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Conserved domains on  [gi|404223395|emb|CBY74757|]
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ABC transporter, ATP-binding/permease protein [Listeria monocytogenes SLCC2540]

Protein Classification

ABC transporter ATP-binding protein( domain architecture ID 11438555)

ABC transporter ATP-binding protein ABC transporter ATP-binding protein containing both ATPase and permease components of an ABC-type transport system

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
1-575 0e+00

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


:

Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 673.03  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395   1 MESMKWIWQYVRKYRLLMIGVFILIFIASGISIIYPLLGGKVIDDVVYQNKTNLLIPLLLIMIISTIIRTICRYTYQIMC 80
Cdd:COG1132    6 RKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQRYLL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  81 ERIGQNSLFRIREDLYKKLQSLDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENVFLFSFAIIIMAAIDWKLTL 160
Cdd:COG1132   86 ARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLAL 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 161 ALVIVTPLIAILTMKMSSKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSR 240
Cdd:COG1132  166 IVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSA 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 241 TYLPVLDSLAGMLVVITLIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPMRMSGWLINDVQRFIASSFKIQDMMATDAKIP 320
Cdd:COG1132  246 LFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEIP 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 321 IHAE-KPAPSLQGHVEFKNVSFHFEDDpnTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVD 399
Cdd:COG1132  326 DPPGaVPLPPVRGEIEFENVSFSYPGD--RPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVD 403
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 400 ARKWHVRELRNHIATVMQDIFLFSDTIEGNIAFGAPDATMEDVRRMARIADADHFIETMPESYDTIVGERGVGLSGGQKQ 479
Cdd:COG1132  404 IRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQ 483
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 480 RISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHRISSVKEADEILILNHGEIIERGTHSSLLA 559
Cdd:COG1132  484 RIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLA 563
                        570
                 ....*....|....*.
gi 404223395 560 EKGYYFDIYNKQLGTE 575
Cdd:COG1132  564 RGGLYARLYRLQFGEE 579
 
Name Accession Description Interval E-value
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
1-575 0e+00

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 673.03  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395   1 MESMKWIWQYVRKYRLLMIGVFILIFIASGISIIYPLLGGKVIDDVVYQNKTNLLIPLLLIMIISTIIRTICRYTYQIMC 80
Cdd:COG1132    6 RKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQRYLL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  81 ERIGQNSLFRIREDLYKKLQSLDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENVFLFSFAIIIMAAIDWKLTL 160
Cdd:COG1132   86 ARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLAL 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 161 ALVIVTPLIAILTMKMSSKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSR 240
Cdd:COG1132  166 IVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSA 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 241 TYLPVLDSLAGMLVVITLIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPMRMSGWLINDVQRFIASSFKIQDMMATDAKIP 320
Cdd:COG1132  246 LFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEIP 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 321 IHAE-KPAPSLQGHVEFKNVSFHFEDDpnTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVD 399
Cdd:COG1132  326 DPPGaVPLPPVRGEIEFENVSFSYPGD--RPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVD 403
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 400 ARKWHVRELRNHIATVMQDIFLFSDTIEGNIAFGAPDATMEDVRRMARIADADHFIETMPESYDTIVGERGVGLSGGQKQ 479
Cdd:COG1132  404 IRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQ 483
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 480 RISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHRISSVKEADEILILNHGEIIERGTHSSLLA 559
Cdd:COG1132  484 RIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLA 563
                        570
                 ....*....|....*.
gi 404223395 560 EKGYYFDIYNKQLGTE 575
Cdd:COG1132  564 RGGLYARLYRLQFGEE 579
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
7-574 2.40e-128

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


Pssm-ID: 131258 [Multi-domain]  Cd Length: 571  Bit Score: 387.92  E-value: 2.40e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395    7 IWQYVRKYRLLMIGVFILIFIASGISIIYPLLGGKVIDDVVYQNKTNLLIPLLLIMIISTIIRTICRYTYQIMCERIGQN 86
Cdd:TIGR02203   5 LWSYVRPYKAGLVLAGVAMILVAATESTLAALLKPLLDDGFGGRDRSVLWWVPLVVIGLAVLRGICSFVSTYLLSWVSNK 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395   87 SLFRIREDLYKKLQSLDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENVFLFSFAIIIMAAIDWKLTLALVIVT 166
Cdd:TIGR02203  85 VVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLTLIVVVML 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  167 PLIAILTMKMSSKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSRTYLPVL 246
Cdd:TIGR02203 165 PVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSAGSISSPIT 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  247 DSLAGMLVVITLIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPMRMSGWLINDVQRFIASSFKIQDMMATdakiPIHAE-- 324
Cdd:TIGR02203 245 QLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDS----PPEKDtg 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  325 -KPAPSLQGHVEFKNVSFHFEDDpNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKW 403
Cdd:TIGR02203 321 tRAIERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADY 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  404 HVRELRNHIATVMQDIFLFSDTIEGNIAFGAP-DATMEDVRRMARIADADHFIETMPESYDTIVGERGVGLSGGQKQRIS 482
Cdd:TIGR02203 400 TLASLRRQVALVSQDVVLFNDTIANNIAYGRTeQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLA 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  483 LARALLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHRISSVKEADEILILNHGEIIERGTHSSLLAEKG 562
Cdd:TIGR02203 480 IARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNG 559
                         570
                  ....*....|..
gi 404223395  563 YYFDIYNKQLGT 574
Cdd:TIGR02203 560 LYAQLHNMQFRE 571
ABC_6TM_YknU_like cd18542
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ...
18-309 1.13e-125

Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349986 [Multi-domain]  Cd Length: 292  Bit Score: 370.99  E-value: 1.13e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  18 MIGVFILIFIASGISIIYPLLGGKVIDDVVYQNKTNLLIPLLLIMIISTIIRTICRYTYQIMCERIGQNSLFRIREDLYK 97
Cdd:cd18542    1 YLLAILALLLATALNLLIPLLIRRIIDSVIGGGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  98 KLQSLDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENVFLFSFAIIIMAAIDWKLTLALVIVTPLIAILTMKMS 177
Cdd:cd18542   81 HLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYVFF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 178 SKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSRTYLPVLDSLAGMLVVIT 257
Cdd:cd18542  161 KKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVLV 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 404223395 258 LIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPMRMSGWLINDVQRFIASSFKI 309
Cdd:cd18542  241 LWVGGYLVINGEITLGELVAFISYLWMLIWPVRQLGRLINDMSRASASAERI 292
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
21-571 5.27e-112

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


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 345.93  E-value: 5.27e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  21 VFILIFIASgISIIYPLLGGKVIDDVVYQNKTNLLIPLLLIMIIST-IIRTICRYTYQIMcerigqnsLF--------RI 91
Cdd:PRK10789   1 VALLIIIAM-LQLIPPKVVGIIVDGVTEQHMTTGQILMWIGTMVLIaVVVYLLRYVWRVL--------LFgasyqlavEL 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  92 REDLYKKLQSLDFDFFNNTRVGDIMARMTGDTDAIRhFVSWVSYNILENVFLFSFAIIIMAA--IDWKLTLALVIVTPLI 169
Cdd:PRK10789  72 REDFYRQLSRQHPEFYLRHRTGDLMARATNDVDRVV-FAAGEGVLTLVDSLVMGCAVLIVMStqISWQLTLLALLPMPVM 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 170 AILTMKMSSKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSRTYLPVLDSL 249
Cdd:PRK10789 151 AIMIKRYGDQLHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARIDARFDPTIYIA 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 250 AGMLVVITLIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPMRMSGWLINDVQRFIASSFKIQDMMAtDAKIPIHAEKPAPS 329
Cdd:PRK10789 231 IGMANLLAIGGGSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRIRAMLA-EAPVVKDGSEPVPE 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 330 LQGHVEFKNVSFHFeddPNTD--VLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRE 407
Cdd:PRK10789 310 GRGELDVNIRQFTY---PQTDhpALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDS 386
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 408 LRNHIATVMQDIFLFSDTIEGNIAFGAPDATMEDVRRMARIADADHFIETMPESYDTIVGERGVGLSGGQKQRISLARAL 487
Cdd:PRK10789 387 WRSRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARAL 466
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 488 LKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHRISSVKEADEILILNHGEIIERGTHSSLLAEKGYYFDI 567
Cdd:PRK10789 467 LLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDM 546

                 ....
gi 404223395 568 YNKQ 571
Cdd:PRK10789 547 YRYQ 550
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
352-501 1.92e-46

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


Pssm-ID: 394964 [Multi-domain]  Cd Length: 150  Bit Score: 160.12  E-value: 1.92e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  352 LKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIATVMQDIFLFSD-TIEGNI 430
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 404223395  431 AFGapdATMEDVRRMARIADADHFIETMPESY--DTIVGERGVGLSGGQKQRISLARALLKNPSILILDDTTS 501
Cdd:pfam00005  81 RLG---LLLKGLSKREKDARAEEALEKLGLGDlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
361-553 1.45e-10

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 59.69  E-value: 1.45e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395   361 PGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIdgvdarkwhvrelrnhiatvmqdiflfsdtiegniafgapdatme 440
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY--------------------------------------------- 35
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395   441 dvrrmarIADADHFIETMPESYDTIVGERGVGLSGGQKQRISLARALLKNPSILILDDTTSAVDMETEVKIQ-------G 513
Cdd:smart00382  36 -------IDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleelrlL 108
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 404223395   514 ELKKITENTTTFIIAHRISSVKEADEILILNHGEIIERGT 553
Cdd:smart00382 109 LLLKSEKNLTVILTTNDEKDLGPALLRRRFDRRIVLLLIL 148
GguA NF040905
sugar ABC transporter ATP-binding protein;
352-550 3.44e-10

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 62.50  E-value: 3.44e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 352 LKNISLKASPGQTIAILGETGAGKSTLVNLICRFYdPT---SGEILIDGVDARKWHVRELRNH-IATVMQDIFLFSD-TI 426
Cdd:NF040905  17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGEVCRFKDIRDSEALgIVIIHQELALIPYlSI 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 427 EGNIAFGAPDATMEDVRRMARIADADHFIET--MPESYDTIVGERGVGlsggQKQRISLARALLKNPSILILDDTTSAV- 503
Cdd:NF040905  96 AENIFLGNERAKRGVIDWNETNRRARELLAKvgLDESPDTLVTDIGVG----KQQLVEIAKALSKDVKLLILDEPTAALn 171
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 404223395 504 --DMETEVKIQGELKKitENTTTFIIAHRISSVKE-ADEILILNHGEIIE 550
Cdd:NF040905 172 eeDSAALLDLLLELKA--QGITSIIISHKLNEIRRvADSITVLRDGRTIE 219
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
368-504 1.50e-07

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 54.36  E-value: 1.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 368 LGETGAGKST----LVNLIcrfyDPTSGEILIDG--VDARKWHVR--------------ELrnhiaTVMQDIFLFsdtie 427
Cdd:NF033858 298 LGSNGCGKSTtmkmLTGLL----PASEGEAWLFGqpVDAGDIATRrrvgymsqafslygEL-----TVRQNLELH----- 363
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 428 gniA--FGAPDATMED-VRRMARIADADHFIETMPESydtivgergvgLSGGQKQRISLARALLKNPSILILDDTTSAVD 504
Cdd:NF033858 364 ---ArlFHLPAAEIAArVAEMLERFDLADVADALPDS-----------LPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
334-504 2.76e-07

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 53.59  E-value: 2.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFEDdpnTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVD-ARKWHVRELRNHI 412
Cdd:NF033858   2 ARLEGVSHRYGK---TVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDmADARHRRAVCPRI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 413 ATVMQDI--FLFSD-TIEGNIAF-----GAPDAtmEDVRRMARIADA---DHFietmpesydtivGERGVG-LSGGQKQR 480
Cdd:NF033858  79 AYMPQGLgkNLYPTlSVFENLDFfgrlfGQDAA--ERRRRIDELLRAtglAPF------------ADRPAGkLSGGMKQK 144
                        170       180
                 ....*....|....*....|....
gi 404223395 481 ISLARALLKNPSILILDDTTSAVD 504
Cdd:NF033858 145 LGLCCALIHDPDLLILDEPTTGVD 168
GguA NF040905
sugar ABC transporter ATP-binding protein;
335-504 1.24e-06

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 51.33  E-value: 1.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 335 EFKNVSFHFEDDPNTDVLKNISLKASPGQTIAILGETGAGKSTL-VNLICRFYDP-TSGEILIDGVDARKWHVRE-LRNH 411
Cdd:NF040905 259 EVKNWTVYHPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELaMSVFGRSYGRnISGTVFKDGKEVDVSTVSDaIDAG 338
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 412 IATVMQDI----FLFSDTIEGNIafgapdaTMEDVRRMARIADADHFIET-MPESYDT---I----VGERGVGLSGGQKQ 479
Cdd:NF040905 339 LAYVTEDRkgygLNLIDDIKRNI-------TLANLGKVSRRGVIDENEEIkVAEEYRKkmnIktpsVFQKVGNLSGGNQQ 411
                        170       180
                 ....*....|....*....|....*
gi 404223395 480 RISLARALLKNPSILILDDTTSAVD 504
Cdd:NF040905 412 KVVLSKWLFTDPDVLILDEPTRGID 436
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
441-562 1.77e-06

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 50.50  E-value: 1.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 441 DVRRMARIADADHFIETMpeSYDTIVGERGVGLSGGQKQRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITE 520
Cdd:NF000106 115 DLSRKDARARADELLERF--SLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVR 192
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 404223395 521 NTTTFIIAHRISSVKE--ADEILILNHGEIIERGTHSSLLAEKG 562
Cdd:NF000106 193 DGATVLLTTQYMEEAEqlAHELTVIDRGRVIADGKVDELKTKVG 236
 
Name Accession Description Interval E-value
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
1-575 0e+00

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 673.03  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395   1 MESMKWIWQYVRKYRLLMIGVFILIFIASGISIIYPLLGGKVIDDVVYQNKTNLLIPLLLIMIISTIIRTICRYTYQIMC 80
Cdd:COG1132    6 RKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQRYLL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  81 ERIGQNSLFRIREDLYKKLQSLDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENVFLFSFAIIIMAAIDWKLTL 160
Cdd:COG1132   86 ARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLAL 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 161 ALVIVTPLIAILTMKMSSKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSR 240
Cdd:COG1132  166 IVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSA 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 241 TYLPVLDSLAGMLVVITLIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPMRMSGWLINDVQRFIASSFKIQDMMATDAKIP 320
Cdd:COG1132  246 LFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEIP 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 321 IHAE-KPAPSLQGHVEFKNVSFHFEDDpnTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVD 399
Cdd:COG1132  326 DPPGaVPLPPVRGEIEFENVSFSYPGD--RPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVD 403
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 400 ARKWHVRELRNHIATVMQDIFLFSDTIEGNIAFGAPDATMEDVRRMARIADADHFIETMPESYDTIVGERGVGLSGGQKQ 479
Cdd:COG1132  404 IRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQ 483
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 480 RISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHRISSVKEADEILILNHGEIIERGTHSSLLA 559
Cdd:COG1132  484 RIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLA 563
                        570
                 ....*....|....*.
gi 404223395 560 EKGYYFDIYNKQLGTE 575
Cdd:COG1132  564 RGGLYARLYRLQFGEE 579
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
3-572 5.07e-170

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


Pssm-ID: 441875 [Multi-domain]  Cd Length: 711  Bit Score: 499.75  E-value: 5.07e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395   3 SMKWIWQYVRKYRLLMIGVFILIFIASGISIIYPLLGGKVIDDVVYQNKTNLLIPLLLIMIISTIIRTICRYTYQIMCER 82
Cdd:COG2274  143 GLRWFLRLLRRYRRLLLQVLLASLLINLLALATPLFTQVVIDRVLPNQDLSTLWVLAIGLLLALLFEGLLRLLRSYLLLR 222
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  83 IGQNSLFRIREDLYKKLQSLDFDFFNNTRVGDIMARMtGDTDAIRHFVSWVSYNILENVFLFSFAIIIMAAIDWKLTLAL 162
Cdd:COG2274  223 LGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRF-RDVESIREFLTGSLLTALLDLLFVLIFLIVLFFYSPPLALVV 301
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 163 VIVTPLIAILTMKMSSKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSRTY 242
Cdd:COG2274  302 LLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLL 381
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 243 LPVLDSLAGMLVVITLIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPM-RMSGwLINDVQRFIASSFKIQDMMATDAKIPI 321
Cdd:COG2274  382 STLSGLLQQLATVALLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVaQLIG-LLQRFQDAKIALERLDDILDLPPEREE 460
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 322 HAEK-PAPSLQGHVEFKNVSFHFEDDpNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDA 400
Cdd:COG2274  461 GRSKlSLPRLKGDIELENVSFRYPGD-SPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDL 539
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 401 RKWHVRELRNHIATVMQDIFLFSDTIEGNIAFGAPDATMEDVRRMARIADADHFIETMPESYDTIVGERGVGLSGGQKQR 480
Cdd:COG2274  540 RQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQR 619
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 481 ISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHRISSVKEADEILILNHGEIIERGTHSSLLAE 560
Cdd:COG2274  620 LAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLAR 699
                        570
                 ....*....|..
gi 404223395 561 KGYYFDIYNKQL 572
Cdd:COG2274  700 KGLYAELVQQQL 711
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
7-574 2.40e-128

