWRAIDVtalqHDLDL-LPGRDLTEIGERGVNISGGQKQRVSMA 752
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536    92 RALVRNPKILILDEATSALDSESESAV-QAALEKASKGRTTIVVAHRLSTIRSADLIVTLKDGMLAEKGAHAELmAKRGL 170
Cdd:PLN03232  753 RAVYSNSDIYIFDDPLSALDAHVAHQVfDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAEL-SKSGS 831
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536   171 YYSLVM--------SQDIKKADEQMESMTYSTERKTNSLPLHSV---KSIKSDFIDKAEESTQSkeislpeVSLLKILKL 239
Cdd:PLN03232  832 LFKKLMenagkmdaTQEVNTNDENILKLGPTVTIDVSERNLGSTkqgKRGRSVLVKQEERETGI-------ISWNVLMRY 904
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536   240 NKPE---WpfVVLGTLASVLNGTVHPVFSIIFAKIITmfgnnDKTTLK-HDAEIYSMIFVILGVICFVSYFMQGLFYGRA 315
Cdd:PLN03232  905 NKAVgglW--VVMILLVCYLTTEVLRVSSSTWLSIWT-----DQSTPKsYSPGFYIVVYALLGFGQVAVTFTNSFWLISS 977
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536   316 GEILTMRLRHLAFKAMLYQDIAWFDEkeNSTGGLTTILAIDIAQIQgatgSRIGVLTQNATNMGLSVIISF-IYGWEMTF 394
Cdd:PLN03232  978 SLHAAKRLHDAMLNSILRAPMLFFHT--NPTGRVINRFSKDIGDID----RNVANLMNMFMNQLWQLLSTFaLIGTVSTI 1051
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536   395 LILSIAPVLavtgMIETAAMTGFANKDKqELKHAGKIATEAL-----ENIRTIVSLTREKAFEQM-------YEEMLQTQ 462
Cdd:PLN03232 1052 SLWAIMPLL----ILFYAAYLYYQSTSR-EVRRLDSVTRSPIyaqfgEALNGLSSIRAYKAYDRMakingksMDNNIRFT 1126
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536   463 HRNTSKKAQIIGSCYAFSHAFIYF-AYAAGFRFGAYLIQAGRMTPEGMFIVFTaiaygamaIGKTLVLAPEYSKAKSGAA 541
Cdd:PLN03232 1127 LANTSSNRWLTIRLETLGGVMIWLtATFAVLRNGNAENQAGFASTMGLLLSYT--------LNITTLLSGVLRQASKAEN 1198
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536   542 HLFALLEKKPNIDSRSQ-----EGKKPDT---CEGNLEFREVSFFYpcRPDVF-ILRGLSLSIERGKTVAFVGSSGCGKS 612
Cdd:PLN03232 1199 SLNSVERVGNYIDLPSEataiiENNRPVSgwpSRGSIKFEDVHLRY--RPGLPpVLHGLSFFVSPSEKVGVVGRTGAGKS 1276
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536   613 TSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRSQIAIVPQEPVLFNCSIAENIAygdnsrvvPLDE-----IKEAANAA 687
Cdd:PLN03232 1277 SMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNID--------PFSEhndadLWEALERA 1348
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536   688 NIHSFIEGPPEKYNTQVGLKGAQLSGGQKQRLAIARALLQKPKILLLDEATSALDNDSEKVVQHALDKARTGRTCLVVTH 767
Cdd:PLN03232 1349 HIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAH 1428
                         810       820       830       840
                  ....*....|....*....|....*....|....*....|..
gi 56849536   768 RLSAIQNADLIVVLHNGKIKEQGTHQELL-RNRDIYFKLVNA 808
Cdd:PLN03232 1429 RLNTIIDCDKILVLSSGQVLEYDSPQELLsRDTSAFFRMVHS 1470
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
1-175 4.81e-41

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 161.74  E-value: 4.81e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536     1 MVDENDIRALNVRHYRDHIGVVSQEPVLFGTTISNNIKYGRDDVTDEEMERAAREANAYDFIMEFPNKFNTLVGEKGAQM 80
Cdd:PTZ00265 1280 LLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSL 1359
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536    81 SGGQKQRIAIARALVRNPKILILDEATSALDSESESAVQAALE--KASKGRTTIVVAHRLSTIRSADLIVTLKD-----G 153
Cdd:PTZ00265 1360 SGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVdiKDKADKTIITIAHRIASIKRSDKIVVFNNpdrtgS 1439
                         170       180
                  ....*....|....*....|...
gi 56849536   154 MLAEKGAHAELM-AKRGLYYSLV 175
Cdd:PTZ00265 1440 FVQAHGTHEELLsVQDGVYKKYV 1462
PLN03232 PLN03232
ABC transporter C family member; Provisional
1-201 2.95e-23

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 105.06  E-value: 2.95e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536     1 MVDENDIRALNVRHYRDHIGVVSQEPVLFGTTISNNIKYGRDDvTDEEMERAAREANAYDFIMEFPNKFNTLVGEKGAQM 80
Cdd:PLN03232 1294 MIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEH-NDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENF 1372
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536    81 SGGQKQRIAIARALVRNPKILILDEATSALDSESESAVQAALEKASKGRTTIVVAHRLSTIRSADLIVTLKDGMLAEKGA 160
Cdd:PLN03232 1373 SVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDS 1452
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 56849536   161 HAELMAKRGLYYSLvMSQDIKKADEQ-MESMTYstERKTNSL 201
Cdd:PLN03232 1453 PQELLSRDTSAFFR-MVHSTGPANAQyLSNLVF--ERRENGM 1491
ycf16 CHL00131
sulfate ABC transporter protein; Validated
587-791 3.11e-13