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


Pssm-ID: 131258 [Multi-domain]  Cd Length: 571  Bit Score: 387.92  E-value: 2.40e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395    7 IWQYVRKYRLLMIGVFILIFIASGISIIYPLLGGKVIDDVVYQNKTNLLIPLLLIMIISTIIRTICRYTYQIMCERIGQN 86
Cdd:TIGR02203   5 LWSYVRPYKAGLVLAGVAMILVAATESTLAALLKPLLDDGFGGRDRSVLWWVPLVVIGLAVLRGICSFVSTYLLSWVSNK 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395   87 SLFRIREDLYKKLQSLDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENVFLFSFAIIIMAAIDWKLTLALVIVT 166
Cdd:TIGR02203  85 VVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLTLIVVVML 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  167 PLIAILTMKMSSKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSRTYLPVL 246
Cdd:TIGR02203 165 PVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSAGSISSPIT 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  247 DSLAGMLVVITLIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPMRMSGWLINDVQRFIASSFKIQDMMATdakiPIHAE-- 324
Cdd:TIGR02203 245 QLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDS----PPEKDtg 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  325 -KPAPSLQGHVEFKNVSFHFEDDpNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKW 403
Cdd:TIGR02203 321 tRAIERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADY 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  404 HVRELRNHIATVMQDIFLFSDTIEGNIAFGAP-DATMEDVRRMARIADADHFIETMPESYDTIVGERGVGLSGGQKQRIS 482
Cdd:TIGR02203 400 TLASLRRQVALVSQDVVLFNDTIANNIAYGRTeQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLA 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  483 LARALLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHRISSVKEADEILILNHGEIIERGTHSSLLAEKG 562
Cdd:TIGR02203 480 IARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNG 559
                         570
                  ....*....|..
gi 404223395  563 YYFDIYNKQLGT 574
Cdd:TIGR02203 560 LYAQLHNMQFRE 571
MsbA_rel TIGR02204
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ...
4-564 2.76e-128

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: 387.90  E-value: 2.76e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395    4 MKWIWQYVRKYRLLMIGVFILIFIASGISIIYPLLGGKVIDDVVYQNKTNLLIPLLLIMIISTII---RTICRYtYQIMc 80
Cdd:TIGR02204   6 LAALWPFVRPYRGRVLAALVALLITAAATLSLPYAVRLMIDHGFSKDSSGLLNRYFAFLLVVALVlalGTAARF-YLVT- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395   81 eRIGQNSLFRIREDLYKKLQSLDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENVFLFSFAIIIMAAIDWKLTL 160
Cdd:TIGR02204  84 -WLGERVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTS 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  161 ALVIVTPLIAILTMKMSSKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEdfkkRNLDSADVSR 240
Cdd:TIGR02204 163 LVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVE----KAYEAARQRI 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  241 TYLPVLDSLAGML----VVITLIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPMRMSGWLINDVQRFIASSFKIQDMMAT- 315
Cdd:TIGR02204 239 RTRALLTAIVIVLvfgaIVGVLWVGAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGAAERLIELLQAe 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  316 -DAKIPIHAEKPAPSLQGHVEFKNVSFHFEDDPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEIL 394
Cdd:TIGR02204 319 pDIKAPAHPKTLPVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRIL 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  395 IDGVDARKWHVRELRNHIATVMQDIFLFSDTIEGNIAFGAPDATMEDVRRMARIADADHFIETMPESYDTIVGERGVGLS 474
Cdd:TIGR02204 399 LDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLS 478
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  475 GGQKQRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHRISSVKEADEILILNHGEIIERGTH 554
Cdd:TIGR02204 479 GGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTH 558
                         570
                  ....*....|
gi 404223395  555 SSLLAEKGYY 564
Cdd:TIGR02204 559 AELIAKGGLY 568
ABC_6TM_YknU_like cd18542
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ...
18-309 1.13e-125

Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349986 [Multi-domain]  Cd Length: 292  Bit Score: 370.99  E-value: 1.13e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  18 MIGVFILIFIASGISIIYPLLGGKVIDDVVYQNKTNLLIPLLLIMIISTIIRTICRYTYQIMCERIGQNSLFRIREDLYK 97
Cdd:cd18542    1 YLLAILALLLATALNLLIPLLIRRIIDSVIGGGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  98 KLQSLDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENVFLFSFAIIIMAAIDWKLTLALVIVTPLIAILTMKMS 177
Cdd:cd18542   81 HLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYVFF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 178 SKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSRTYLPVLDSLAGMLVVIT 257
Cdd:cd18542  161 KKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVLV 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 404223395 258 LIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPMRMSGWLINDVQRFIASSFKI 309
Cdd:cd18542  241 LWVGGYLVINGEITLGELVAFISYLWMLIWPVRQLGRLINDMSRASASAERI 292
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
82-571 4.00e-122

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


Pssm-ID: 444078 [Multi-domain]  Cd Length: 605  Bit Score: 373.00  E-value: 4.00e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  82 RIGQNSLFRIREDLYKKLQSLDFDFFNNTRVGDimarMTGD----TDAIRHFVSWVSYNILENVFLFSFAIIIMAAI-DW 156
Cdd:COG5265  104 RVTQRAVRRLALEVFRHLHALSLRFHLERQTGG----LSRDiergTKGIEFLLRFLLFNILPTLLEIALVAGILLVKyDW 179
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 157 KLTLALVIVTPLIAILTMKMSskaqpvfyEIRESFSRlnSMVEENISGNRV----------VKAFAREDFEMKKFHEHNE 226
Cdd:COG5265  180 WFALITLVTVVLYIAFTVVVT--------EWRTKFRR--EMNEADSEANTRavdsllnyetVKYFGNEAREARRYDEALA 249
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 227 DFKKrnldsADV-SRTYLPVLDS-----LAGMLVVItLIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPMRMSGWlindVQ 300
Cdd:COG5265  250 RYER-----AAVkSQTSLALLNFgqaliIALGLTAM-MLMAAQGVVAGTMTVGDFVLVNAYLIQLYIPLNFLGF----VY 319
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 301 RFIASSF-KIQDM---MATDAKIpihAEKP-APSL---QGHVEFKNVSFHFedDPNTDVLKNISLKASPGQTIAILGETG 372
Cdd:COG5265  320 REIRQALaDMERMfdlLDQPPEV---ADAPdAPPLvvgGGEVRFENVSFGY--DPERPILKGVSFEVPAGKTVAIVGPSG 394
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 373 AGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIATVMQDIFLFSDTIEGNIAFGAPDATMEDVRRMARIADAD 452
Cdd:COG5265  395 AGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIH 474
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 453 HFIETMPESYDTIVGERGVGLSGGQKQRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHRIS 532
Cdd:COG5265  475 DFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLS 554
                        490       500       510
                 ....*....|....*....|....*....|....*....
gi 404223395 533 SVKEADEILILNHGEIIERGTHSSLLAEKGYYFDIYNKQ 571
Cdd:COG5265  555 TIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQ 593
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
12-564 1.47e-117

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 364.43  E-value: 1.47e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395   12 RKYRLLMIGvFILIFIASGISIIYPLLGGKVIDDVV----YQNKTNLLIPLLLIMIISTIIRTICRYTYQIMCERIGQns 87
Cdd:TIGR00958 158 RDWPWLISA-FVFLTLSSLGEMFIPFYTGRVIDTLGgdkgPPALASAIFFMCLLSIASSVSAGLRGGSFNYTMARINL-- 234
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395   88 lfRIREDLYKKLQSLDFDFFNNTRVGDIMARMTGDTDAIRhfvSWVSYNIleNVFLFSF-----AIIIMAAIDWKLTLAL 162
Cdd:TIGR00958 235 --RIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMS---RSLSLNV--NVLLRNLvmllgLLGFMLWLSPRLTMVT 307
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  163 VIVTPLIAILTMKMSSKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSRTY 242
Cdd:TIGR00958 308 LINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRKALAYAGY 387
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  243 LpVLDSLAGMLV-VITLIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPMRMSGWLINDVQRFIASSFKIQDMMATDAKIPI 321
Cdd:TIGR00958 388 L-WTTSVLGMLIqVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLDRKPNIPL 466
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  322 HAEKPAPSLQGHVEFKNVSFHFEDDPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDAR 401
Cdd:TIGR00958 467 TGTLAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLV 546
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  402 KWHVRELRNHIATVMQDIFLFSDTIEGNIAFGAPDATMEDVRRMARIADADHFIETMPESYDTIVGERGVGLSGGQKQRI 481
Cdd:TIGR00958 547 QYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRI 626
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  482 SLARALLKNPSILILDDTTSAVDMETEVKIQgELKKiTENTTTFIIAHRISSVKEADEILILNHGEIIERGTHSSLLAEK 561
Cdd:TIGR00958 627 AIARALVRKPRVLILDEATSALDAECEQLLQ-ESRS-RASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQ 704

                  ...
gi 404223395  562 GYY 564
Cdd:TIGR00958 705 GCY 707
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
334-568 1.04e-112

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: 335.35  E-value: 1.04e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFEDDPNTdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIA 413
Cdd:cd03251    1 VEFKNVTFRYPGDGPP-VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 414 TVMQDIFLFSDTIEGNIAFGAPDATMEDVRRMARIADADHFIETMPESYDTIVGERGVGLSGGQKQRISLARALLKNPSI 493
Cdd:cd03251   80 LVSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 404223395 494 LILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHRISSVKEADEILILNHGEIIERGTHSSLLAEKGYYFDIY 568
Cdd:cd03251  160 LILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKLH 234
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
21-571 5.27e-112

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


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 345.93  E-value: 5.27e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  21 VFILIFIASgISIIYPLLGGKVIDDVVYQNKTNLLIPLLLIMIIST-IIRTICRYTYQIMcerigqnsLF--------RI 91
Cdd:PRK10789   1 VALLIIIAM-LQLIPPKVVGIIVDGVTEQHMTTGQILMWIGTMVLIaVVVYLLRYVWRVL--------LFgasyqlavEL 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  92 REDLYKKLQSLDFDFFNNTRVGDIMARMTGDTDAIRhFVSWVSYNILENVFLFSFAIIIMAA--IDWKLTLALVIVTPLI 169
Cdd:PRK10789  72 REDFYRQLSRQHPEFYLRHRTGDLMARATNDVDRVV-FAAGEGVLTLVDSLVMGCAVLIVMStqISWQLTLLALLPMPVM 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 170 AILTMKMSSKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSRTYLPVLDSL 249
Cdd:PRK10789 151 AIMIKRYGDQLHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARIDARFDPTIYIA 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 250 AGMLVVITLIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPMRMSGWLINDVQRFIASSFKIQDMMAtDAKIPIHAEKPAPS 329
Cdd:PRK10789 231 IGMANLLAIGGGSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRIRAMLA-EAPVVKDGSEPVPE 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 330 LQGHVEFKNVSFHFeddPNTD--VLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRE 407
Cdd:PRK10789 310 GRGELDVNIRQFTY---PQTDhpALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDS 386
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 408 LRNHIATVMQDIFLFSDTIEGNIAFGAPDATMEDVRRMARIADADHFIETMPESYDTIVGERGVGLSGGQKQRISLARAL 487
Cdd:PRK10789 387 WRSRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARAL 466
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 488 LKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHRISSVKEADEILILNHGEIIERGTHSSLLAEKGYYFDI 567
Cdd:PRK10789 467 LLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDM 546

                 ....
gi 404223395 568 YNKQ 571
Cdd:PRK10789 547 YRYQ 550
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
153-564 1.04e-111

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 345.41  E-value: 1.04e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 153 AIDWKLTL---ALVIVTPLIAILTMKMSSKAQPvfyEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHnedfk 229
Cdd:PRK13657 153 FMNWRLSLvlvVLGIVYTLITTLVMRKTKDGQA---AVEEHYHDLFAHVSDAIGNVSVVQSYNRIEAETQALRDI----- 224
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 230 KRNLDSADvsrtyLPVLD--SLAGML--------VVITLIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPM-RMSGWlIND 298
Cdd:PRK13657 225 ADNLLAAQ-----MPVLSwwALASVLnraastitMLAILVLGAALVQKGQLRVGEVVAFVGFATLLIGRLdQVVAF-INQ 298
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 299 VqrfIASSFKIQDMMATDAKIPIHAEKP-APSLQ---GHVEFKNVSFHFedDPNTDVLKNISLKASPGQTIAILGETGAG 374
Cdd:PRK13657 299 V---FMAAPKLEEFFEVEDAVPDVRDPPgAIDLGrvkGAVEFDDVSFSY--DNSRQGVEDVSFEAKPGQTVAIVGPTGAG 373
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 375 KSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIATVMQDIFLFSDTIEGNIAFGAPDATMEDVRRMARIADADHF 454
Cdd:PRK13657 374 KSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDF 453
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 455 IETMPESYDTIVGERGVGLSGGQKQRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHRISSV 534
Cdd:PRK13657 454 IERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTV 533
                        410       420       430
                 ....*....|....*....|....*....|
gi 404223395 535 KEADEILILNHGEIIERGTHSSLLAEKGYY 564
Cdd:PRK13657 534 RNADRILVFDNGRVVESGSFDELVARGGRF 563
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
5-562 7.84e-111

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


Pssm-ID: 444012 [Multi-domain]  Cd Length: 563  Bit Score: 342.51  E-value: 7.84e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395   5 KWIWQYVRKYRLLMIGVFILIFIASGISIIYPLLGGKVIDDVVYQNKT-NLLIPLLLIMIISTIIRTICRYTYQIMCERI 83
Cdd:COG4988    6 KRLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLIIGGAPlSALLPLLGLLLAVLLLRALLAWLRERAAFRA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  84 GQNSLFRIREDLYKKLQSLDFDFFNNTRVGDIMARMTGDTDAIRHFVS-WVSYNILenVFLFSFAI-IIMAAIDWKLTLA 161
Cdd:COG4988   86 AARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFArYLPQLFL--AALVPLLIlVAVFPLDWLSGLI 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 162 LVIVTPLI---AILTMKMSSKAQpvfYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRN------ 232
Cdd:COG4988  164 LLVTAPLIplfMILVGKGAAKAS---RRQWRALARLSGHFLDRLRGLTTLKLFGRAKAEAERIAEASEDFRKRTmkvlrv 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 233 --LDSAdvsrtylpVLDSLAGMLVVITLIFGGYLVIKGQMTLGdlVAFngFLWMLNG----PMR---------MSGwlin 297
Cdd:COG4988  241 afLSSA--------VLEFFASLSIALVAVYIGFRLLGGSLTLF--AAL--FVLLLAPefflPLRdlgsfyharANG---- 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 298 dvqrfIASSFKIQDMMATDAKIPIHAEKPAPSLQG-HVEFKNVSFHFEDDPNtdVLKNISLKASPGQTIAILGETGAGKS 376
Cdd:COG4988  305 -----IAAAEKIFALLDAPEPAAPAGTAPLPAAGPpSIELEDVSFSYPGGRP--ALDGLSLTIPPGERVALVGPSGAGKS 377
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 377 TLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIATVMQDIFLFSDTIEGNIAFGAPDATMEDVRRMARIADADHFIE 456
Cdd:COG4988  378 TLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVA 457
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 457 TMPESYDTIVGERGVGLSGGQKQRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHRISSVKE 536
Cdd:COG4988  458 ALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQ 537
                        570       580
                 ....*....|....*....|....*.
gi 404223395 537 ADEILILNHGEIIERGTHSSLLAEKG 562
Cdd:COG4988  538 ADRILVLDDGRIVEQGTHEELLAKNG 563
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
67-569 4.02e-110