sulfate ABC transporter protein; Validated


Pssm-ID: 214372 [Multi-domain]  Cd Length: 252  Bit Score: 69.29  E-value: 3.11e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536  587 ILRGLSLSIERGKTVAFVGSSGCGKSTSVQLL--QRLYDPVQGQVLFDGVDAKELNVQwLRSQIAIVP--QEPVLFNCSI 662
Cdd:CHL00131  22 ILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIagHPAYKILEGDILFKGESILDLEPE-ERAHLGIFLafQYPIEIPGVS 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536  663 AEN---IAYGDNSRVVPLDEIKEAanaanihSFIEGPPEKYNTqVGLKGAQL--------SGGQKQRLAIARALLQKPKI 731
Cdd:CHL00131 101 NADflrLAYNSKRKFQGLPELDPL-------EFLEIINEKLKL-VGMDPSFLsrnvnegfSGGEKKRNEILQMALLDSEL 172
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 56849536  732 LLLDEATSALDNDSEKVVQHALDKARTGRTCLV-VTH--RLSAIQNADLIVVLHNGKIKEQGT 791
Cdd:CHL00131 173 AILDETDSGLDIDALKIIAEGINKLMTSENSIIlITHyqRLLDYIKPDYVHVMQNGKIIKTGD 235
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
597-778 3.34e-11

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 62.01  E-value: 3.34e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536    597 RGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRSQIAIvpqepvlfncsiaeniaygdnsrvvp 676
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIV-------------------------- 54
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536    677 ldeikeaanaanihsfiegppekyntqvGLKGAQLSGGQKQRLAIARALLQKPKILLLDEATSALDNDSEKVVQHALD-- 754
Cdd:smart00382  55 ----------------------------GGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElr 106
                          170       180
                   ....*....|....*....|....*....
gi 56849536    755 -----KARTGRTCLVVTHRLSAIQNADLI 778
Cdd:smart00382 107 lllllKSEKNLTVILTTNDEKDLGPALLR 135
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
70-147 1.07e-08

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 54.30  E-value: 1.07e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536     70 NTLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSALDSESESAVQAALE-------KASKGRTTIVVAHRLSTIR 142
Cdd:smart00382  51 LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrlllllKSEKNLTVILTTNDEKDLG 130

                   ....*
gi 56849536    143 SADLI 147
Cdd:smart00382 131 PALLR 135
 
Name Accession Description Interval E-value
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
571-809 5.58e-141

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


Pssm-ID: 213216 [Multi-domain]  Cd Length: 238  Bit Score: 418.87  E-value: 5.58e-141
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 571 EFREVSFFYPCRPDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRSQIAI 650
Cdd:cd03249   2 EFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 651 VPQEPVLFNCSIAENIAYGDNSRVVplDEIKEAANAANIHSFIEGPPEKYNTQVGLKGAQLSGGQKQRLAIARALLQKPK 730
Cdd:cd03249  82 VSQEPVLFDGTIAENIRYGKPDATD--EEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPK 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 56849536 731 ILLLDEATSALDNDSEKVVQHALDKARTGRTCLVVTHRLSAIQNADLIVVLHNGKIKEQGTHQELLRNRDIYFKLVNAQ 809
Cdd:cd03249 160 ILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
1-178 1.14e-102

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


Pssm-ID: 213216 [Multi-domain]  Cd Length: 238  Bit Score: 319.10  E-value: 1.14e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536   1 MVDENDIRALNVRHYRDHIGVVSQEPVLFGTTISNNIKYGRDDVTDEEMERAAREANAYDFIMEFPNKFNTLVGEKGAQM 80
Cdd:cd03249  61 LLDGVDIRDLNLRWLRSQIGLVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQL 140
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536  81 SGGQKQRIAIARALVRNPKILILDEATSALDSESESAVQAALEKASKGRTTIVVAHRLSTIRSADLIVTLKDGMLAEKGA 160
Cdd:cd03249 141 SGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGT 220
                       170
                ....*....|....*...
gi 56849536 161 HAELMAKRGLYYSLVMSQ 178
Cdd:cd03249 221 HDELMAQKGVYAKLVKAQ 238
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
570-805 4.83e-98

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


Pssm-ID: 213218 [Multi-domain]  Cd Length: 234  Bit Score: 306.85  E-value: 4.83e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 570 LEFREVSFFYPCRPDvFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRSQIA 649
Cdd:cd03251   1 VEFKNVTFRYPGDGP-PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 650 IVPQEPVLFNCSIAENIAYGDnsRVVPLDEIKEAANAANIHSFIEGPPEKYNTQVGLKGAQLSGGQKQRLAIARALLQKP 729
Cdd:cd03251  80 LVSQDVFLFNDTVAENIAYGR--PGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDP 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 56849536 730 KILLLDEATSALDNDSEKVVQHALDKARTGRTCLVVTHRLSAIQNADLIVVLHNGKIKEQGTHQELLRNRDIYFKL 805
Cdd:cd03251 158 PILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
570-809 1.92e-96

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


Pssm-ID: 213220 [Multi-domain]  Cd Length: 236  Bit Score: 302.61  E-value: 1.92e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 570 LEFREVSFFYPcrPDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRSQIA 649
Cdd:cd03253   1 IEFENVTFAYD--PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 650 IVPQEPVLFNCSIAENIAYGDNSrvVPLDEIKEAANAANIHSFIEGPPEKYNTQVGLKGAQLSGGQKQRLAIARALLQKP 729
Cdd:cd03253  79 VVPQDTVLFNDTIGYNIRYGRPD--ATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNP 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 730 KILLLDEATSALDNDSEKVVQHALDKARTGRTCLVVTHRLSAIQNADLIVVLHNGKIKEQGTHQELLRNRDIYFKLVNAQ 809
Cdd:cd03253 157 PILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
568-800 1.60e-89

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


Pssm-ID: 213221 [Multi-domain]  Cd Length: 229  Bit Score: 284.12  E-value: 1.60e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 568 GNLEFREVSFFYpcRPDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRSQ 647
Cdd:cd03254   1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 648 IAIVPQEPVLFNCSIAENIAYGDNSrvVPLDEIKEAANAANIHSFIEGPPEKYNTQVGLKGAQLSGGQKQRLAIARALLQ 727
Cdd:cd03254  79 IGVVLQDTFLFSGTIMENIRLGRPN--ATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLR 156
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 56849536 728 KPKILLLDEATSALDNDSEKVVQHALDKARTGRTCLVVTHRLSAIQNADLIVVLHNGKIKEQGTHQELLRNRD 800
Cdd:cd03254 157 DPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
563-786 2.19e-83