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


Pssm-ID: 444011 [Multi-domain]  Cd Length: 569  Bit Score: 340.98  E-value: 4.02e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  67 IIRTICRYtyqimCER-IGQNSLFRI----REDLYKKLQSLDFDFFNNTRVGDIMARMTGDTDAIRHF---------VSW 132
Cdd:COG4987   66 IGRTVFRY-----LERlVSHDATLRLladlRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLylrvllpllVAL 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 133 VSYnilenvflfSFAIIIMAAIDWK----LTLALVIVTPLIAILTMKMSSKAQpvfYEIRESFSRLNSMVEENISGNRVV 208
Cdd:COG4987  141 LVI---------LAAVAFLAFFSPAlalvLALGLLLAGLLLPLLAARLGRRAG---RRLAAARAALRARLTDLLQGAAEL 208
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 209 KAFAREDFEMKKFHEHNEDFKK--RNLDSADVSRTYLPVLdsLAGMLVVITLIFGGYLVIKGQM--------TLGDLVAF 278
Cdd:COG4987  209 AAYGALDRALARLDAAEARLAAaqRRLARLSALAQALLQL--AAGLAVVAVLWLAAPLVAAGALsgpllallVLAALALF 286
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 279 NGFlwmlnGPMRMSGWLINDVqrfIASSFKIQDMMATDAKIPIHAEKPAPSLQGHVEFKNVSFHFEDDPnTDVLKNISLK 358
Cdd:COG4987  287 EAL-----APLPAAAQHLGRV---RAAARRLNELLDAPPAVTEPAEPAPAPGGPSLELEDVSFRYPGAG-RPVLDGLSLT 357
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 359 ASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIATVMQDIFLFSDTIEGNIAFGAPDAT 438
Cdd:COG4987  358 LPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDAT 437
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 439 MEDVRRMARIADADHFIETMPESYDTIVGERGVGLSGGQKQRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKI 518
Cdd:COG4987  438 DEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEA 517
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|.
gi 404223395 519 TENTTTFIIAHRISSVKEADEILILNHGEIIERGTHSSLLAEKGYYFDIYN 569
Cdd:COG4987  518 LAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRYRQLYQ 568
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
334-571 1.39e-105

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: 317.56  E-value: 1.39e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFEDDPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIA 413
Cdd:cd03249    1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 414 TVMQDIFLFSDTIEGNIAFGAPDATMEDVRRMARIADADHFIETMPESYDTIVGERGVGLSGGQKQRISLARALLKNPSI 493
Cdd:cd03249   81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 404223395 494 LILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHRISSVKEADEILILNHGEIIERGTHSSLLAEKGYYFDIYNKQ 571
Cdd:cd03249  161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
5-573 2.65e-104

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 326.21  E-value: 2.65e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395   5 KWIWQYVRKYRL-LMIGVFILIFIASG----ISIIYPLLggkviDDVVYQNKTNLLIPLLLIMIISTIIRTICRY--TYQ 77
Cdd:PRK11176  14 RRLWPTIAPFKAgLIVAGVALILNAASdtfmLSLLKPLL-----DDGFGKADRSVLKWMPLVVIGLMILRGITSFisSYC 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  78 ImcERIGQNSLFRIREDLYKKLQSLDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVSYNIL-ENVFLFSFaIIIMAAIDW 156
Cdd:PRK11176  89 I--SWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVrEGASIIGL-FIMMFYYSW 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 157 KLTLALVIVTPLIAILTMKMSSKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSA 236
Cdd:PRK11176 166 QLSLILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRQQGMKMV 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 237 DVSRTYLPVLDSLAGMLVVITLIFGGYLVIKGQMTLGDL-VAFNGFLWMlngpMRMSGWLIN---DVQRFIASS---FKI 309
Cdd:PRK11176 246 SASSISDPIIQLIASLALAFVLYAASFPSVMDTLTAGTItVVFSSMIAL----MRPLKSLTNvnaQFQRGMAACqtlFAI 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 310 QDMmATDAKIPIHAEKPApslQGHVEFKNVSFHFEDDpNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPT 389
Cdd:PRK11176 322 LDL-EQEKDEGKRVIERA---KGDIEFRNVTFTYPGK-EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDID 396
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 390 SGEILIDGVDARKWHVRELRNHIATVMQDIFLFSDTIEGNIAFGAPDA-TMEDVRRMARIADADHFIETMPESYDTIVGE 468
Cdd:PRK11176 397 EGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAYAMDFINKMDNGLDTVIGE 476
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 469 RGVGLSGGQKQRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHRISSVKEADEILILNHGEI 548
Cdd:PRK11176 477 NGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEI 556
                        570       580
                 ....*....|....*....|....*
gi 404223395 549 IERGTHSSLLAEKGYYFDIYNKQLG 573
Cdd:PRK11176 557 VERGTHAELLAQNGVYAQLHKMQFG 581
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
334-571 9.51e-103

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: 309.93  E-value: 9.51e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFedDPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIA 413
Cdd:cd03253    1 IEFENVTFAY--DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 414 TVMQDIFLFSDTIEGNIAFGAPDATMEDVRRMARIADADHFIETMPESYDTIVGERGVGLSGGQKQRISLARALLKNPSI 493
Cdd:cd03253   79 VVPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPI 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 404223395 494 LILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHRISSVKEADEILILNHGEIIERGTHSSLLAEKGYYFDIYNKQ 571
Cdd:cd03253  159 LLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
332-562 5.65e-102

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: 307.61  E-value: 5.65e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 332 GHVEFKNVSFHFedDPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNH 411
Cdd:cd03254    1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 412 IATVMQDIFLFSDTIEGNIAFGAPDATMEDVRRMARIADADHFIETMPESYDTIVGERGVGLSGGQKQRISLARALLKNP 491
Cdd:cd03254   79 IGVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDP 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 404223395 492 SILILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHRISSVKEADEILILNHGEIIERGTHSSLLAEKG 562
Cdd:cd03254  159 KILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
type_I_sec_HlyB TIGR01846
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ...
6-573 2.07e-98

type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 273831 [Multi-domain]  Cd Length: 694  Bit Score: 313.99  E-value: 2.07e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395    6 WIWQYVRKYRLLMIGVFILIFIASGISIIYPLLGGKVIDDVVYQNKTNLLIPLLLIMIISTI-------IRTicrYTYQI 78
Cdd:TIGR01846 129 WFIPAIIRYRKQFREVLLISLALQLFALVTPLLFQVVIDKVLVHRGLSTLSVLALAMLAVAIfepalggLRT---YLFAH 205
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395   79 MCERIGqnslFRIREDLYKKLQSLDFDFFNNTRVGDIMARMTgDTDAIRHFVSWVSYNILENVFlfsFAIIIMAAIDW-- 156
Cdd:TIGR01846 206 LTSRID----VELGARLYRHLLGLPLGYFESRRVGDTVARVR-ELEQIRNFLTGSALTVVLDLL---FVVVFLAVMFFys 277
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  157 -KLTLALVIVTPLIAILTMKMSSKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDS 235
Cdd:TIGR01846 278 pTLTGVVIGSLVCYALLSVFVGPILRKRVEDKFERSAAATSFLVESVTGIETIKATATEPQFQNRWDRQLAAYVAASFRV 357
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  236 ADVSRTYLPVLDSLAGMLVVITLIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPMRMSGWLINDVQRFIASSFKIQDMMAT 315
Cdd:TIGR01846 358 TNLGNIAGQAIELIQKLTFAILLWFGAHLVIGGALSPGQLVAFNMLAGRVTQPVLRLAQLWQDFQQTGIALERLGDILNS 437
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  316 DAKiPIHAEKPA-PSLQGHVEFKNVSFHFEDDpNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEIL 394
Cdd:TIGR01846 438 PTE-PRSAGLAAlPELRGAITFENIRFRYAPD-SPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVL 515
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  395 IDGVDARKWHVRELRNHIATVMQDIFLFSDTIEGNIAFGAPDATMEDVRRMARIADADHFIETMPESYDTIVGERGVGLS 474
Cdd:TIGR01846 516 VDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCNPGAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLS 595
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  475 GGQKQRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHRISSVKEADEILILNHGEIIERGTH 554
Cdd:TIGR01846 596 GGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRH 675
                         570
                  ....*....|....*....
gi 404223395  555 SSLLAEKGYYFDIYNKQLG 573
Cdd:TIGR01846 676 EELLALQGLYARLWQQQSG 694
chvA TIGR01192
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ...
153-565 4.86e-90

glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 130260 [Multi-domain]  Cd Length: 585  Bit Score: 289.10  E-value: 4.86e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  153 AIDWKLTLALV---IVTPLIAILTMKMSSKAQPVfyeIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEdfk 229
Cdd:TIGR01192 153 AMDWRLSIVLMvlgILYILIAKLVMQRTKNGQAA---VEHHYHNVFKHVSDSISNVSVVHSYNRIEAETSALKQFTN--- 226
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  230 krNLDSADVsrtylPVLD--SLAGML--------VVITLIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPM-RMSGWlind 298
Cdd:TIGR01192 227 --NLLSAQY-----PVLDwwALASGLnrmastisMMCILVIGTVLVIKGELSVGEVIAFIGFANLLIGRLdQMSGF---- 295
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  299 VQRFIASSFKIQDMMATDAKIpIHAEKPA-----PSLQGHVEFKNVSFHFeddPNTDV-LKNISLKASPGQTIAILGETG 372
Cdd:TIGR01192 296 ITQIFEARAKLEDFFDLEDSV-FQREEPAdapelPNVKGAVEFRHITFEF---ANSSQgVFDVSFEAKAGQTVAIVGPTG 371
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  373 AGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIATVMQDIFLFSDTIEGNIAFGAPDATMEDVRRMARIADAD 452
Cdd:TIGR01192 372 AGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESLRKSIATVFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAH 451
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  453 HFIETMPESYDTIVGERGVGLSGGQKQRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHRIS 532
Cdd:TIGR01192 452 DFILKRSNGYDTLVGERGNRLSGGERQRLAIARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLS 531
                         410       420       430
                  ....*....|....*....|....*....|...
gi 404223395  533 SVKEADEILILNHGEIIERGTHSSLLAEKGYYF 565
Cdd:TIGR01192 532 TVRNADLVLFLDQGRLIEKGSFQELIQKDGRFY 564
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
334-571 5.80e-85

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: 264.35  E-value: 5.80e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFEDDpNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIA 413
Cdd:cd03252    1 ITFEHVRFRYKPD-GPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 414 TVMQDIFLFSDTIEGNIAFGAPDATMEDVRRMARIADADHFIETMPESYDTIVGERGVGLSGGQKQRISLARALLKNPSI 493
Cdd:cd03252   80 VVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRI 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 404223395 494 LILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHRISSVKEADEILILNHGEIIERGTHSSLLAEKGYYFDIYNKQ 571
Cdd:cd03252  160 LIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
NHLM_micro_ABC1 TIGR03796
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ...
106-564 1.17e-82

NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]


Pssm-ID: 274788 [Multi-domain]  Cd Length: 710  Bit Score: 272.97  E-value: 1.17e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  106 FFNNTRVGDIMARMTGDtDAIRHFVSWVSYNILENVFLFSFAIIIMAAIDWKLTLaLVIVTPLIAILTMKMSSKAQPVF- 184
Cdd:TIGR03796 244 FFAQRHAGDIASRVQLN-DQVAEFLSGQLATTALDAVMLVFYALLMLLYDPVLTL-IGIAFAAINVLALQLVSRRRVDAn 321
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  185 YEIRESFSRLNSMVEENISGNRVVKAFARED--------FEMKKFHEHNEdfkkrnLDSADVSRTYLP-VLDSLAGMLVv 255
Cdd:TIGR03796 322 RRLQQDAGKLTGVAISGLQSIETLKASGLESdffsrwagYQAKLLNAQQE------LGVLTQILGVLPtLLTSLNSALI- 394
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  256 itLIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPM-RMSGwLINDVQRFIASSFKIQDMM-------ATDAKIPIHAEKPA 327
Cdd:TIGR03796 395 --LVVGGLRVMEGQLTIGMLVAFQSLMSSFLEPVnNLVG-FGGTLQELEGDLNRLDDVLrnpvdplLEEPEGSAATSEPP 471
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  328 PSLQGHVEFKNVSFHFE--DDPntdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHV 405
Cdd:TIGR03796 472 RRLSGYVELRNITFGYSplEPP---LIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPR 548
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  406 RELRNHIATVMQDIFLFSDTIEGNIAFGAPDATMEDVRRMARIADADHFIETMPESYDTIVGERGVGLSGGQKQRISLAR 485
Cdd:TIGR03796 549 EVLANSVAMVDQDIFLFEGTVRDNLTLWDPTIPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIAR 628
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 404223395  486 ALLKNPSILILDDTTSAVDMETEVKIQGELKKitENTTTFIIAHRISSVKEADEILILNHGEIIERGTHSSLLAEKGYY 564
Cdd:TIGR03796 629 ALVRNPSILILDEATSALDPETEKIIDDNLRR--RGCTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELWAVGGAY 705
ABC_6TM_exporters cd07346
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ...
18-305 4.41e-82

Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349983 [Multi-domain]  Cd Length: 292  Bit Score: 258.63  E-value: 4.41e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  18 MIGVFILIFIASGISIIYPLLGGKVIDDVVYQNKTNLLIPLLLIMIISTIIRTICRYTYQIMCERIGQNSLFRIREDLYK 97
Cdd:cd07346    1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  98 KLQSLDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENVFLFSFAIIIMAAIDWKLTLALVIVTPLIAILTMKMS 177
Cdd:cd07346   81 HLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 178 SKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSRTYLPVLDSLAGMLVVIT 257
Cdd:cd07346  161 RRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALV 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 404223395 258 LIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPMRMSGWLINDVQRFIAS 305
Cdd:cd07346  241 LLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALAS 288
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
332-552 2.35e-78

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: 246.35  E-value: 2.35e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 332 GHVEFKNVSFHFEDDPNtDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNH 411
Cdd:cd03245    1 GRIEFRNVSFSYPNQEI-PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 412 IATVMQDIFLFSDTIEGNIAFGAPDATMEDVRRMARIADADHFIETMPESYDTIVGERGVGLSGGQKQRISLARALLKNP 491
Cdd:cd03245   80 IGYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDP 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 404223395 492 SILILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHRISSVKEADEILILNHGEIIERG 552
Cdd:cd03245  160 PILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
ABC_6TM_TmrB_like cd18541
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ...
17-305 2.86e-78

Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349985 [Multi-domain]  Cd Length: 293  Bit Score: 248.87  E-value: 2.86e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  17 LMIGVFILIfIASGISIIYPLLGGKVIDDVVYQNKTNLLIPLLLIM-IISTIIRTICRYTYQIMCERIGQNSLFRIREDL 95
Cdd:cd18541    1 YLLGILFLI-LVDLLQLLIPRIIGRAIDALTAGTLTASQLLRYALLiLLLALLIGIFRFLWRYLIFGASRRIEYDLRNDL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  96 YKKLQSLDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENVFLFSFAIIIMAAIDWKLTLALVIVTPLIAILTMK 175
Cdd:cd18541   80 FAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLVYR 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 176 MSSKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSRTYLPVLDSLAGMLVV 255
Cdd:cd18541  160 LGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLSFL 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 404223395 256 ITLIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPMRMSGWLINDVQRFIAS 305
Cdd:cd18541  240 IVLWYGGRLVIRGTITLGDLVAFNSYLGMLIWPMMALGWVINLIQRGAAS 289
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
334-547 1.09e-76

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: 240.36  E-value: 1.09e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFEDDPNTdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIA 413
Cdd:cd03228    1 IEFKNVSFSYPGRPKP-VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 414 TVMQDIFLFSDTIEGNIafgapdatmedvrrmariadadhfietmpesydtivgergvgLSGGQKQRISLARALLKNPSI 493
Cdd:cd03228   80 YVPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPI 117
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 404223395 494 LILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHRISSVKEADEILILNHGE 547
Cdd:cd03228  118 LILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
107-575 3.31e-75

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


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 250.41  E-value: 3.31e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 107 FNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENVFLFSFAIIIMAAIDWKLTLALVIVTPLIAILTMKMSSKAQPVFYE 186
Cdd:PRK10790 116 FDTQPVGQLISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWRMALVAIMIFPAVLVVMVIYQRYSTPIVRR 195
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 187 IRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSRTYLPVLDSLAGMLVV--ITLIFGgyL 264
Cdd:PRK10790 196 VRAYLADINDGFNEVINGMSVIQQFRQQARFGERMGEASRSHYMARMQTLRLDGFLLRPLLSLFSALILcgLLMLFG--F 273
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 265 VIKGQMTLGDLVAFNGFLWMLNGPmrmsgwLI------NDVQRFIASSFKIQDMMatDAKIPIHAEKPAPSLQGHVEFKN 338
Cdd:PRK10790 274 SASGTIEVGVLYAFISYLGRLNEP------LIelttqqSMLQQAVVAGERVFELM--DGPRQQYGNDDRPLQSGRIDIDN 345
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 339 VSFHFEDDpnTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIATVMQD 418
Cdd:PRK10790 346 VSFAYRDD--NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQD 423
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 419 IFLFSDTIEGNIAFGApDATMEDVRRMARIADADHFIETMPESYDTIVGERGVGLSGGQKQRISLARALLKNPSILILDD 498
Cdd:PRK10790 424 PVVLADTFLANVTLGR-DISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDE 502
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 404223395 499 TTSAVDMETEVKIQGELKKITENTTTFIIAHRISSVKEADEILILNHGEIIERGTHSSLLAEKGYYFDIYNKQLGTE 575
Cdd:PRK10790 503 ATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQLQLAGE 579
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
11-569 5.72e-75

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


Pssm-ID: 130261 [Multi-domain]  Cd Length: 708  Bit Score: 252.35  E-value: 5.72e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395   11 VRKYRLLMIGVFILIFIASGISIIYPLLGGKVIDDVVYQNKTNLLIPLLLIMIISTIIRTICRYTYQIMCERIGQNSLFR 90
Cdd:TIGR01193 151 ITRQKKLIVNIVIAAIIVTLISIAGSYYLQKIIDTYIPHKMMGTLGIISIGLIIAYIIQQILSYIQIFLLNVLGQRLSID 230
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395   91 IREDLYKKLQSLDFDFFNNTRVGDIMARMTgDTDAIRHFVSWVSYNILENVFLFSFAIIIMAAIDWKLTLALVIVTPLIA 170
Cdd:TIGR01193 231 IILSYIKHLFELPMSFFSTRRTGEIVSRFT-DASSIIDALASTILSLFLDMWILVIVGLFLVRQNMLLFLLSLLSIPVYA 309
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  171 ILTMKMSSKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNL--DSADVSRTYLPVLDS 248
Cdd:TIGR01193 310 VIIILFKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEAERYSKIDSEFGDYLNKSFkyQKADQGQQAIKAVTK 389
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  249 LagMLVVITLIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPMRMSGWLINDVQRFIASSFKIQDMMATDAK-IPIHAEKPA 327
Cdd:TIGR01193 390 L--ILNVVILWTGAYLVMRGKLTLGQLITFNALLSYFLTPLENIINLQPKLQAARVANNRLNEVYLVDSEfINKKKRTEL 467
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  328 PSLQGHVEFKNVSFHFedDPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRE 407
Cdd:TIGR01193 468 NNLNGDIVINDVSYSY--GYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHT 545
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  408 LRNHIATVMQDIFLFSDTIEGNIAFGA-PDATMEDVRRMARIADADHFIETMPESYDTIVGERGVGLSGGQKQRISLARA 486
Cdd:TIGR01193 546 LRQFINYLPQEPYIFSGSILENLLLGAkENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARA 625
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  487 LLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFiIAHRISSVKEADEILILNHGEIIERGTHSSLLAEKGYYFD 566
Cdd:TIGR01193 626 LLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDKTIIF-VAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYAS 704

                  ...
gi 404223395  567 IYN 569
Cdd:TIGR01193 705 LIH 707
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
149-543 8.52e-75

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


Pssm-ID: 274323 [Multi-domain]  Cd Length: 529  Bit Score: 247.59  E-value: 8.52e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  149 IIMAAI---DWKLTLALVIVTPLIAILTMKMSSKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHN 225
Cdd:TIGR02857 134 AILAAVfpqDWISGLILLLTAPLIPIFMILIGWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAAIRRSS 213
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  226 EDFKKRN--------LDSAdvsrtylpVLDSLAGMLVVITLIFGGYLVIKGQMTLgdlvaFNGFLWML-----NGPMRMS 292
Cdd:TIGR02857 214 EEYRERTmrvlriafLSSA--------VLELFATLSVALVAVYIGFRLLAGDLDL-----ATGLFVLLlapefYLPLRQL 280
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  293 GWLINDVQRFIASSFKIQDMMATDAkIPIHAEKPAPSLQGH-VEFKNVSFHFEDDPNtdVLKNISLKASPGQTIAILGET 371
Cdd:TIGR02857 281 GAQYHARADGVAAAEALFAVLDAAP-RPLAGKAPVTAAPASsLEFSGVSVAYPGRRP--ALRPVSFTVPPGERVALVGPS 357
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  372 GAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIATVMQDIFLFSDTIEGNIAFGAPDATMEDVRRMARIADA 451
Cdd:TIGR02857 358 GAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGL 437
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  452 DHFIETMPESYDTIVGERGVGLSGGQKQRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHRI 531
Cdd:TIGR02857 438 DEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRL 517
                         410
                  ....*....|..
gi 404223395  532 SSVKEADEILIL 543
Cdd:TIGR02857 518 ALAALADRIVVL 529
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
330-548 1.42e-72

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: 231.59  E-value: 1.42e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 330 LQGHVEFKNVSFHFEDDPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELR 409
Cdd:cd03248    8 LKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLH 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 410 NHIATVMQDIFLFSDTIEGNIAFGAPDATMEDVRRMARIADADHFIETMPESYDTIVGERGVGLSGGQKQRISLARALLK 489
Cdd:cd03248   88 SKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIR 167
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 404223395 490 NPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHRISSVKEADEILILNHGEI 548
Cdd:cd03248  168 NPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
ABC_6TM_exporter_like cd18563
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
18-309 1.02e-70

Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 350007 [Multi-domain]  Cd Length: 296  Bit Score: 229.32  E-value: 1.02e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  18 MIGVFILIFIASGISIIYPLLGGKVIDDVVYQNKTNLLIPLLLIMII----STIIRTICRYTYQIMCERIGQNSLFRIRE 93
Cdd:cd18563    1 LILGFLLMLLGTALGLVPPYLTKILIDDVLIQLGPGGNTSLLLLLVLglagAYVLSALLGILRGRLLARLGERITADLRR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  94 DLYKKLQSLDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENVFLFSFAIIIMAAIDWKLTLALVIVTPLIAILT 173
Cdd:cd18563   81 DLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVVWGS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 174 MKMSSKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSRTYLPVLDSLAGML 253
Cdd:cd18563  161 YFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFPLLTFLTSLG 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 404223395 254 VVITLIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPMRMSGWLINDVQRFIASSFKI 309
Cdd:cd18563  241 TLIVWYFGGRQVLSGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRALTSAERI 296
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
141-548 3.08e-65

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


Pssm-ID: 443660 [Multi-domain]  Cd Length: 563  Bit Score: 222.70  E-value: 3.08e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 141 VFLFSFAIIIMAAIdwkLTLALVIVTPLIAILTMKMSSKAQpvfyeirESFSRLNSMVEENISGNRVVKAFAREDFEMKK 220
Cdd:COG4618  150 LFLFHPLLGLLALV---GALVLVALALLNERLTRKPLKEAN-------EAAIRANAFAEAALRNAEVIEAMGMLPALRRR 219
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 221 FHEHNEDFKKRNLDSADVSRTYLPVLDSLAGMLVVITLIFGGYLVIKGQMTLGDLVAFNgflwMLNG----P--MRMSGW 294
Cdd:COG4618  220 WQRANARALALQARASDRAGGFSALSKFLRLLLQSAVLGLGAYLVIQGEITPGAMIAAS----ILMGralaPieQAIGGW 295
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 295 liNDVQRFIASSFKIQDMMATDAKIPIHAEKPAPslQGHVEFKNVSFHFeddPNTD--VLKNISLKASPGQTIAILGETG 372
Cdd:COG4618  296 --KQFVSARQAYRRLNELLAAVPAEPERMPLPRP--KGRLSVENLTVVP---PGSKrpILRGVSFSLEPGEVLGVIGPSG 368
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 373 AGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIATVMQDIFLFSDTIEGNIA-FGAPDAtmEDVRRMARIADA 451
Cdd:COG4618  369 SGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIArFGDADP--EKVVAAAKLAGV 446
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 452 DHFIETMPESYDTIVGERGVGLSGGQKQRISLARALLKNPSILILDDTTSAVDMETEVK----IQgELKKitENTTTFII 527
Cdd:COG4618  447 HEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAAlaaaIR-ALKA--RGATVVVI 523
                        410       420
                 ....*....|....*....|.
gi 404223395 528 AHRISSVKEADEILILNHGEI 548
Cdd:COG4618  524 THRPSLLAAVDKLLVLRDGRV 544
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
332-553 1.90e-63

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: 1.90e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 332 GHVEFKNVSFHFEDDPNTdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNH 411
Cdd:cd03244    1 GDIEFKNVSLRYRPNLPP-VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 412 IATVMQDIFLFSDTIEGNIA-FG-APDATMEDVRRMARIADadhFIETMPESYDTIVGERGVGLSGGQKQRISLARALLK 489
Cdd:cd03244   80 ISIIPQDPVLFSGTIRSNLDpFGeYSDEELWQALERVGLKE---FVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLR 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 404223395 490 NPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHRISSVKEADEILILNHGEIIERGT 553
Cdd:cd03244  157 KSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
303-571 4.94e-63

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 217.39  E-value: 4.94e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 303 IASSFKIQDMMATDAKIPIHAEKPAPSLQGHVEFKNVSFHFEDDPNTdVLKNISLKASPGQTIAILGETGAGKSTLVNLI 382
Cdd:PRK11160 308 IASARRINEITEQKPEVTFPTTSTAAADQVSLTLNNVSFTYPDQPQP-VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLL 386
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 383 CRFYDPTSGEILIDGVDARKWHVRELRNHIATVMQDIFLFSDTIEGNIAFGAPDATMEDVRRMARIADADHFIETmPESY 462
Cdd:PRK11160 387 TRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGLEKLLED-DKGL 465
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 463 DTIVGERGVGLSGGQKQRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHRISSVKEADEILI 542
Cdd:PRK11160 466 NAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICV 545
                        250       260
                 ....*....|....*....|....*....
gi 404223395 543 LNHGEIIERGTHSSLLAEKGYYFDIYNKQ 571
Cdd:PRK11160 546 MDNGQIIEQGTHQELLAQQGRYYQLKQRL 574
ABC_6TM_YknV_like cd18545
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ...
18-309 1.05e-62

Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349989 [Multi-domain]  Cd Length: 293  Bit Score: 208.09  E-value: 1.05e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  18 MIGVFILIFIASGISIIYPLLGGKVIDDVVYQNKTNLLIPLLLIMIISTIIRTICRYTYQIMCERIGQNSLFRIREDLYK 97
Cdd:cd18545    2 LLLALLLMLLSTAASLAGPYLIKIAIDEYIPNGDLSGLLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  98 KLQSLDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENVFLFSFAIIIMAAIDWKLTLALVIVTPLIAILTMKMS 177
Cdd:cd18545   82 HLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVVFLLR 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 178 SKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSRTYLPVLDSLAGMLVVIT 257
Cdd:cd18545  162 RRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLNALFWPLVELISALGTALV 241
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 404223395 258 LIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPMRMSGWLINDVQRFIASSFKI 309
Cdd:cd18545  242 YWYGGKLVLGGAITVGVLVAFIGYVGRFWQPIRNLSNFYNQLQSAMASAERI 293
ABC_6TM_Tm288_like cd18547
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ...
18-306 8.28e-62

Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349991 [Multi-domain]  Cd Length: 298  Bit Score: 206.10  E-value: 8.28e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  18 MIGVFILIFIASGISIIYPLLGGKVIDDVVYQNKTNLLIPLLLIMIISTI------IRTICRYTYQIMCERIGQNSLFRI 91
Cdd:cd18547    1 LILVIILAIISTLLSVLGPYLLGKAIDLIIEGLGGGGGVDFSGLLRILLLllglylLSALFSYLQNRLMARVSQRTVYDL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  92 REDLYKKLQSLDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENVFLFSFAIIIMAAIDWKLTLALVIVTPLIAI 171
Cdd:cd18547   81 RKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 172 LTMKMSSKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSRTYLPVLDSLAG 251
Cdd:cd18547  161 VTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFKAQFYSGLLMPIMNFINN 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 404223395 252 MLVVITLIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPMRMSGWLINDVQRFIASS 306
Cdd:cd18547  241 LGYVLVAVVGGLLVINGALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAGA 295
ABC_6TM_exporter_like cd18778
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
18-306 1.17e-61

Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 350051 [Multi-domain]  Cd Length: 293  Bit Score: 205.46  E-value: 1.17e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  18 MIGVFILIFIASGISIIYPLLGGKVIDDV-VYQNKTNLLIPLLLIMIISTIIRTICRYTYQIMCERIGQNSLFRIREDLY 96
Cdd:cd18778    1 LILTLLCALLSTLLGLVPPWLIRELVDLVtIGSKSLGLLLGLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADLRSDLY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  97 KKLQSLDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENVFLFSFAIIIMAAIDWKLTLALVIVTPLIAILTMKM 176
Cdd:cd18778   81 DKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLALGAWLY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 177 SSKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSRTYLPVLDSLAGMLVVI 256
Cdd:cd18778  161 SKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWAIFHPLMEFLTSLGTVL 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 404223395 257 TLIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPM-RMSGwLINDVQRFIASS 306
Cdd:cd18778  241 VLGFGGRLVLAGELTIGDLVAFLLYLGLFYEPItSLHG-LNEMLQRALAGA 290
ABC_6TM_TmrA_like cd18544
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ...
18-309 3.83e-61

Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349988 [Multi-domain]  Cd Length: 294  Bit Score: 204.16  E-value: 3.83e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  18 MIGVFILIFIASGISIIYPLLGGKVIDDVVYQNKTNLLIPLLLIMI--ISTIIRTICRYTYQIMCERIGQNSLFRIREDL 95
Cdd:cd18544    1 FILALLLLLLATALELLGPLLIKRAIDDYIVPGQGDLQGLLLLALLylGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  96 YKKLQSLDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENVFLFSFAIIIMAAIDWKLTLALVIVTPLIAILTMK 175
Cdd:cd18544   81 FSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATYL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 176 MSSKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSRTYLPVLDSLAGMLVV 255
Cdd:cd18544  161 FRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELLSSLALA 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 404223395 256 ITLIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPMRMSGWLINDVQRFIASSFKI 309
Cdd:cd18544  241 LVLWYGGGQVLSGAVTLGVLYAFIQYIQRFFRPIRDLAEKFNILQSAMASAERI 294
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
67-530 3.34e-58

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


Pssm-ID: 274331 [Multi-domain]  Cd Length: 530  Bit Score: 203.36  E-value: 3.34e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395   67 IIRTICRYtyqimCER-IGQNSLFRI----REDLYKKLQSLDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENV 141
Cdd:TIGR02868  64 IGRAVFRY-----LERlVGHDAALRSlgalRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGVAL 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  142 FLFSFAIIIMAAIDWKLTLALVI-------VTPLIAILTMKMSSKAqpvfyeIRESFSRLNSMVEENISGNRVVKAFARE 214
Cdd:TIGR02868 139 VVGAAAVAAIAVLSVPAALILAAglllagfVAPLVSLRAARAAEQA------LARLRGELAAQLTDALDGAAELVASGAL 212
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  215 DFEMKKFHEHNEDFKK--RNLDSADVSRTYLPVLdsLAGMLVVITLIFGGYLVIKGQMT--------LGDLVAFNGFlwm 284
Cdd:TIGR02868 213 PAALAQVEEADRELTRaeRRAAAATALGAALTLL--AAGLAVLGALWAGGPAVADGRLApvtlavlvLLPLAAFEAF--- 287
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  285 lnGPMRMSgwlINDVQRFIASSFKIQDmmATDAKIPI-----HAEKPAPSLQGHVEFKNVSFHFEDDPntDVLKNISLKA 359
Cdd:TIGR02868 288 --AALPAA---AQQLTRVRAAAERIVE--VLDAAGPVaegsaPAAGAVGLGKPTLELRDLSAGYPGAP--PVLDGVSLDL 358
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  360 SPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIATVMQDIFLFSDTIEGNIAFGAPDATM 439
Cdd:TIGR02868 359 PPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATD 438
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  440 EDVRRMARIADADHFIETMPESYDTIVGERGVGLSGGQKQRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKIT 519
Cdd:TIGR02868 439 EELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAAL 518
                         490
                  ....*....|.
gi 404223395  520 ENTTTFIIAHR 530
Cdd:TIGR02868 519 SGRTVVLITHH 529
ABC_6TM_MsbA_like cd18552
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ...
18-305 1.37e-56

Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349996 [Multi-domain]  Cd Length: 292  Bit Score: 191.87  E-value: 1.37e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  18 MIGVFILIFIASGISIIYPLLGGKVIDDVVYQNKTNLLIPLLLIMIISTIIRTICRYTYQIMCERIGQNSLFRIREDLYK 97
Cdd:cd18552    1 LALAILGMILVAATTAALAWLLKPLLDDIFVEKDLEALLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRNDLFD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  98 KLQSLDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENVFLFSFAIIIMAAIDWKLTLALVIVTPLIAILTMKMS 177
Cdd:cd18552   81 KLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPIRRIG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 178 SKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSRTYLPVLDSLAGMLVVIT 257
Cdd:cd18552  161 KRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELLGAIAIALV 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 404223395 258 LIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPMRMSGWLINDVQRFIAS 305
Cdd:cd18552  241 LWYGGYQVISGELTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAA 288
ABC_6TM_Rv0194_D1_like cd18543
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ...
18-306 2.45e-56

Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349987 [Multi-domain]  Cd Length: 291  Bit Score: 191.16  E-value: 2.45e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  18 MIGVFILIFIASGISIIYPLLGGKVIDDVVYQNKTNLLIPLLLIMIISTIIRTICRYTYQIMCERIGQNSLFRIREDLYK 97
Cdd:cd18543    1 LILALLAALLATLAGLAIPLLTRRAIDGPIAHGDRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  98 KLQSLDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVSYnILENVFLFSFAIIIMAAIDWKLTLALVIVTPLIAILTMKMS 177
Cdd:cd18543   81 HLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLAFGPF-LLGNLLTLVVGLVVMLVLSPPLALVALASLPPLVLVARRFR 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 178 SKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSRTYLPVLDSLAGMLVVIT 257
Cdd:cd18543  160 RRYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWPLLEALPELGLAAV 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 404223395 258 LIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPMRMSGWLINDVQRFIASS 306
Cdd:cd18543  240 LALGGWLVANGSLTLGTLVAFSAYLTMLVWPVRMLGWLLAMAQRARAAA 288
ABC_6TM_YwjA_like cd18549
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ...
15-302 2.22e-55

Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar proteins; This group represents the six-transmembrane helical domain of an uncharacterized ABC transporter YwjA from Bacillus subtilis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349993 [Multi-domain]  Cd Length: 295  Bit Score: 188.81  E-value: 2.22e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  15 RLLMIGVFILIFIASGISIIYPLLGGKVIDDVVYQNKTNLLIPLLLIMIISTIIRTICRYTYQIMCERIGQNSLFRIRED 94
Cdd:cd18549    1 KKLFFLDLFCAVLIAALDLVFPLIVRYIIDDLLPSKNLRLILIIGAILLALYILRTLLNYFVTYWGHVMGARIETDMRRD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  95 LYKKLQSLDFDFFNNTRVGDIMARMTGDTDAIrhfvSWVSYNILENVFLFSF----AIIIMAAIDWKLTLALVIVTPLIA 170
Cdd:cd18549   81 LFEHLQKLSFSFFDNNKTGQLMSRITNDLFDI----SELAHHGPEDLFISIItiigSFIILLTINVPLTLIVFALLPLMI 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 171 ILTMKMSSKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSRTYLPVLDSLA 250
Cdd:cd18549  157 IFTIYFNKKMKKAFRRVREKIGEINAQLEDSLSGIRVVKAFANEEYEIEKFDEGNDRFLESKKKAYKAMAYFFSGMNFFT 236
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 404223395 251 GMLVVITLIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPMRMsgwLINDVQRF 302
Cdd:cd18549  237 NLLNLVVLVAGGYFIIKGEITLGDLVAFLLYVNVFIKPIRR---LVNFTEQY 285
type_I_sec_PrtD TIGR01842
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ...
110-560 8.46e-55

type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 200134 [Multi-domain]  Cd Length: 544  Bit Score: 194.49  E-value: 8.46e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  110 TRVGDIMARMTGDTDAIRHFVS-----------WVSYNILEnVFLFS--FAIIIMAAidwkltlALVIVTplIAILTMKM 176
Cdd:TIGR01842  95 RRGSGDGLQALRDLDQLRQFLTgpglfaffdapWMPIYLLV-CFLLHpwIGILALGG-------AVVLVG--LALLNNRA 164
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  177 SSKAqpvFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSAD-------VSRTYLPVLDSL 249
Cdd:TIGR01842 165 TKKP---LKEATEASIRANNLADSALRNAEVIEAMGMMGNLTKRWGRFHSKYLSAQSAASDragmlsnLSKYFRIVLQSL 241
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  250 agMLVVitlifGGYLVIKGQMTLGDLVAFNGFLWMLNGPMRMsgwLINDVQRFIAS--SFK-IQDMMATDAKIPIHAEKP 326
Cdd:TIGR01842 242 --VLGL-----GAYLAIDGEITPGMMIAGSILVGRALAPIDG---AIGGWKQFSGArqAYKrLNELLANYPSRDPAMPLP 311
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  327 APslQGHVEFKNVSFhFEDDPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVR 406
Cdd:TIGR01842 312 EP--EGHLSVENVTI-VPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRE 388
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  407 ELRNHIATVMQDIFLFSDTIEGNIAFGAPDATMEDVRRMARIADADHFIETMPESYDTIVGERGVGLSGGQKQRISLARA 486
Cdd:TIGR01842 389 TFGKHIGYLPQDVELFPGTVAENIARFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARA 468
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 404223395  487 LLKNPSILILDDTTSAVDMETEVKIQ---GELKKitENTTTFIIAHRISSVKEADEILILNHGEIIERGTHSSLLAE 560
Cdd:TIGR01842 469 LYGDPKLVVLDEPNSNLDEEGEQALAnaiKALKA--RGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
3-564 1.10e-54

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 200.64  E-value: 1.10e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395    3 SMKWIWQYVRKYRLLMIGVFILIFIASGISIIYPLLGGKVIDDV-----VYQNKTNLLIPLLLIMIISTIIRTICRYTYQ 77
Cdd:PTZ00265  812 NLRIVYREIFSYKKDVTIIALSILVAGGLYPVFALLYAKYVSTLfdfanLEANSNKYSLYILVIAIAMFISETLKNYYNN 891
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395   78 IMCERIGQNSLFRIRED-LYKKLQSLDFD-----FFNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENVFLFSFAIIIM 151
Cdd:PTZ00265  892 VIGEKVEKTMKRRLFENiLYQEISFFDQDkhapgLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSMVMSFYFCPIVA 971
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  152 AAidwkLTLALVIVTPLIAILTMKMSSKA-------QP----VFYEIRESFSRLNSMVEENISGNRVVKAFAREDFeMKK 220
Cdd:PTZ00265  972 AV----LTGTYFIFMRVFAIRARLTANKDvekkeinQPgtvfAYNSDDEIFKDPSFLIQEAFYNMNTVIIYGLEDY-FCN 1046
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  221 FHEHNEDFKKRNLDSADVSRTYLPVLDSLAGMLV-VITLIFGGYLVIKGQMTLGDLVAfNGFLWMLNGP-----MRMSGw 294
Cdd:PTZ00265 1047 LIEKAIDYSNKGQKRKTLVNSMLWGFSQSAQLFInSFAYWFGSFLIRRGTILVDDFMK-SLFTFLFTGSyagklMSLKG- 1124
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  295 linDVQRFIASSFKIQDMMATDAKIPIHAE-----KPAPSLQGHVEFKNVSFHFEDDPNTDVLKNISLKASPGQTIAILG 369
Cdd:PTZ00265 1125 ---DSENAKLSFEKYYPLIIRKSNIDVRDNggiriKNKNDIKGKIEIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIVG 1201
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  370 ETGAGKSTLVNLICRFYD------------------------------------------------------PTSGEILI 395
Cdd:PTZ00265 1202 ETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfKNSGKILL 1281
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  396 DGVDARKWHVRELRNHIATVMQDIFLFSDTIEGNIAFGAPDATMEDVRRMARIADADHFIETMPESYDTIVGERGVGLSG 475
Cdd:PTZ00265 1282 DGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSG 1361
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  476 GQKQRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITE--NTTTFIIAHRISSVKEADEILILNH----GEII 549
Cdd:PTZ00265 1362 GQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkaDKTIITIAHRIASIKRSDKIVVFNNpdrtGSFV 1441
                         650
                  ....*....|....*..
gi 404223395  550 E-RGTHSSLL-AEKGYY 564
Cdd:PTZ00265 1442 QaHGTHEELLsVQDGVY 1458
ABC_6TM_bac_exporter_ABCB8_10_like cd18576
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ...
22-306 5.83e-53

Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.


Pssm-ID: 350020 [Multi-domain]  Cd Length: 289  Bit Score: 182.30  E-value: 5.83e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  22 FILIFIASGISIIYPLLGGKVIDDVVYQNKTNLLIPLLLIMIISTIIRTICRYTYQIMCERIGQNSLFRIREDLYKKLQS 101
Cdd:cd18576    2 LILLLLSSAIGLVFPLLAGQLIDAALGGGDTASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 102 LDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENVFLFSFAIIIMAAIDWKLTLALVIVTPLIAILTM------- 174
Cdd:cd18576   82 LPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVlfgrrir 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 175 KMSSKAQpvfyeirESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSRTYLPVLDSLAGMLV 254
Cdd:cd18576  162 KLSKKVQ-------DELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAI 234
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 404223395 255 VITLIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPMRMSGWLINDVQRFIASS 306
Cdd:cd18576  235 VAVLWYGGRLVLAGELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKALGAS 286
ABC_6TM_exporter_like cd18564
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
16-290 1.26e-52

Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 350008 [Multi-domain]  Cd Length: 307  Bit Score: 181.94  E-value: 1.26e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  16 LLMIGVFILIFIASGISIIYPLlgGKVIDDVVYQNKTNLLIPLLLIMIIS---------------TIIRTICRYTYQIMC 80
Cdd:cd18564    1 LALALLALLLETALRLLEPWPL--KVVIDDVLGDKPLPGLLGLAPLLGPDplallllaaaalvgiALLRGLASYAGTYLT 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  81 ERIGQNSLFRIREDLYKKLQSLDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENVFLFSFAIIIMAAIDWKLTL 160
Cdd:cd18564   79 ALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGVMFWLDWQLAL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 161 ALVIVTPLIAILTMKMSSKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSR 240
Cdd:cd18564  159 IALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFARENRKSLRAGLRAARLQA 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 404223395 241 TYLPVLDSLAGMLVVITLIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPMR 290
Cdd:cd18564  239 LLSPVVDVLVAVGTALVLWFGAWLVLAGRLTPGDLLVFLAYLKNLYKPVR 288
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
352-569 7.21e-51

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 184.28  E-value: 7.21e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 352 LKNISLKASPGQTIAILGETGAGKSTLVNLICRFYdPTSGEILIDGVDARKWHVRELRNHIATVMQDIFLFSDTIEGNIA 431
Cdd:PRK11174 366 AGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVL 444
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 432 FGAPDATMEDVRRMARIADADHFIETMPESYDTIVGERGVGLSGGQKQRISLARALLKNPSILILDDTTSAVDMETEVKI 511
Cdd:PRK11174 445 LGNPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLV 524
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 404223395 512 QGELKKITENTTTFIIAHRISSVKEADEILILNHGEIIERGTHSSLLAEKGYYFDIYN 569
Cdd:PRK11174 525 MQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLA 582
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
335-548 2.78e-50

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: 171.25  E-value: 2.78e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 335 EFKNVSFHFEDDPNTdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIAT 414
Cdd:cd03246    2 EVENVSFRYPGAEPP-VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 415 VMQDIFLFSDTIEGNIafgapdatmedvrrmariadadhfietmpesydtivgergvgLSGGQKQRISLARALLKNPSIL 494
Cdd:cd03246   81 LPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRIL 118
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 404223395 495 ILDDTTSAVDMETEVKIQ---GELKKitENTTTFIIAHRISSVKEADEILILNHGEI 548
Cdd:cd03246  119 VLDEPNSHLDVEGERALNqaiAALKA--AGATRIVIAHRPETLASADRILVLEDGRV 173
ABC_6TM_exporter_like cd18550
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
18-289 2.79e-50

Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349994 [Multi-domain]  Cd Length: 294  Bit Score: 175.36  E-value: 2.79e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  18 MIGVFILIFIASGISIIYPLLGGKVIDDVVYQNKTNLLIPLLLIMIISTIIRTICRYTYQIMCERIGQNSLFRIREDLYK 97
Cdd:cd18550    1 LALVLLLILLSALLGLLPPLLLREIIDDALPQGDLGLLVLLALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRVQLYA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  98 KLQSLDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENVFLFSFAIIIMAAIDWKLTLALVIVTPLIAILTMKMS 177
Cdd:cd18550   81 HLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVLPTRRVG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 178 SKAQPVFYEIRESFSRLNSMVEE--NISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSRTYLPVLDSLAGMLVV 255
Cdd:cd18550  161 RRRRKLTREQQEKLAELNSIMQEtlSVSGALLVKLFGREDDEAARFARRSRELRDLGVRQALAGRWFFAALGLFTAIGPA 240
                        250       260       270
                 ....*....|....*....|....*....|....
gi 404223395 256 ITLIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPM 289
Cdd:cd18550  241 LVYWVGGLLVIGGGLTIGTLVAFTALLGRLYGPL 274
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
95-565 3.23e-50

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


Pssm-ID: 188098 [Multi-domain]  Cd Length: 1522  Bit Score: 187.46  E-value: 3.23e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395    95 LYKKLQSlDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENVF-LFSFAIIIMAAIdwklTLALVIVTPLIAILT 173
Cdd:TIGR00957 1045 LHNKLRS-PMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFnVIGALIVILLAT----PIAAVIIPPLGLLYF 1119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395   174 MKMSSKAQPVFYEIR-ESFSR--LNSMVEENISGNRVVKAFAR-EDFEmkkfheHNEDFK----KRNLDSADVSRTYLPV 245
Cdd:TIGR00957 1120 FVQRFYVASSRQLKRlESVSRspVYSHFNETLLGVSVIRAFEEqERFI------HQSDLKvdenQKAYYPSIVANRWLAV 1193
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395   246 LDSLAGMLVVItliFGGYLVIKGQMTL-----GDLVAFN-GFLWMLNGPMRMSgwliNDVQRFIASSFKIQDMMATDAKI 319
Cdd:TIGR00957 1194 RLECVGNCIVL---FAALFAVISRHSLsaglvGLSVSYSlQVTFYLNWLVRMS----SEMETNIVAVERLKEYSETEKEA 1266
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395   320 PIHAEKPAPSL----QGHVEFKNVSFHFEDDPNTdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILI 395
Cdd:TIGR00957 1267 PWQIQETAPPSgwppRGRVEFRNYCLRYREDLDL-VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIII 1345
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395   396 DGVDARKWHVRELRNHIATVMQDIFLFSDTIEGNI-AFGApdATMEDVRRMARIADADHFIETMPESYDTIVGERGVGLS 474
Cdd:TIGR00957 1346 DGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLdPFSQ--YSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLS 1423
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395   475 GGQKQRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHRISSVKEADEILILNHGEIIERGTH 554
Cdd:TIGR00957 1424 VGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAP 1503
                          490
                   ....*....|.
gi 404223395   555 SSLLAEKGYYF 565
Cdd:TIGR00957 1504 SNLLQQRGIFY 1514
ABC_6TM_exporter_like cd18565
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
74-306 1.47e-48

Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 350009 [Multi-domain]  Cd Length: 313  Bit Score: 171.21  E-value: 1.47e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  74 YTYQIMCERIGQNSLFRIREDLYKKLQSLDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENVFLFSFAIIIMAA 153
Cdd:cd18565   72 YLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFY 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 154 IDWKLTLALVIVTPLIAILTMKMSSKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNL 233
Cdd:cd18565  152 LNWQLALVALLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAEDFERERVADASEEYRDANW 231
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 404223395 234 DSADVSRTYLPVLDSLAGMLVVITLIFGGYLVIKG------QMTLGDLVAFNGFLWMLNGPMRMSGWLINDVQRFIASS 306
Cdd:cd18565  232 RAIRLRAAFFPVIRLVAGAGFVATFVVGGYWVLDGpplftgTLTVGTLVTFLFYTQRLLWPLTRLGDLIDQYQRAMASA 310
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
334-561 2.10e-48

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


Pssm-ID: 440739 [Multi-domain]  Cd Length: 230  Bit Score: 168.28  E-value: 2.10e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFEDDpnTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIA 413
Cdd:COG1122    1 IELENLSFSYPGG--TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 414 TVMQ--DIFLFSDTIEGNIAFG-----APDATMED-VRRMARIADADHFIETMPESydtivgergvgLSGGQKQRISLAR 485
Cdd:COG1122   79 LVFQnpDDQLFAPTVEEDVAFGpenlgLPREEIRErVEEALELVGLEHLADRPPHE-----------LSGGQKQRVAIAG 147
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 404223395 486 ALLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIA-HRISSVKE-ADEILILNHGEIIERGTHSSLLAEK 561
Cdd:COG1122  148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVtHDLDLVAElADRVIVLDDGRIVADGTPREVFSDY 225
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
332-553 4.63e-47

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: 163.74  E-value: 4.63e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 332 GHVEFKNVSFHFEDDpNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNH 411
Cdd:cd03369    5 GEIEVENLSVRYAPD-LPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSS 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 412 IATVMQDIFLFSDTIEGNIAfgaPDATMEDVRRMARIAdadhfietmpesydtiVGERGVGLSGGQKQRISLARALLKNP 491
Cdd:cd03369   84 LTIIPQDPTLFSGTIRSNLD---PFDEYSDEEIYGALR----------------VSEGGLNLSQGQRQLLCLARALLKRP 144
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 404223395 492 SILILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHRISSVKEADEILILNHGEIIERGT 553
Cdd:cd03369  145 RVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
335-547 7.91e-47

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: 7.91e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 335 EFKNVSFHFEDDpNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIAT 414
Cdd:cd03225    1 ELKNLSFSYPDG-ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 415 VMQ--DIFLFSDTIEGNIAFGA-----PDATMED-VRRMARIADADHFIETMPESydtivgergvgLSGGQKQRISLARA 486
Cdd:cd03225   80 VFQnpDDQFFGPTVEEEVAFGLenlglPEEEIEErVEEALELVGLEGLRDRSPFT-----------LSGGQKQRVAIAGV 148
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 404223395 487 LLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIA-HRISSVKE-ADEILILNHGE 547
Cdd:cd03225  149 LAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVtHDLDLLLElADRVIVLEDGK 211
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
334-547 9.78e-47

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: 162.64  E-value: 9.78e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFEDDPNTD--VLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGvdarkwhvrelrnH 411
Cdd:cd03250    1 ISVEDASFTWDSGEQETsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------S 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 412 IATVMQDIFLFSDTIEGNIAFGAPdatmEDVRRMARIADA-----DhfIETMPESYDTIVGERGVGLSGGQKQRISLARA 486
Cdd:cd03250   68 IAYVSQEPWIQNGTIRENILFGKP----FDEERYEKVIKAcalepD--LEILPDGDLTEIGEKGINLSGGQKQRISLARA 141
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 404223395 487 LLKNPSILILDDTTSAVDMETEVKI-----QGELKKiteNTTTFIIAHRISSVKEADEILILNHGE 547
Cdd:cd03250  142 VYSDADIYLLDDPLSAVDAHVGRHIfenciLGLLLN---NKTRILVTHQLQLLPHADQIVVLDNGR 204
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
352-501 1.92e-46

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


Pssm-ID: 394964 [Multi-domain]  Cd Length: 150  Bit Score: 160.12  E-value: 1.92e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  352 LKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIATVMQDIFLFSD-TIEGNI 430
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 404223395  431 AFGapdATMEDVRRMARIADADHFIETMPESY--DTIVGERGVGLSGGQKQRISLARALLKNPSILILDDTTS 501
Cdd:pfam00005  81 RLG---LLLKGLSKREKDARAEEALEKLGLGDlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
ABC_6TM_TAP_ABCB8_10_like cd18557
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ...
22-309 5.14e-46

Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.


Pssm-ID: 350001 [Multi-domain]  Cd Length: 289  Bit Score: 163.50  E-value: 5.14e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  22 FILIFIASGISIIYPLLGGKVIDDVV---YQNKTNLLIPLLLIMIISTIIRTICRYT-YQIMCERIgqnsLFRIREDLYK 97
Cdd:cd18557    2 LLFLLISSAAQLLLPYLIGRLIDTIIkggDLDVLNELALILLAIYLLQSVFTFVRYYlFNIAGERI----VARLRRDLFS 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  98 KLQSLDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENVFLFSFAIIIMAAIDWKLTLALVIVTPLIAILTMKMS 177
Cdd:cd18557   78 SLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 178 SKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSRTYLPVLDSLAGMLVVIT 257
Cdd:cd18557  158 RYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLV 237
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 404223395 258 LIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPMRMSGWLINDVQRFIASSFKI 309
Cdd:cd18557  238 LWYGGYLVLSGQLTVGELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289
ABC_6TM_Rv0194_D2_like cd18546
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ...
18-309 9.57e-46

Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349990 [Multi-domain]  Cd Length: 292  Bit Score: 163.04  E-value: 9.57e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  18 MIGVFILIFIASGISIIYPLLGGKVIDDVVYQNKTNLLIPLLLIMIISTIIRTICRYTYQIMCERIGQNSLFRIREDLYK 97
Cdd:cd18546    1 LALALLLVVVDTAASLAGPLLVRYGIDSGVRAGDLGVLLLAAAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  98 KLQSLDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENVFLFSFAIIIMAAIDWKLTLALVIVTPLIAILTMKMS 177
Cdd:cd18546   81 HLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALATRWFR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 178 SKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSRTYLPVLDSLAGMLVVIT 257
Cdd:cd18546  161 RRSSRAYRRARERIAAVNADLQETLAGIRVVQAFRRERRNAERFAELSDDYRDARLRAQRLVAIYFPGVELLGNLATAAV 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 404223395 258 LIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPMRMSGWLINDVQRFIASSFKI 309
Cdd:cd18546  241 LLVGAWRVAAGTLTVGVLVAFLLYLRRFFAPIQQLSQVFDSYQQARAALEKI 292
ABC_membrane pfam00664
ABC transporter transmembrane region; This family represents a unit of six transmembrane ...
18-289 1.05e-45

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: 459896 [Multi-domain]  Cd Length: 274  Bit Score: 162.43  E-value: 1.05e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395   18 MIGVFILIFIASGISIIYPLLGGKVIDDVVYQNKTNLLIPLLLIMIIS--TIIRTICRYTYQIMCERIGQNSLFRIREDL 95
Cdd:pfam00664   1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQALNVYSLALLllGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395   96 YKKLQSLDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENVFLFSFAIIIMAAIDWKLTLALVIVTPLIAILTMK 175
Cdd:pfam00664  81 FKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  176 MSSKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSRTYLPVLDSLAGMLVV 255
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYA 240
                         250       260       270
                  ....*....|....*....|....*....|....
gi 404223395  256 ITLIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPM 289
Cdd:pfam00664 241 LALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
143-579 1.84e-45

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 172.91  E-value: 1.84e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  143 LFSFAIIIMAAIDW------KLTLALVIVTPLIAILTMKMSSKAQpvfyeIRESFSRL---NSM--VEENISGNRVVKAF 211
Cdd:PTZ00265  178 IFTYASAFLGLYIWslfknaRLTLCITCVFPLIYICGVICNKKVK-----INKKTSLLynnNTMsiIEEALVGIRTVVSY 252
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  212 AREDFEMKKFHEHNEDFKKRNLDSADVSRTYLPVLDSLAGMLVVITLIFGGYLVIKGQMTLGDLVAFNG--FLWMLNG-- 287
Cdd:PTZ00265  253 CGEKTILKKFNLSEKLYSKYILKANFMESLHIGMINGFILASYAFGFWYGTRIIISDLSNQQPNNDFHGgsVISILLGvl 332
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  288 -PMRMSGWLINDVQRFIASsfkiqdMMATDAKIPIHAEKPA----------PSLQgHVEFKNVSFHFEDDPNTDVLKNIS 356
Cdd:PTZ00265  333 iSMFMLTIILPNITEYMKS------LEATNSLYEIINRKPLvennddgkklKDIK-KIQFKNVRFHYDTRKDVEIYKDLN 405
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  357 LKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILI-DGVDARKWHVRELRNHIATVMQDIFLFSDTIEGNIAF--- 432
Cdd:PTZ00265  406 FTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYsly 485
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  433 ---------------GAPDATMEDVRRMAR----------------------------IADAD-----------HFIETM 458
Cdd:PTZ00265  486 slkdlealsnyynedGNDSQENKNKRNSCRakcagdlndmsnttdsneliemrknyqtIKDSEvvdvskkvlihDFVSAL 565
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  459 PESYDTIVGERGVGLSGGQKQRISLARALLKNPSILILDDTTSAVDMETEVKIQGELK--KITENTTTFIIAHRISSVKE 536
Cdd:PTZ00265  566 PDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINnlKGNENRITIIIAHRLSTIRY 645
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  537 ADEILILNHGE-----------------------------------------------IIERGTHSSLLAEKG--YYFDI 567
Cdd:PTZ00265  646 ANTIFVLSNRErgstvdvdiigedptkdnkennnknnkddnnnnnnnnnnkinnagsyIIEQGTHDALMKNKNgiYYTMI 725
                         570
                  ....*....|..
gi 404223395  568 YNKQLGTEANVN 579
Cdd:PTZ00265  726 NNQKVSSKKSSN 737
ABC_6TM_exporter_like cd18540
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
15-305 1.97e-45

Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349984 [Multi-domain]  Cd Length: 295  Bit Score: 162.26  E-value: 1.97e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  15 RLLMIGVFILIFIASGISIIYPLLGGKVIDDVVYQNKTNLLIPLLLIMIISTIIRTICRYTYQIMCERIGQNSLFRIRED 94
Cdd:cd18540    1 KKLLILLIILMLLVALLDAVFPLLTKYAIDHFITPGTLDGLTGFILLYLGLILIQALSVFLFIRLAGKIEMGVSYDLRKK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  95 LYKKLQSLDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENVFLFSFAIIIMAAIDWKLTLALVIVTPLIAILTM 174
Cdd:cd18540   81 AFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVPVLAVVSI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 175 KMSSKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSRTYLPVLDSLAGMLV 254
Cdd:cd18540  161 YFQKKILKAYRKVRKINSRITGAFNEGITGAKTTKTLVREEKNLREFKELTEEMRRASVRAARLSALFLPIVLFLGSIAT 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 404223395 255 VITLIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPMRMSGWLINDVQRFIAS 305
Cdd:cd18540  241 ALVLWYGGILVLAGAITIGTLVAFISYATQFFEPIQQLARVLAELQSAQAS 291
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
334-552 5.47e-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: 158.45  E-value: 5.47e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFEDDPntdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRElRNhIA 413
Cdd:cd03259    1 LELKGLSKTYGSVR---ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPER-RN-IG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 414 TVMQDIFLFSD-TIEGNIAFG-----APDATMED-VRRMARIADADHFIETMPESydtivgergvgLSGGQKQRISLARA 486
Cdd:cd03259   76 MVFQDYALFPHlTVAENIAFGlklrgVPKAEIRArVRELLELVGLEGLLNRYPHE-----------LSGGQQQRVALARA 144
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 404223395 487 LLKNPSILILDDTTSAVDMETEVKIQGELKKITENT--TTFIIAHRISSVKE-ADEILILNHGEIIERG 552
Cdd:cd03259  145 LAREPSLLLLDEPLSALDAKLREELREELKELQRELgiTTIYVTHDQEEALAlADRIAVMNEGRIVQVG 213
ABC_6TM_LmrA_like cd18551
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ...
18-309 2.64e-44

Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349995 [Multi-domain]  Cd Length: 289  Bit Score: 159.14  E-value: 2.64e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  18 MIGVFILIFIASGISIIYPLLGGKVIDDVVYQNK-TNLLIPLLLIMIISTIIRTICRYtyqiMCERIGQNSLFRIREDLY 96
Cdd:cd18551    1 LILALLLSLLGTAASLAQPLLVKNLIDALSAGGSsGGLLALLVALFLLQAVLSALSSY----LLGRTGERVVLDLRRRLW 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  97 KKLQSLDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENVFLFSFAIIIMAAIDWKLTLALVIVTPLIAILTMKM 176
Cdd:cd18551   77 RRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILPL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 177 SSKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSRTYLPVLdSLAGMLVVI 256
Cdd:cd18551  157 GRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLM-GLAVQLALL 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 404223395 257 T-LIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPMRMSGWLINDVQRFIASSFKI 309
Cdd:cd18551  236 VvLGVGGARVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGALERI 289
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
334-559 5.43e-44

ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440740 [Multi-domain]  Cd Length: 514  Bit Score: 163.92  E-value: 5.43e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFEDDPNTDV--LKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWH---VREL 408
Cdd:COG1123  261 LEVRNLSKRYPVRGKGGVraVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLREL 340
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 409 RNHIATVMQDIF--LF-SDTIEGNIAFGApdatmeDVRRMARIADADHFIETM-------PESYDTIVGErgvgLSGGQK 478
Cdd:COG1123  341 RRRVQMVFQDPYssLNpRMTVGDIIAEPL------RLHGLLSRAERRERVAELlervglpPDLADRYPHE----LSGGQR 410
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 479 QRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITE--NTTTFIIAHRISSVKE-ADEILILNHGEIIERGTHS 555
Cdd:COG1123  411 QRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRelGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTE 490

                 ....
gi 404223395 556 SLLA 559
Cdd:COG1123  491 EVFA 494
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
334-552 1.80e-43

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: 153.24  E-value: 1.80e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFEDDpNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHvRELRNHIA 413
Cdd:cd03247    1 LSINNVSFSYPEQ-EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLIS 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 414 TVMQDIFLFSDTIEGNIafgapdatmedvrrmariadadhfietmpesydtivGERgvgLSGGQKQRISLARALLKNPSI 493
Cdd:cd03247   79 VLNQRPYLFDTTLRNNL------------------------------------GRR---FSGGERQRLALARILLQDAPI 119
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 404223395 494 LILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHRISSVKEADEILILNHGEIIERG 552
Cdd:cd03247  120 VLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
ABC_6TM_Tm287_like cd18548
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ...
18-306 2.54e-43

Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349992 [Multi-domain]  Cd Length: 292  Bit Score: 156.40  E-value: 2.54e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  18 MIGVFILIFIASGISIIYPLLGGKVIDDVVYQNKTNLLIPLLLIMIISTIIRTICRYTYQIMCERIGQNSLFRIREDLYK 97
Cdd:cd18548    1 AILAPLFKLLEVLLELLLPTLMADIIDEGIANGDLSYILRTGLLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  98 KLQSLDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENVFLFSFAIIIMAAIDWKLTLALVIVTPLIAILTMKMS 177
Cdd:cd18548   81 KIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPILALVVFLIM 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 178 SKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSRTYLPVLDSLAGMLVVIT 257
Cdd:cd18548  161 KKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPLMMLIMNLAIVAI 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 404223395 258 LIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPMRMSGWLINDVQRFIASS 306
Cdd:cd18548  241 LWFGGHLINAGSLQVGDLVAFINYLMQILMSLMMLSMVFVMLPRASASA 289
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
334-552 4.43e-43