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


Pssm-ID: 213215 [Multi-domain]  Cd Length: 226  Bit Score: 267.80  E-value: 2.19e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 563 PDTCEGNLEFREVSFFYPCRPDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQ 642
Cdd:cd03248   5 PDHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHK 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 643 WLRSQIAIVPQEPVLFNCSIAENIAYGDNSrvVPLDEIKEAANAANIHSFIEGPPEKYNTQVGLKGAQLSGGQKQRLAIA 722
Cdd:cd03248  85 YLHSKVSLVGQEPVLFARSLQDNIAYGLQS--CSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIA 162
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 56849536 723 RALLQKPKILLLDEATSALDNDSEKVVQHALDKARTGRTCLVVTHRLSAIQNADLIVVLHNGKI 786
Cdd:cd03248 163 RALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
2-174 3.22e-81

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


Pssm-ID: 213218 [Multi-domain]  Cd Length: 234  Bit Score: 262.17  E-value: 3.22e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536   2 VDENDIRALNVRHYRDHIGVVSQEPVLFGTTISNNIKYGRDDVTDEEMERAAREANAYDFIMEFPNKFNTLVGEKGAQMS 81
Cdd:cd03251  61 IDGHDVRDYTLASLRRQIGLVSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLS 140
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536  82 GGQKQRIAIARALVRNPKILILDEATSALDSESESAVQAALEKASKGRTTIVVAHRLSTIRSADLIVTLKDGMLAEKGAH 161
Cdd:cd03251 141 GGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTH 220
                       170
                ....*....|...
gi 56849536 162 AELMAKRGLYYSL 174
Cdd:cd03251 221 EELLAQGGVYAKL 233
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
570-809 3.54e-80

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


Pssm-ID: 213219 [Multi-domain]  Cd Length: 237  Bit Score: 259.34  E-value: 3.54e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 570 LEFREVSFFYpcRPD-VFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRSQI 648
Cdd:cd03252   1 ITFEHVRFRY--KPDgPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 649 AIVPQEPVLFNCSIAENIAYGDNSrvVPLDEIKEAANAANIHSFIEGPPEKYNTQVGLKGAQLSGGQKQRLAIARALLQK 728
Cdd:cd03252  79 GVVLQENVLFNRSIRDNIALADPG--MSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHN 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 729 PKILLLDEATSALDNDSEKVVQHALDKARTGRTCLVVTHRLSAIQNADLIVVLHNGKIKEQGTHQELLRNRDIYFKLVNA 808
Cdd:cd03252 157 PRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQL 236

                .
gi 56849536 809 Q 809
Cdd:cd03252 237 Q 237
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
570-785 3.91e-79

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


Pssm-ID: 213195 [Multi-domain]  Cd Length: 171  Bit Score: 254.23  E-value: 3.91e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 570 LEFREVSFFYPCRPdVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRSQIA 649
Cdd:cd03228   1 IEFKNVSFSYPGRP-KPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 650 IVPQEPVLFNCSIAENIaygdnsrvvpldeikeaanaanihsfiegppekyntqvglkgaqLSGGQKQRLAIARALLQKP 729
Cdd:cd03228  80 YVPQDPFLFSGTIRENI--------------------------------------------LSGGQRQRIAIARALLRDP 115
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 56849536 730 KILLLDEATSALDNDSEKVVQHALDKARTGRTCLVVTHRLSAIQNADLIVVLHNGK 785
Cdd:cd03228 116 PILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
2-178 9.48e-79

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


Pssm-ID: 213220 [Multi-domain]  Cd Length: 236  Bit Score: 255.62  E-value: 9.48e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536   2 VDENDIRALNVRHYRDHIGVVSQEPVLFGTTISNNIKYGRDDVTDEEMERAAREANAYDFIMEFPNKFNTLVGEKGAQMS 81
Cdd:cd03253  60 IDGQDIREVTLDSLRRAIGVVPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLS 139
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536  82 GGQKQRIAIARALVRNPKILILDEATSALDSESESAVQAALEKASKGRTTIVVAHRLSTIRSADLIVTLKDGMLAEKGAH 161
Cdd:cd03253 140 GGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTH 219
                       170
                ....*....|....*..
gi 56849536 162 AELMAKRGLYYSLVMSQ 178
Cdd:cd03253 220 EELLAKGGLYAEMWKAQ 236
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
2-169 1.37e-68

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


Pssm-ID: 213221 [Multi-domain]  Cd Length: 229  Bit Score: 227.49  E-value: 1.37e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536   2 VDENDIRALNVRHYRDHIGVVSQEPVLFGTTISNNIKYGRDDVTDEEMERAAREANAYDFIMEFPNKFNTLVGEKGAQMS 81
Cdd:cd03254  62 IDGIDIRDISRKSLRSMIGVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLS 141
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536  82 GGQKQRIAIARALVRNPKILILDEATSALDSESESAVQAALEKASKGRTTIVVAHRLSTIRSADLIVTLKDGMLAEKGAH 161
Cdd:cd03254 142 QGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTH 221

                ....*...
gi 56849536 162 AELMAKRG 169
Cdd:cd03254 222 DELLAKKG 229
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
568-790 2.17e-67

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


Pssm-ID: 213212 [Multi-domain]  Cd Length: 220  Bit Score: 224.01  E-value: 2.17e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 568 GNLEFREVSFFYPCRPDVfILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRSQ 647
Cdd:cd03245   1 GRIEFRNVSFSYPNQEIP-ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 648 IAIVPQEPVLFNCSIAENIAYGDnsRVVPLDEIKEAANAANIHSFIEGPPEKYNTQVGLKGAQLSGGQKQRLAIARALLQ 727
Cdd:cd03245  80 IGYVPQDVTLFYGTLRDNITLGA--PLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLN 157
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 56849536 728 KPKILLLDEATSALDNDSEKVVQHALDKARTGRTCLVVTHRLSAIQNADLIVVLHNGKIKEQG 790
Cdd:cd03245 158 DPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
1-178 1.35e-62

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


Pssm-ID: 213219 [Multi-domain]  Cd Length: 237  Bit Score: 211.19  E-value: 1.35e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536   1 MVDENDIRALNVRHYRDHIGVVSQEPVLFGTTISNNIKYGRDDVTDEEMERAAREANAYDFIMEFPNKFNTLVGEKGAQM 80
Cdd:cd03252  60 LVDGHDLALADPAWLRRQVGVVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGL 139
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536  81 SGGQKQRIAIARALVRNPKILILDEATSALDSESESAVQAALEKASKGRTTIVVAHRLSTIRSADLIVTLKDGMLAEKGA 160
Cdd:cd03252 140 SGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGS 219
                       170
                ....*....|....*...
gi 56849536 161 HAELMAKRGLYYSLVMSQ 178
Cdd:cd03252 220 HDELLAENGLYAYLYQLQ 237
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
568-791 1.29e-61

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


Pssm-ID: 213211 [Multi-domain]  Cd Length: 221  Bit Score: 207.73  E-value: 1.29e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 568 GNLEFREVSFFYpcRPD-VFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRS 646
Cdd:cd03244   1 GDIEFKNVSLRY--RPNlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 647 QIAIVPQEPVLFNCSIAENIA----YGDnsrvvplDEIKEAANAANIHSFIEGPPEKYNTQVGLKGAQLSGGQKQRLAIA 722
Cdd:cd03244  79 RISIIPQDPVLFSGTIRSNLDpfgeYSD-------EELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLA 151
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 56849536 723 RALLQKPKILLLDEATSALDNDSEKVVQHALDKARTGRTCLVVTHRLSAIQNADLIVVLHNGKIKEQGT 791
Cdd:cd03244 152 RALLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
1-155 1.00e-54

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


Pssm-ID: 213215 [Multi-domain]  Cd Length: 226  Bit Score: 188.45  E-value: 1.00e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536   1 MVDENDIRALNVRHYRDHIGVVSQEPVLFGTTISNNIKYGRDDVTDEEMERAAREANAYDFIMEFPNKFNTLVGEKGAQM 80
Cdd:cd03248  72 LLDGKPISQYEHKYLHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQL 151
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 56849536  81 SGGQKQRIAIARALVRNPKILILDEATSALDSESESAVQAALEKASKGRTTIVVAHRLSTIRSADLIVTLKDGML 155
Cdd:cd03248 152 SGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
570-793 1.41e-50

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


Pssm-ID: 213227 [Multi-domain]  Cd Length: 227  Bit Score: 176.99  E-value: 1.41e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 570 LEFREVSFFYPcrpDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYD-----PVQGQVLFDGVD--AKELNVQ 642
Cdd:cd03260   1 IELRDLNVYYG---DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDiyDLDVDVL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 643 WLRSQIAIVPQEPVLFNCSIAENIAYGdnsrvVPLDEIKEaanaaniHSFIEGPPEKYNTQVGL--------KGAQLSGG 714
Cdd:cd03260  78 ELRRRVGMVFQKPNPFPGSIYDNVAYG-----LRLHGIKL-------KEELDERVEEALRKAALwdevkdrlHALGLSGG 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 715 QKQRLAIARALLQKPKILLLDEATSALDNDSEKVVQHALDKARTGRTCLVVTHRLS-AIQNADLIVVLHNGKIKEQG-TH 792
Cdd:cd03260 146 QQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQqAARVADRTAFLLNGRLVEFGpTE 225

                .
gi 56849536 793 Q 793
Cdd:cd03260 226 Q 226
ABC_membrane pfam00664
ABC transporter transmembrane region; This family represents a unit of six transmembrane ...
251-523 1.26e-49

ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.


Pssm-ID: 250039  Cd Length: 274  Bit Score: 175.94  E-value: 1.26e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536   251 TLASVLNGTVHPVFSIIFAKII-TMFGNNDKTTLKHDAEIYSMIFVILGVICFVSYFMQGLFYGraGEILTMRLRHLAFK 329
Cdd:pfam00664   1 LLIGILLLILAGATALVFPLLLgRFLDSLIDGNGDERSSLISLAILLIAVGVLQGLLLQGYFYL--GERLGQRIRKRLFR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536   330 AMLYQDIAWFDE--KENSTGGLTTILAIDIAQIQGATGSRIGVLTQNATNMGLSVIISFIYGWEMTFLILSIAPVLAVTG 407
Cdd:pfam00664  79 ALLRQILGLFMSffDTNSVGELTSRLTNDVSKIRDGLGDKLGLFFQSLATVVGGFIVMFYYGWKLTLVLLAILPLLILLS 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536   408 MIETAAMTGFANKDKQELKHAGKIATEALENIRTIVSLTREKAFEQMYEEMLQTQHRNTSKKAQIIGSCYAFSHAFIYFA 487
Cdd:pfam00664 159 AVLAKKLRKLNRKEQKAYAKAGSVAEESLSGIRTVKAFGREEYELERYDKALEDAEKAGIKKAIAAGLSFGITQFISYLS 238
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 56849536   488 YAAGFRFGAYLIQAGRMTPEGMFIVFTAIAYGAMAI 523
Cdd:pfam00664 239 YALALWFGGYLVISGGLSVGTVFAFLSLGLQLSGPL 274
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
570-789 7.97e-48

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: 169.19  E-value: 7.97e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 570 LEFREVSFFYP-CRPDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNvqwlrSQI 648
Cdd:cd03293   1 LEVRNVSKTYGgGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG-----PDR 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 649 AIVPQEPVLFN-CSIAENIAYGDNSRVVPLDEIKEAAnaaniHSFIEgppekyntQVGLKGA------QLSGGQKQRLAI 721
Cdd:cd03293  76 GYVFQQDALLPwLTVLDNVALGLELQGVPKAEARERA-----EELLE--------LVGLSGFenayphQLSGGMRQRVAL 142
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 56849536 722 ARALLQKPKILLLDEATSALDNDSEKVVQHALDK--ARTGRTCLVVTHRLS-AIQNADLIVVLHN--GKIKEQ 789
Cdd:cd03293 143 ARALAVDPDVLLLDEPFSALDALTREQLQEELLDiwRETGKTVLLVTHDIDeAVFLADRVVVLSArpGRIVAE 215
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
2-153 1.97e-47