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: 153.82  E-value: 4.43e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFEDDPNTD-VLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVD---ARKWHVRELR 409
Cdd:cd03257    2 LEVKNLSVSFPTGGGSVkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDllkLSRRLRKIRR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 410 NHIATVMQDIFL---FSDTIEGNIAFGAPDATMEDVRRMARIADADHFIEtMPESyDTIVGERGVGLSGGQKQRISLARA 486
Cdd:cd03257   82 KEIQMVFQDPMSslnPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVG-VGLP-EEVLNRYPHELSGGQRQRVAIARA 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 404223395 487 LLKNPSILILDDTTSAVDMETEVKIQGELKKITE--NTTTFIIAHRISSVKE-ADEILILNHGEIIERG 552
Cdd:cd03257  160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
334-560 7.65e-43

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 153.30  E-value: 7.65e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFEDdpnTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHvRELRNHIA 413
Cdd:COG1131    1 IEVRGLTKRYGD---KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDP-AEVRRRIG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 414 TVMQDIFLFSD-TIEGNIAFGapdATMEDVRRMARIADADHFIET--MPESYDTIVGErgvgLSGGQKQRISLARALLKN 490
Cdd:COG1131   77 YVPQEPALYPDlTVRENLRFF---ARLYGLPRKEARERIDELLELfgLTDAADRKVGT----LSGGMKQRLGLALALLHD 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 404223395 491 PSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIA-HRISSVKE-ADEILILNHGEIIERGTHSSLLAE 560
Cdd:COG1131  150 PELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLStHYLEEAERlCDRVAIIDKGRIVADGTPDELKAR 221
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
334-551 6.31e-42

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: 150.31  E-value: 6.31e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFED-DPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDarkwhVRELRNHI 412
Cdd:cd03293    1 LEVRNVSKTYGGgGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEP-----VTGPGPDR 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 413 ATVMQDIFLFS-DTIEGNIAFGapdATMEDVRRMARIADADHFIETmpesydtiVGERGVG------LSGGQKQRISLAR 485
Cdd:cd03293   76 GYVFQQDALLPwLTVLDNVALG---LELQGVPKAEARERAEELLEL--------VGLSGFEnayphqLSGGMRQRVALAR 144
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 404223395 486 ALLKNPSILILDDTTSAVDMETEVKIQGELKKI--TENTTTFIIAHrisSVKEA----DEILILN--HGEIIER 551
Cdd:cd03293  145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDIwrETGKTVLLVTH---DIDEAvflaDRVVVLSarPGRIVAE 215
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
334-559 9.28e-42

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: 150.42  E-value: 9.28e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFEDDPN-TDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDA---RKWHVRELR 409
Cdd:cd03258    2 IELKNVSKVFGDTGGkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLtllSGKELRKAR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 410 NHIATVMQDIFLFSD-TIEGNIAF-----GAPDATMED-VRRMARIADADHFIETMPESydtivgergvgLSGGQKQRIS 482
Cdd:cd03258   82 RRIGMIFQHFNLLSSrTVFENVALpleiaGVPKAEIEErVLELLELVGLEDKADAYPAQ-----------LSGGQKQRVG 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 483 LARALLKNPSILILDDTTSAVDMETEVKIQGELKKITE--NTTTFIIAHRISSVKE-ADEILILNHGEIIERGTHSSLLA 559
Cdd:cd03258  151 IARALANNPKVLLCDEATSALDPETTQSILALLRDINRelGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVFA 230
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
335-562 1.10e-41

ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];


Pssm-ID: 443618 [Multi-domain]  Cd Length: 243  Bit Score: 150.39  E-value: 1.10e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 335 EFKNVSFHFEDDPntdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKwHVRELRNHIAT 414
Cdd:COG4555    3 EVENLSKKYGKVP---ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRK-EPREARRQIGV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 415 VMQDIFLFSD-TIEGNIAFGAPDATMEDVRRMARIADADHFIEtMPESYDTIVGErgvgLSGGQKQRISLARALLKNPSI 493
Cdd:COG4555   79 LPDERGLYDRlTVRENIRYFAELYGLFDEELKKRIEELIELLG-LEEFLDRRVGE----LSTGMKKKVALARALVHDPKV 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 404223395 494 LILDDTTSAVDMETEVKIQGELKKITENTTTFIIA-HRISSVKE-ADEILILNHGEIIERGTHSSLLAEKG 562
Cdd:COG4555  154 LLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSsHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
334-553 1.89e-40

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 150.25  E-value: 1.89e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFEDdpnTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARkwHVR-ELRNhI 412
Cdd:COG3842    6 LELENVSKRYGD---VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVT--GLPpEKRN-V 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 413 ATVMQDIFLFSD-TIEGNIAFG-----APDATMED-VRRMARIADADHFIETMPESydtivgergvgLSGGQKQRISLAR 485
Cdd:COG3842   80 GMVFQDYALFPHlTVAENVAFGlrmrgVPKAEIRArVAELLELVGLEGLADRYPHQ-----------LSGGQQQRVALAR 148
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 404223395 486 ALLKNPSILILDDTTSAVDMETEVKIQGELKKITENT-TTFIIA-HrisSVKEA----DEILILNHGEIIERGT 553
Cdd:COG3842  149 ALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELgITFIYVtH---DQEEAlalaDRIAVMNDGRIEQVGT 219
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
335-547 1.52e-39

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: 141.61  E-value: 1.52e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 335 EFKNVSFHFEDDPntdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIAT 414
Cdd:cd00267    1 EIENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 415 VMQdiflfsdtiegniafgapdatmedvrrmariadadhfietmpesydtivgergvgLSGGQKQRISLARALLKNPSIL 494
Cdd:cd00267   78 VPQ-------------------------------------------------------LSGGQRQRVALARALLLNPDLL 102
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 404223395 495 ILDDTTSAVDMETEVKIQGELKKITENTTTFIIA-HRISSVKEA-DEILILNHGE 547
Cdd:cd00267  103 LLDEPTSGLDPASRERLLELLRELAEEGRTVIIVtHDPELAELAaDRVIVLKDGK 157
PLN03130 PLN03130
ABC transporter C family member; Provisional
313-565 3.54e-39

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 154.13  E-value: 3.54e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  313 MATDAKIPIHAEKPAPS--LQGHVEFKNVSFHFEDD--PntdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDP 388
Cdd:PLN03130 1215 LPSEAPLVIENNRPPPGwpSSGSIKFEDVVLRYRPElpP---VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVEL 1291
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  389 TSGEILIDGVDARKWHVRELRNHIATVMQDIFLFSDTIEGNI-AFGA-PDATMEDVRRMARIADAdhfIETMPESYDTIV 466
Cdd:PLN03130 1292 ERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLdPFNEhNDADLWESLERAHLKDV---IRRNSLGLDAEV 1368
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  467 GERGVGLSGGQKQRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHRISSVKEADEILILNHG 546
Cdd:PLN03130 1369 SEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAG 1448
                         250
                  ....*....|....*....
gi 404223395  547 EIIERGTHSSLLAEKGYYF 565
Cdd:PLN03130 1449 RVVEFDTPENLLSNEGSAF 1467
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
334-548 4.00e-39

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


Pssm-ID: 213222 [Multi-domain]  Cd Length: 218  Bit Score: 142.63  E-value: 4.00e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHF-EDDPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVREL---- 408
Cdd:cd03255    1 IELKNLSKTYgGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 409 RNHIATVMQDIFLFSD-TIEGNIAFGAPDATMEDVRRMARIADA------DHFIETMPESydtivgergvgLSGGQKQRI 481
Cdd:cd03255   81 RRHIGFVFQSFNLLPDlTALENVELPLLLAGVPKKERRERAEELlervglGDRLNHYPSE-----------LSGGQQQRV 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 404223395 482 SLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITE--NTTTFIIAHRISSVKEADEILILNHGEI 548
Cdd:cd03255  150 AIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKeaGTTIVVVTHDPELAEYADRIIELRDGKI 218
ABCC_SUR2 cd03288
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...
330-568 4.34e-39

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


Pssm-ID: 213255 [Multi-domain]  Cd Length: 257  Bit Score: 143.90  E-value: 4.34e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 330 LQGHVEFKNVSFHFEDDPNTdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELR 409
Cdd:cd03288   16 LGGEIKIHDLCVRYENNLKP-VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLR 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 410 NHIATVMQDIFLFSDTIEGNIAfgaPDATMEDVR--RMARIADADHFIETMPESYDTIVGERGVGLSGGQKQRISLARAL 487
Cdd:cd03288   95 SRLSIILQDPILFSGSIRFNLD---PECKCTDDRlwEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAF 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 488 LKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHRISSVKEADEILILNHGEIIERGTHSSLLAEKGYYFDI 567
Cdd:cd03288  172 VRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVFAS 251

                 .
gi 404223395 568 Y 568
Cdd:cd03288  252 L 252
ABC_6TM_TAP cd18572
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ...
22-309 1.08e-38

Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.


Pssm-ID: 350016 [Multi-domain]  Cd Length: 289  Bit Score: 143.84  E-value: 1.08e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  22 FILIFIASGISIIYPLLGGKVIDDVVYQNKTNLLIPLLLIMIISTIIRTIC----RYTYQImcerIGQNSLFRIREDLYK 97
Cdd:cd18572    2 FVFLVVAALSELAIPHYTGAVIDAVVADGSREAFYRAVLLLLLLSVLSGLFsglrGGCFSY----AGTRLVRRLRRDLFR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  98 KLQSLDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENVFLFSFAIIIMAAIDWKLTLALVIVTPLIAILTMKMS 177
Cdd:cd18572   78 SLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 178 SKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSRTYLPVLDSLAGMLVVIT 257
Cdd:cd18572  158 RYYRKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLV 237
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 404223395 258 LIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPMRMSGWLINDVQRFIASSFKI 309
Cdd:cd18572  238 LFYGGHLVLSGRMSAGQLVTFMLYQQQLGEAFQSLGDVFSSLMQAVGAAEKV 289
PLN03232 PLN03232
ABC transporter C family member; Provisional
106-565 1.50e-38

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 152.44  E-value: 1.50e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  106 FFNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENVF--LFSFAIIIMAAidwklTLALVIVTPLI-----AILTMKMSS 178
Cdd:PLN03232 1000 FFHTNPTGRVINRFSKDIGDIDRNVANLMNMFMNQLWqlLSTFALIGTVS-----TISLWAIMPLLilfyaAYLYYQSTS 1074
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  179 KA---------QPVFYEIRESFSRLNSMveenisgnRVVKAFAREDFEMKKFHEHNEDFKKRNLDSadvSRTYLPVLDSL 249
Cdd:PLN03232 1075 REvrrldsvtrSPIYAQFGEALNGLSSI--------RAYKAYDRMAKINGKSMDNNIRFTLANTSS---NRWLTIRLETL 1143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  250 AGMLVVITLIFG--GYLVIKGQM----TLGDLVAFN-GFLWMLNGPMRMSGWLINDVQRFIASSFKIQdmMATDAKIPIH 322
Cdd:PLN03232 1144 GGVMIWLTATFAvlRNGNAENQAgfasTMGLLLSYTlNITTLLSGVLRQASKAENSLNSVERVGNYID--LPSEATAIIE 1221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  323 AEKPAPS--LQGHVEFKNVsfHFEDDPN-TDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVD 399
Cdd:PLN03232 1222 NNRPVSGwpSRGSIKFEDV--HLRYRPGlPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCD 1299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  400 ARKWHVRELRNHIATVMQDIFLFSDTIEGNI-AFGA-PDATMEDVRRMARIADAdhfIETMPESYDTIVGERGVGLSGGQ 477
Cdd:PLN03232 1300 VAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIdPFSEhNDADLWEALERAHIKDV---IDRNPFGLDAEVSEGGENFSVGQ 1376
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  478 KQRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHRISSVKEADEILILNHGEIIERGTHSSL 557
Cdd:PLN03232 1377 RQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQEL 1456

                  ....*...
gi 404223395  558 LAEKGYYF 565
Cdd:PLN03232 1457 LSRDTSAF 1464
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
334-552 1.58e-38

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: 141.16  E-value: 1.58e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFEDDpntDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYD-----PTSGEILIDGVDARKWHVR-- 406
Cdd:cd03260    1 IELRDLNVYYGDK---HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDvl 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 407 ELRNHIATVMQDIFLFSDTIEGNIAFG----------APDATMEDVRRMARIADAdhfietmpesydtiVGER--GVGLS 474
Cdd:cd03260   78 ELRRRVGMVFQKPNPFPGSIYDNVAYGlrlhgiklkeELDERVEEALRKAALWDE--------------VKDRlhALGLS 143
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 404223395 475 GGQKQRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHRISSVKE-ADEILILNHGEIIERG 552
Cdd:cd03260  144 GGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFG 222
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
334-547 2.52e-38

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: 139.24  E-value: 2.52e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFeddPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARK--WHVRELRNH 411
Cdd:cd03229    1 LELKNVSKRY---GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDleDELPPLRRR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 412 IATVMQDIFLFSD-TIEGNIAFgapdatmedvrrmariadadhfietmpesydtivgergvGLSGGQKQRISLARALLKN 490
Cdd:cd03229   78 IGMVFQDFALFPHlTVLENIAL---------------------------------------GLSGGQQQRVALARALAMD 118
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 491 PSILILDDTTSAVDMETEVKIQGELKKITEN--TTTFIIAHRISSVKE-ADEILILNHGE 547
Cdd:cd03229  119 PDVLLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARlADRVVVLRDGK 178
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
333-550 2.65e-38

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


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 141.77  E-value: 2.65e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 333 HVEFKNVSFHFEDDPN-TDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDarkwhVRELRNH 411
Cdd:COG1116    7 ALELRGVSKRFPTGGGgVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKP-----VTGPGPD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 412 IATVMQDIFLFs-dTIEGNIAFGAPdatMEDVRRMARIADADHFIEtmpesydtIVGERGVG------LSGGQKQRISLA 484
Cdd:COG1116   82 RGVVFQEPALLpwlTVLDNVALGLE---LRGVPKAERRERARELLE--------LVGLAGFEdayphqLSGGMRQRVAIA 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 404223395 485 RALLKNPSILILDDTTSAVDMETEVKIQGELKKI--TENTTTFIIAHrisSVKEA----DEILILNH--GEIIE 550
Cdd:COG1116  151 RALANDPEVLLMDEPFGALDALTRERLQDELLRLwqETGKTVLFVTH---DVDEAvflaDRVVVLSArpGRIVE 221
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
334-559 3.52e-38

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: 140.90  E-value: 3.52e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFEDDPNtdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIA 413
Cdd:cd03295    1 IEFENVTKRYGGGKK--AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 414 TVMQDIFLFSD-TIEGNIAFgAPdaTMEDVRRMARIADADHFIETM---PESYdtivGERGVG-LSGGQKQRISLARALL 488
Cdd:cd03295   79 YVIQQIGLFPHmTVEENIAL-VP--KLLKWPKEKIRERADELLALVgldPAEF----ADRYPHeLSGGQQQRVGVARALA 151
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 404223395 489 KNPSILILDDTTSAVDMETEVKIQGELKKITE--NTTTFIIAHRI-SSVKEADEILILNHGEIIERGTHSSLLA 559
Cdd:cd03295  152 ADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILR 225
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
334-559 1.66e-37

ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440740 [Multi-domain]  Cd Length: 514  Bit Score: 145.43  E-value: 1.66e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFEDDPNTdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPT---SGEILIDGVDARKWHVRELRN 410
Cdd:COG1123    5 LEVRDLSVRYPGGDVP-AVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 411 HIATVMQDIF--LFSDTIEGNIAFG------APDATMEDVRRMARIADADHFIETMPESydtivgergvgLSGGQKQRIS 482
Cdd:COG1123   84 RIGMVFQDPMtqLNPVTVGDQIAEAlenlglSRAEARARVLELLEAVGLERRLDRYPHQ-----------LSGGQRQRVA 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 483 LARALLKNPSILILDDTTSAVDMETEVKIQGELKKITE--NTTTFIIAHRISSVKE-ADEILILNHGEIIERGTHSSLLA 559
Cdd:COG1123  153 IAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRerGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILA 232
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
334-548 1.92e-37

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: 136.37  E-value: 1.92e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFeddPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKwHVRELRNHIA 413
Cdd:cd03230    1 IEVRNLSKRY---GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 414 TVMQDIFLFSD-TIEGNIAfgapdatmedvrrmariadadhfietmpesydtivgergvgLSGGQKQRISLARALLKNPS 492
Cdd:cd03230   77 YLPEEPSLYENlTVRENLK-----------------------------------------LSGGMKQRLALAQALLHDPE 115
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 404223395 493 ILILDDTTSAVDMETEVKIQGELKKIT-ENTTTFIIAHRISSVKE-ADEILILNHGEI 548
Cdd:cd03230  116 LLILDEPTSGLDPESRREFWELLRELKkEGKTILLSSHILEEAERlCDRVAILNNGRI 173
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
334-559 2.51e-37

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


Pssm-ID: 440741 [Multi-domain]  Cd Length: 248  Bit Score: 138.78  E-value: 2.51e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHF-EDDPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHI 412
Cdd:COG1124    2 LEVRNLSVSYgQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 413 ATVMQDiflfsdtiegniAFGA--PDATMEDV-----------RRMARIADAdhfIET--MPESY-DTIVGErgvgLSGG 476
Cdd:COG1124   82 QMVFQD------------PYASlhPRHTVDRIlaeplrihglpDREERIAEL---LEQvgLPPSFlDRYPHQ----LSGG 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 477 QKQRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITE--NTTTFIIAHRISSVKE-ADEILILNHGEIIERGT 553
Cdd:COG1124  143 QRQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREerGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELT 222

                 ....*.
gi 404223395 554 HSSLLA 559
Cdd:COG1124  223 VADLLA 228
ABC_6TM_PCAT1_LagD_like cd18570
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ...
15-311 8.03e-37

Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.