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


Pssm-ID: 213195 [Multi-domain]  Cd Length: 171  Bit Score: 166.40  E-value: 1.97e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536   2 VDENDIRALNVRHYRDHIGVVSQEPVLFGTTISNNIkygrddvtdeemeraareanaydfimefpnkfntlvgekgaqMS 81
Cdd:cd03228  61 IDGVDLRDLDLESLRKNIAYVPQDPFLFSGTIRENI------------------------------------------LS 98
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 56849536  82 GGQKQRIAIARALVRNPKILILDEATSALDSESESAVQAALEKASKGRTTIVVAHRLSTIRSADLIVTLKDG 153
Cdd:cd03228  99 GGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
570-790 2.14e-46

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: 164.02  E-value: 2.14e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 570 LEFREVSFFYPCRPDVfILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQwLRSQIA 649
Cdd:cd03247   1 LSINNVSFSYPEQEQQ-VLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-LSSLIS 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 650 IVPQEPVLFNCSIAENIaygdnsrvvpldeikeaanaanihsfiegppekyntqvglkGAQLSGGQKQRLAIARALLQKP 729
Cdd:cd03247  79 VLNQRPYLFDTTLRNNL-----------------------------------------GRRFSGGERQRLALARILLQDA 117
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 56849536 730 KILLLDEATSALDNDSEKVVQHALDKARTGRTCLVVTHRLSAIQNADLIVVLHNGKIKEQG 790
Cdd:cd03247 118 PIVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
571-785 6.96e-46

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: 163.41  E-value: 6.96e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 571 EFREVSFFYPcRPDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRSQIAI 650
Cdd:cd03225   1 ELKNLSFSYP-DGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 651 VPQEP--VLFNCSIAENIAYGDNSRVVPLDEIKEAANAA----NIHSFIEGPPEkyntqvglkgaQLSGGQKQRLAIARA 724
Cdd:cd03225  80 VFQNPddQFFGPTVEEEVAFGLENLGLPEEEIEERVEEAlelvGLEGLRDRSPF-----------TLSGGQKQRVAIAGV 148
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 56849536 725 LLQKPKILLLDEATSALDNDSEKVVQHALDK-ARTGRTCLVVTHRLSAIQN-ADLIVVLHNGK 785
Cdd:cd03225 149 LAMDPDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
570-790 1.02e-45

ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.


Pssm-ID: 213224 [Multi-domain]  Cd Length: 228  Bit Score: 163.83  E-value: 1.02e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 570 LEFREVSFFYPCRPD-VFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWL---R 645
Cdd:cd03257   2 LEVKNLSVSFPTGGGsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirR 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 646 SQIAIVPQEPVL-FN--CSIAENIA--YGDNSRVVPLDEIKEAANAANIHsfIEGPPEKYNtqvgLKGAQLSGGQKQRLA 720
Cdd:cd03257  82 KEIQMVFQDPMSsLNprMTIGEQIAepLRIHGKLSKKEARKEAVLLLLVG--VGLPEEVLN----RYPHELSGGQRQRVA 155
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 56849536 721 IARALLQKPKILLLDEATSALDNDSEKVVQHALDKART--GRTCLVVTHRLSAIQN-ADLIVVLHNGKIKEQG 790
Cdd:cd03257 156 IARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
570-790 2.28e-45

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: 162.30  E-value: 2.28e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 570 LEFREVSFFYPcrpDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQwlRSQIA 649
Cdd:cd03259   1 LELKGLSKTYG---SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIG 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 650 IVPQEPVLF-NCSIAENIAYGDNSRVVPLDEIKEAANAANIHSFIEGPPEKYNtqvglkgAQLSGGQKQRLAIARALLQK 728
Cdd:cd03259  76 MVFQDYALFpHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYP-------HELSGGQQQRVALARALARE 148
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 56849536 729 PKILLLDEATSALDNDSEKVVQHALDK--ARTGRTCLVVTHRLS-AIQNADLIVVLHNGKIKEQG 790
Cdd:cd03259 149 PSLLLLDEPLSALDAKLREELREELKElqRELGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
570-786 4.19e-45

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


Pssm-ID: 213213 [Multi-domain]  Cd Length: 173  Bit Score: 160.07  E-value: 4.19e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 570 LEFREVSFFYP--CRPdvfILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRSQ 647
Cdd:cd03246   1 LEVENVSFRYPgaEPP---VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDH 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 648 IAIVPQEPVLFNCSIAENIaygdnsrvvpldeikeaanaanihsfiegppekyntqvglkgaqLSGGQKQRLAIARALLQ 727
Cdd:cd03246  78 VGYLPQDDELFSGSIAENI--------------------------------------------LSGGQRQRLGLARALYG 113
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 728 KPKILLLDEATSALDNDSEKVVQHALDKAR-TGRTCLVVTHRLSAIQNADLIVVLHNGKI 786
Cdd:cd03246 114 NPRILVLDEPNSHLDVEGERALNQAIAALKaAGATRIVIAHRPETLASADRILVLEDGRV 173
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
588-739 5.28e-43

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: 249501  Cd Length: 150  Bit Score: 153.57  E-value: 5.28e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536   588 LRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRSQIAIVPQEPVLFN-CSIAENI 666
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPGLFPrLTVRENL 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 56849536   667 AYG----DNSRVVPLDEIKEAANAANIhsfiegpPEKYNTQVGLKGAQLSGGQKQRLAIARALLQKPKILLLDEATS 739
Cdd:pfam00005  81 RLGlllkGLSKREKDARAEEALEKLGL-------GDLLDRPVGENPGTLSGGQKQRVAIARALLTKPKLLLLDEPTA 150
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
570-798 7.46e-43

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


Pssm-ID: 213262 [Multi-domain]  Cd Length: 242  Bit Score: 156.31  E-value: 7.46e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 570 LEFREVSFFYPCRPdvFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRSQIA 649
Cdd:cd03295   1 IEFENVTKRYGGGK--KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 650 IVPQEPVLF-NCSIAENIAygdnsrVVP----LDEIKEAANAANIHSFIEGPPEKYntqVGLKGAQLSGGQKQRLAIARA 724
Cdd:cd03295  79 YVIQQIGLFpHMTVEENIA------LVPkllkWPKEKIRERADELLALVGLDPAEF---ADRYPHELSGGQQQRVGVARA 149
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 56849536 725 LLQKPKILLLDEATSALDNDSEKVVQHALDK--ARTGRTCLVVTHRL-SAIQNADLIVVLHNGKIKEQGTHQELLRN 798
Cdd:cd03295 150 LAADPPLLLMDEPFGALDPITRDQLQEEFKRlqQELGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILRS 226
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
570-785 3.00e-42

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: 152.34  E-value: 3.00e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 570 LEFREVSFFYPcrpDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDG--VDAKELNVQWLRSQ 647
Cdd:cd03229   1 LELKNVSKRYG---QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGedLTDLEDELPPLRRR 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 648 IAIVPQEPVLF-NCSIAENIAYGdnsrvvpldeikeaanaanihsfiegppekyntqvglkgaqLSGGQKQRLAIARALL 726
Cdd:cd03229  78 IGMVFQDFALFpHLTVLENIALG-----------------------------------------LSGGQQQRVALARALA 116
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 56849536 727 QKPKILLLDEATSALDNDSEKVVQHALD--KARTGRTCLVVTHRLS-AIQNADLIVVLHNGK 785
Cdd:cd03229 117 MDPDVLLLDEPTSALDPITRREVRALLKslQAQLGITVVLVTHDLDeAARLADRVVVLRDGK 178
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
1-153 1.95e-41

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


Pssm-ID: 213212 [Multi-domain]  Cd Length: 220  Bit Score: 151.59  E-value: 1.95e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536   1 MVDENDIRALNVRHYRDHIGVVSQEPVLFGTTISNNIKYGRDDVTDEEMERAAREANAYDFIMEFPNKFNTLVGEKGAQM 80
Cdd:cd03245  62 LLDGTDIRQLDPADLRRNIGYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGL 141
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 56849536  81 SGGQKQRIAIARALVRNPKILILDEATSALDSESESAVQAALEKASKGRTTIVVAHRLSTIRSADLIVTLKDG 153
Cdd:cd03245 142 SGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSG 214
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
570-785 3.66e-41

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


Pssm-ID: 213217 [Multi-domain]  Cd Length: 204  Bit Score: 150.31  E-value: 3.66e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 570 LEFREVSFFYPCRPDV--FILRGLSLSIERGKTVAFVGSSGCGKSTsvqLLQRL---YDPVQGQVlfdgvdakelnvqWL 644
Cdd:cd03250   1 ISVEDASFTWDSGEQEtsFTLKDINLEVPKGELVAIVGPVGSGKSS---LLSALlgeLEKLSGSV-------------SV 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 645 RSQIAIVPQEPVLFNCSIAENIAYGdnsrvVPLDE--IKEAANAANIHSFIEGPPEKYNTQVGLKGAQLSGGQKQRLAIA 722
Cdd:cd03250  65 PGSIAYVSQEPWIQNGTIRENILFG-----KPFDEerYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLA 139
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 56849536 723 RALLQKPKILLLDEATSALDND-SEKVVQHALDKA-RTGRTCLVVTHRLSAIQNADLIVVLHNGK 785
Cdd:cd03250 140 RAVYSDADIYLLDDPLSAVDAHvGRHIFENCILGLlLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
568-791 1.13e-40

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


Pssm-ID: 213269 [Multi-domain]  Cd Length: 207  Bit Score: 149.10  E-value: 1.13e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 568 GNLEFREVSFFYpcRPDV-FILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRS 646
Cdd:cd03369   5 GEIEVENLSVRY--APDLpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 647 QIAIVPQEPVLFNCSIAENI----AYGDnsrvvplDEIKEAANAAnihsfiEGppekyntqvglkGAQLSGGQKQRLAIA 722
Cdd:cd03369  83 SLTIIPQDPTLFSGTIRSNLdpfdEYSD-------EEIYGALRVS------EG------------GLNLSQGQRQLLCLA 137
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 56849536 723 RALLQKPKILLLDEATSALDNDSEKVVQHALDKARTGRTCLVVTHRLSAIQNADLIVVLHNGKIKEQGT 791
Cdd:cd03369 138 RALLKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
571-785 2.47e-40

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: 146.24  E-value: 2.47e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 571 EFREVSFFYPcrpDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRSQIAI 650
Cdd:cd00267   1 EIENLSFRYG---GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 651 VPQepvlfncsiaeniaygdnsrvvpldeikeaanaanihsfiegppekyntqvglkgaqLSGGQKQRLAIARALLQKPK 730
Cdd:cd00267  78 VPQ---------------------------------------------------------LSGGQRQRVALARALLLNPD 100
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 56849536 731 ILLLDEATSALDNDS-EKVVQHALDKARTGRTCLVVTHRLSAIQNA-DLIVVLHNGK 785
Cdd:cd00267 101 LLLLDEPTSGLDPASrERLLELLRELAEEGRTVIIVTHDPELAELAaDRVIVLKDGK 157
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
2-160 2.47e-40

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


Pssm-ID: 213211 [Multi-domain]  Cd Length: 221  Bit Score: 148.41  E-value: 2.47e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536   2 VDENDIRALNVRHYRDHIGVVSQEPVLFGTTISNNI----KYgrddvTDEEMERAAREANAYDFIMEFPNKFNTLVGEKG 77
Cdd:cd03244  63 IDGVDISKIGLHDLRSRISIIPQDPVLFSGTIRSNLdpfgEY-----SDEELWQALERVGLKEFVESLPGGLDTVVEEGG 137
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536  78 AQMSGGQKQRIAIARALVRNPKILILDEATSALDSESESAVQAALEKASKGRTTIVVAHRLSTIRSADLIVTLKDGMLAE 157
Cdd:cd03244 138 ENLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVE 217

                ...
gi 56849536 158 KGA 160
Cdd:cd03244 218 FDS 220
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
570-786 4.34e-40

ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and cell division protein; 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. An FtsE null mutants showed filamentous growth and appeared viable on high salt medium only, indicating a role for FtsE in cell division and/or salt transport. 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: 147.64  E-value: 4.34e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 570 LEFREVSFFYPCRPD-VFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWL---- 644
Cdd:cd03255   1 IELKNLSKTYGGGGEkVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 645 RSQIAIVPQE----PVLfncSIAENIAYGDNSRVVPLDEIKEAAnaaniHSFIEgppekyntQVGLKG------AQLSGG 714
Cdd:cd03255  81 RRHIGFVFQSfnllPDL---TALENVELPLLLAGVPKKERRERA-----EELLE--------RVGLGDrlnhypSELSGG 144
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 56849536 715 QKQRLAIARALLQKPKILLLDEATSALDNDSEKVVQHALDK--ARTGRTCLVVTHRLSAIQNADLIVVLHNGKI 786
Cdd:cd03255 145 QQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRElnKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistant to organic solvents; ABC ...
570-800 6.78e-39

ATP-binding cassette transport system involved in resistant 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: 144.95  E-value: 6.78e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 570 LEFREVSFFYPCRPdvfILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNV---QWLRS 646
Cdd:cd03261   1 IELRGLTKSFGGRT---VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEaelYRLRR 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 647 QIAIVPQEPVLFNC-SIAENIAYG--DNSRvVPLDEIKEAANaanihsfiegppEKYNTqVGLKG------AQLSGGQKQ 717
Cdd:cd03261  78 RMGMLFQSGALFDSlTVFENVAFPlrEHTR-LSEEEIREIVL------------EKLEA-VGLRGaedlypAELSGGMKK 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 718 RLAIARALLQKPKILLLDEATSALDN-DSEKVVQHALD-KARTGRTCLVVTHRL-SAIQNADLIVVLHNGKIKEQGTHQE 794
Cdd:cd03261 144 RVALARALALDPELLLYDEPTAGLDPiASGVIDDLIRSlKKELGLTSIMVTHDLdTAFAIADRIAVLYDGKIVAEGTPEE 223

                ....*.
gi 56849536 795 LLRNRD 800
Cdd:cd03261 224 LRASDD 229
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
570-798 9.67e-39

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: 144.26  E-value: 9.67e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 570 LEFREVSFFYPCRPDVFI-LRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELN---VQWLR 645
Cdd:cd03258   2 IELKNVSKVFGDTGGKVTaLKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSgkeLRKAR 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 646 SQIAIVPQEPVLFNC-SIAENIAYGDNSRVVPLDEIKEAANAanihsFIEgppekyntQVGLKG------AQLSGGQKQR 718
Cdd:cd03258  82 RRIGMIFQHFNLLSSrTVFENVALPLEIAGVPKAEIEERVLE-----LLE--------LVGLEDkadaypAQLSGGQKQR 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 719 LAIARALLQKPKILLLDEATSALDNDSEKVVQHALDK--ARTGRTCLVVTHRLSAIQN-ADLIVVLHNGKIKEQGTHQEL 795
Cdd:cd03258 149 VGIARALANNPKVLLCDEATSALDPETTQSILALLRDinRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEV 228

                ...
gi 56849536 796 LRN 798
Cdd:cd03258 229 FAN 231
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
570-795 2.34e-38

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: 143.15  E-value: 2.34e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 570 LEFREVSFFYPcrpDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAkeLNVQWLRSQIA 649
Cdd:cd03300   1 IELENVSKFYG---GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--TNLPPHKRPVN 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 650 IVPQEPVLF-NCSIAENIAYGDNSRVVPLDEIKEAANAAnIHsfiegppekyntQVGLKG------AQLSGGQKQRLAIA 722
Cdd:cd03300  76 TVFQNYALFpHLTVFENIAFGLRLKKLPKAEIKERVAEA-LD------------LVQLEGyanrkpSQLSGGQQQRVAIA 142
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 56849536 723 RALLQKPKILLLDEATSALDNDSEKVVQHALDK--ARTGRTCLVVTHRLS-AIQNADLIVVLHNGKIKEQGTHQEL 795
Cdd:cd03300 143 RALVNEPKVLLLDEPLGALDLKLRKDMQLELKRlqKELGITFVFVTHDQEeALTMSDRIAVMNKGKIQQIGTPEEI 218
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
571-790 6.34e-37

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


Pssm-ID: 213181 [Multi-domain]  Cd Length: 180  Bit Score: 137.57  E-value: 6.34e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 571 EFREVSFFYPCRPdvfILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRSQIAI 650
Cdd:cd03214   1 EVENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 651 VPQepvlfncsiaeniaygdnsrvvpldeikeAANAANIHSFIEgppEKYNTqvglkgaqLSGGQKQRLAIARALLQKPK 730
Cdd:cd03214  78 VPQ-----------------------------ALELLGLAHLAD---RPFNE--------LSGGERQRVLLARALAQEPP 117
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 56849536 731 ILLLDEATSALDndsekvVQHALD--------KARTGRTCLVVTHRLS-AIQNADLIVVLHNGKIKEQG 790
Cdd:cd03214 118 ILLLDEPTSHLD------IAHQIEllellrrlARERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
587-786 1.27e-36

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


Pssm-ID: 213229 [Multi-domain]  Cd Length: 213  Bit Score: 137.66  E-value: 1.27e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 587 ILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDG--VDAKELNVQWLRSQIAIVPQEPVLF-NCSIA 663
Cdd:cd03262  15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGlkLTDDKKNINELRQKVGMVFQQFNLFpHLTVL 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 664 ENIAYGD-NSRVVPLDEIKEAAnaanihsfiegppEKYNTQVGLKG------AQLSGGQKQRLAIARALLQKPKILLLDE 736
Cdd:cd03262  95 ENITLAPiKVKGMSKAEAEERA-------------LELLEKVGLADkadaypAQLSGGQQQRVAIARALAMNPKVMLFDE 161
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 56849536 737 ATSALD----NDSEKVVQhalDKARTGRTCLVVTHRLS-AIQNADLIVVLHNGKI 786
Cdd:cd03262 162 PTSALDpelvGEVLDVMK---DLAEEGMTMVVVTHEMGfAREVADRVIFMDDGRI 213
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
570-786 3.10e-36

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: 135.22  E-value: 3.10e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 570 LEFREVSFFYPcrpDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQwLRSQIA 649
Cdd:cd03230   1 IEVRNLSKRYG---KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEE-VKRRIG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 650 IVPQEPVLF-NCSIAENIaygdnsrvvpldeikeaanaanihsfiegppekyntqvglkgaQLSGGQKQRLAIARALLQK 728
Cdd:cd03230  77 YLPEEPSLYeNLTVRENL-------------------------------------------KLSGGMKQRLALAQALLHD 113
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 729 PKILLLDEATSALDNDSEKVVQHALDK-ARTGRTCLVVTHRLSAIQN-ADLIVVLHNGKI 786
Cdd:cd03230 114 PELLILDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
586-798 5.35e-36

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


Pssm-ID: 213266 [Multi-domain]  Cd Length: 235  Bit Score: 136.70  E-value: 5.35e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 586 FILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQwlRSQIAIVPQEPVLF-NCSIAE 664
Cdd:cd03299  13 FKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFpHMTVYK 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 665 NIAYGDNSRVVPLDEIK----EAANAANIHSFIEGPPEKyntqvglkgaqLSGGQKQRLAIARALLQKPKILLLDEATSA 740
Cdd:cd03299  91 NIAYGLKKRKVDKKEIErkvlEIAEMLGIDHLLNRKPET-----------LSGGEQQRVAIARALVVNPKILLLDEPFSA 159
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 56849536 741 LDNDSEKVVQHALDKAR--TGRTCLVVTHRLSAIQN-ADLIVVLHNGKIKEQGTHQELLRN 798
Cdd:cd03299 160 LDVRTKEKLREELKKIRkeFGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKK 220
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
588-798 2.20e-35

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: 135.16  E-value: 2.20e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 588 LRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQwlRSQIAIVPQEPVLF-NCSIAENI 666
Cdd:cd03296  18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVGFVFQHYALFrHMTVFDNV 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 667 AYG----DNSRVVPLDEIKEAANAANIHSFIEGPPEKYNtqvglkgAQLSGGQKQRLAIARALLQKPKILLLDEATSALD 742
Cdd:cd03296  96 AFGlrvkPRSERPPEAEIRAKVHELLKLVQLDWLADRYP-------AQLSGGQRQRVALARALAVEPKVLLLDEPFGALD 168
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 56849536 743 NDSEKVVQHALDKA--RTGRTCLVVTHRLS-AIQNADLIVVLHNGKIKEQGTHQELLRN 798
Cdd:cd03296 169 AKVRKELRRWLRRLhdELHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPDEVYDH 227
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
588-798 3.31e-33

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


Pssm-ID: 213261 [Multi-domain]  Cd Length: 269  Bit Score: 129.69  E-value: 3.31e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 588 LRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWL----RSQIAIVPQEPVLF-NCSI 662
Cdd:cd03294  40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLpHRTV 119
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 663 AENIAYGDNSRVVPLDEIKEAANAAnihsfIEgppekyntQVGLKG------AQLSGGQKQRLAIARALLQKPKILLLDE 736
Cdd:cd03294 120 LENVAFGLEVQGVPRAEREERAAEA-----LE--------LVGLEGwehkypDELSGGMQQRVGLARALAVDPDILLMDE 186
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 56849536 737 ATSALDNDSEKVVQHALDK--ARTGRTCLVVTHRLS-AIQNADLIVVLHNGKIKEQGTHQELLRN 798
Cdd:cd03294 187 AFSALDPLIRREMQDELLRlqAELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILTN 251
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
570-795 8.65e-33

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


Pssm-ID: 213223 [Multi-domain]  Cd Length: 241  Bit Score: 127.68  E-value: 8.65e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 570 LEFREVSFFYPcrPDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVD---AKELNVQWLRS 646
Cdd:cd03256   1 IEVENLSKTYP--NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDinkLKGKALRQLRR 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 647 QIAIVPQEPVLFN-CSIAENIAYGDNSRV---------VPLDEIKEAANAANihsfiegppekyntQVGLKG------AQ 710
Cdd:cd03256  79 QIGMIFQQFNLIErLSVLENVLSGRLGRRstwrslfglFPKEEKQRALAALE--------------RVGLLDkayqraDQ 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 711 LSGGQKQRLAIARALLQKPKILLLDEATSALDNDSEKVVQHALDKART--GRTCLVVTHRLS-AIQNADLIVVLHNGKIK 787
Cdd:cd03256 145 LSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINReeGITVIVSLHQVDlAREYADRIVGLKDGRIV 224

                ....*...
gi 56849536 788 EQGTHQEL 795
Cdd:cd03256 225 FDGPPAEL 232
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
571-790 1.32e-32

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: 126.11  E-value: 1.32e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 571 EFREVSFFYPCRPdvfILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELnvqwlRSQIAI 650
Cdd:cd03235   1 EVEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGY 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56849536 651 VPQEPVL---FNCSIAENIAYGDNSRVVPLDEI----KEAANAAnihsfIEgppekyntQVGLKG------AQLSGGQKQ 717
Cdd:cd03235  73 VPQRRSIdrdFPISVRDVVLMGLYGHKGLFRRLskadKAKVDEA-----LE