Pssm-ID: 350014 [Multi-domain]  Cd Length: 294  Bit Score: 138.73  E-value: 8.03e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  15 RLLMIGVFILIFIASGISIIYPLLGGKVIDDVVYQNKTNLLIPLLLIMIISTIIRTICRYTYQIMCERIGQNSLFRIRED 94
Cdd:cd18570    1 KKLLILILLLSLLITLLGIAGSFFFQILIDDIIPSGDINLLNIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  95 LYKKLQSLDFDFFNNTRVGDIMARMTgDTDAIRHFVSWVSYNILENVFLFSFAIIIMAAIDWKLTLALVIVTPLIAILTM 174
Cdd:cd18570   81 YFKHLLKLPLSFFETRKTGEIISRFN-DANKIREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPLYILIIL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 175 KMSSKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSRTYLPVLDSLAGMLV 254
Cdd:cd18570  160 LFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLISLIGS 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 404223395 255 VITLIFGGYLVIKGQMTLGDLVAFNGflwmlngpmrMSGWLINDVQRFIASSFKIQD 311
Cdd:cd18570  240 LLILWIGSYLVIKGQLSLGQLIAFNA----------LLGYFLGPIENLINLQPKIQE 286
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
335-548 1.88e-36

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 134.94  E-value: 1.88e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 335 EFKNVSFHFEDDPntdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIAT 414
Cdd:COG4619    2 ELEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 415 VMQDIFLFSDTIEGNIAFGA----PDATMEDVRR-MARIAdadhfietMPESY-DTIVGErgvgLSGGQKQRISLARALL 488
Cdd:COG4619   79 VPQEPALWGGTVRDNLPFPFqlreRKFDRERALElLERLG--------LPPDIlDKPVER----LSGGERQRLALIRALL 146
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 404223395 489 KNPSILILDDTTSAVDMETEVKIQGELKKI--TENTTTFIIAH---RISSVkeADEILILNHGEI 548
Cdd:COG4619  147 LQPDVLLLDEPTSALDPENTRRVEELLREYlaEEGRAVLWVSHdpeQIERV--ADRVLTLEAGRL 209
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
333-553 2.74e-36

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 138.29  E-value: 2.74e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 333 HVEFKNVSFHFE-DDPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVD---ARKWHVREL 408
Cdd:COG1135    1 MIELENLSKTFPtKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDltaLSERELRAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 409 RNHIATVMQDIFLF-SDTIEGNIAF-----GAPDAtmedvRRMARIAD----------ADHFietmPESydtivgergvg 472
Cdd:COG1135   81 RRKIGMIFQHFNLLsSRTVAENVALpleiaGVPKA-----EIRKRVAEllelvglsdkADAY----PSQ----------- 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 473 LSGGQKQRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITE--NTTTFIIAHRISSVKE-ADEILILNHGEII 549
Cdd:COG1135  141 LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRelGLTIVLITHEMDVVRRiCDRVAVLENGRIV 220

                 ....
gi 404223395 550 ERGT 553
Cdd:COG1135  221 EQGP 224
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
334-550 2.85e-36

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 134.79  E-value: 2.85e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFEDDPntDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVD---ARKWHVRELRN 410
Cdd:COG2884    2 IRFENVSKRYPGGR--EALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDlsrLKRREIPYLRR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 411 HIATVMQDIFLFSD-TIEGNIAF-----GAPDATMEdvrrmARIADA------DHFIETMPESydtivgergvgLSGGQK 478
Cdd:COG2884   80 RIGVVFQDFRLLPDrTVYENVALplrvtGKSRKEIR-----RRVREVldlvglSDKAKALPHE-----------LSGGEQ 143
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 404223395 479 QRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIA-HRISSVKEADE-ILILNHGEIIE 550
Cdd:COG2884  144 QRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIAtHDLELVDRMPKrVLELEDGRLVR 217
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
351-558 6.26e-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: 134.39  E-value: 6.26e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 351 VLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHvRELRNhIATVMQDIFLFSD-TIEGN 429
Cdd:cd03299   14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLP-PEKRD-ISYVPQNYALFPHmTVYKN 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 430 IAFG-----APDATME-DVRRMARIADADHFIETMPESydtivgergvgLSGGQKQRISLARALLKNPSILILDDTTSAV 503
Cdd:cd03299   92 IAYGlkkrkVDKKEIErKVLEIAEMLGIDHLLNRKPET-----------LSGGEQQRVAIARALVVNPKILLLDEPFSAL 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 404223395 504 DMETEVKIQGELKKI-TENTTTFI-IAHRISSVKE-ADEILILNHGEIIERGTHSSLL 558
Cdd:cd03299  161 DVRTKEKLREELKKIrKEFGVTVLhVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVF 218
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
335-552 3.62e-35

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: 130.63  E-value: 3.62e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 335 EFKNVSFHFeddPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIAT 414
Cdd:cd03214    1 EVENLSVGY---GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 415 VMQdiflfsdtiegniafgapdaTMEDVrrmariaDADHFIEtmpESYDTivgergvgLSGGQKQRISLARALLKNPSIL 494
Cdd:cd03214   78 VPQ--------------------ALELL-------GLAHLAD---RPFNE--------LSGGERQRVLLARALAQEPPIL 119
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 404223395 495 ILDDTTSAVDMETEVKIQGELKKIT--ENTTTFIIAHRISSV-KEADEILILNHGEIIERG 552
Cdd:cd03214  120 LLDEPTSHLDIAHQIELLELLRRLAreRGKTVVMVLHDLNLAaRYADRVILLKDGRIVAQG 180
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
334-550 8.49e-35

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 130.93  E-value: 8.49e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFEDDPN-TDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVREL---- 408
Cdd:COG1136    5 LELRNLTKSYGTGEGeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELarlr 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 409 RNHIATVMQDIFLFSD-TIEGNIAF-----GAPDAtmEDVRRMARIADA---DHFIETMPESydtivgergvgLSGGQKQ 479
Cdd:COG1136   85 RRHIGFVFQFFNLLPElTALENVALplllaGVSRK--ERRERARELLERvglGDRLDHRPSQ-----------LSGGQQQ 151
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 404223395 480 RISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITENT-TTFIIA-HRISSVKEADEILILNHGEIIE 550
Cdd:COG1136  152 RVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELgTTIVMVtHDPELAARADRVIRLRDGRIVS 224
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
334-553 1.59e-34

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


Pssm-ID: 213228 [Multi-domain]  Cd Length: 235  Bit Score: 130.70  E-value: 1.59e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFEDDPntdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVREL---RN 410
Cdd:cd03261    1 IELRGLTKSFGGRT---VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELyrlRR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 411 HIATVMQDIFLFSD-TIEGNIAFGAPDATMEDVRRMARIAdadhfIETMPEsydtiVGERGVG------LSGGQKQRISL 483
Cdd:cd03261   78 RMGMLFQSGALFDSlTVFENVAFPLREHTRLSEEEIREIV-----LEKLEA-----VGLRGAEdlypaeLSGGMKKRVAL 147
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 404223395 484 ARALLKNPSILILDDTTSAVDMETEVKIQG---ELKKiTENTTTFIIAHRISSVKE-ADEILILNHGEIIERGT 553
Cdd:cd03261  148 ARALALDPELLLYDEPTAGLDPIASGVIDDlirSLKK-ELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGT 220
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
334-553 2.68e-34

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


Pssm-ID: 440737 [Multi-domain]  Cd Length: 254  Bit Score: 130.55  E-value: 2.68e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFeddPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIA 413
Cdd:COG1120    2 LEAENLSVGY---GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 414 TVMQDI---FLFS--DTIE-GNI----AFGAPDATMED-VRRMARIADADHFIETmpeSYDTivgergvgLSGGQKQRIS 482
Cdd:COG1120   79 YVPQEPpapFGLTvrELVAlGRYphlgLFGRPSAEDREaVEEALERTGLEHLADR---PVDE--------LSGGERQRVL 147
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 404223395 483 LARALLKNPSILILDDTTSAVDMETEVKIQGELKKIT--ENTTTFIIAHRIS-SVKEADEILILNHGEIIERGT 553
Cdd:COG1120  148 IARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLAreRGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGP 221
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
335-561 2.95e-34

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: 130.00  E-value: 2.95e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 335 EFKNVSFHFEDDpnTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRN---H 411
Cdd:cd03256    2 EVENLSKTYPNG--KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQlrrQ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 412 IATVMQDIFLFSD-TIEGNIAFGAPdATMEDVRRMAR------IADADHFIET--MPESYDTIVGErgvgLSGGQKQRIS 482
Cdd:cd03256   80 IGMIFQQFNLIERlSVLENVLSGRL-GRRSTWRSLFGlfpkeeKQRALAALERvgLLDKAYQRADQ----LSGGQQQRVA 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 483 LARALLKNPSILILDDTTSAVDMETEVKIQGELKKI--TENTTTFIIAHRISSVKE-ADEILILNHGEIIERGTHSSLLA 559
Cdd:cd03256  155 IARALMQQPKLILADEPVASLDPASSRQVMDLLKRInrEEGITVIVSLHQVDLAREyADRIVGLKDGRIVFDGPPAELTD 234

                 ..
gi 404223395 560 EK 561
Cdd:cd03256  235 EV 236
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
334-553 3.67e-34

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


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 132.89  E-value: 3.67e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFEDDPntdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRElRNhIA 413
Cdd:COG3839    4 LELENVSKSYGGVE---ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD-RN-IA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 414 TVMQDIFLF-SDTIEGNIAFG-----APDATMED-VRRMARIADADHFIETMPEsydtivgergvGLSGGQKQRISLARA 486
Cdd:COG3839   79 MVFQSYALYpHMTVYENIAFPlklrkVPKAEIDRrVREAAELLGLEDLLDRKPK-----------QLSGGQRQRVALGRA 147
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 404223395 487 LLKNPSILILDDTTSAVDMETEVKIQGELKKITENT-TTFIIA-HRISsvkEA----DEILILNHGEIIERGT 553
Cdd:COG3839  148 LVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLgTTTIYVtHDQV---EAmtlaDRIAVMNDGRIQQVGT 217
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
334-553 3.96e-34

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


Pssm-ID: 440744 [Multi-domain]  Cd Length: 241  Bit Score: 129.71  E-value: 3.96e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFEDDPntdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVD---ARKWHVRELRN 410
Cdd:COG1127    6 IEVRNLTKSFGDRV---VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDitgLSEKELYELRR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 411 HIATVMQDIFLFSD-TIEGNIAF------GAPDATMED-VR---RMARIADADHFietMPesydtivGErgvgLSGGQKQ 479
Cdd:COG1127   83 RIGMLFQGGALFDSlTVFENVAFplrehtDLSEAEIRElVLeklELVGLPGAADK---MP-------SE----LSGGMRK 148
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 404223395 480 RISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITE--NTTTFIIAHRISSVKE-ADEILILNHGEIIERGT 553
Cdd:COG1127  149 RVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDelGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGT 225
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
334-561 7.85e-34

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 129.73  E-value: 7.85e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFEDDPNTdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIA 413
Cdd:PRK13632   8 IKVENVSFSYPNSENN-ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 414 TVMQ--DIFLFSDTIEGNIAFG-----APDATMED-VRRMARIADADHFIETMPESydtivgergvgLSGGQKQRISLAR 485
Cdd:PRK13632  87 IIFQnpDNQFIGATVEDDIAFGlenkkVPPKKMKDiIDDLAKKVGMEDYLDKEPQN-----------LSGGQKQRVAIAS 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 486 ALLKNPSILILDDTTSAVD---METEVKIQGELKKitENTTTFI-IAHRISSVKEADEILILNHGEIIERGTHSSLLAEK 561
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLDpkgKREIKKIMVDLRK--TRKKTLIsITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNK 233
ECF_ATPase_1 TIGR04520
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
334-561 1.10e-33

energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]


Pssm-ID: 275313 [Multi-domain]  Cd Length: 268  Bit Score: 129.09  E-value: 1.10e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  334 VEFKNVSFHFEDDpNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDAR-KWHVRELRNHI 412
Cdd:TIGR04520   1 IEVENVSFSYPES-EKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLdEENLWEIRKKV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  413 ATVMQ--DIFLFSDTIEGNIAFG-----APDATMEdvrrmARIADA------DHFIETMPESydtivgergvgLSGGQKQ 479
Cdd:TIGR04520  80 GMVFQnpDNQFVGATVEDDVAFGlenlgVPREEMR-----KRVDEAlklvgmEDFRDREPHL-----------LSGGQKQ 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  480 RISLARALLKNPSILILDDTTSAVD-------METEVKIQGElkkitENTTTFIIAHRISSVKEADEILILNHGEIIERG 552
Cdd:TIGR04520 144 RVAIAGVLAMRPDIIILDEATSMLDpkgrkevLETIRKLNKE-----EGITVISITHDMEEAVLADRVIVMNKGKIVAEG 218

                  ....*....
gi 404223395  553 THSSLLAEK 561
Cdd:TIGR04520 219 TPREIFSQV 227
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
334-553 1.71e-33

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


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 127.80  E-value: 1.71e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFEDdpnTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDG--VDARKWHVRELRNH 411
Cdd:COG1126    2 IEIENLHKSFGD---LEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGedLTDSKKDINKLRRK 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 412 IATVMQDIFLFSD-TIEGNIAFgAPdatmEDVRRMAR---IADADHFIET--MPESYDTIVGErgvgLSGGQKQRISLAR 485
Cdd:COG1126   79 VGMVFQQFNLFPHlTVLENVTL-AP----IKVKKMSKaeaEERAMELLERvgLADKADAYPAQ----LSGGQQQRVAIAR 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 404223395 486 ALLKNPSILILDDTTSAVD--METEV-KIQGELKKitENTTTFIIAHRISSVKE-ADEILILNHGEIIERGT 553
Cdd:COG1126  150 ALAMEPKVMLFDEPTSALDpeLVGEVlDVMRDLAK--EGMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGP 219
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
334-570 1.96e-33

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: 127.35  E-value: 1.96e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFEDDPntdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARkwHVRELRNHIA 413
Cdd:cd03300    1 IELENVSKFYGGFV---ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDIT--NLPPHKRPVN 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 414 TVMQDIFLFSD-TIEGNIAFG------APDATMEDVRRMARIADADHFIETMPESydtivgergvgLSGGQKQRISLARA 486
Cdd:cd03300   76 TVFQNYALFPHlTVFENIAFGlrlkklPKAEIKERVAEALDLVQLEGYANRKPSQ-----------LSGGQQQRVAIARA 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 487 LLKNPSILILDDTTSAVDMETEVKIQGELKKITENT-TTFI-IAHRISsvkEA----DEILILNHGEIIERGTHSsllae 560
Cdd:cd03300  145 LVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELgITFVfVTHDQE---EAltmsDRIAVMNKGKIQQIGTPE----- 216
                        250
                 ....*....|
gi 404223395 561 kgyyfDIYNK 570
Cdd:cd03300  217 -----EIYEE 221
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
334-548 2.39e-33

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


Pssm-ID: 213268 [Multi-domain]  Cd Length: 213  Bit Score: 126.60  E-value: 2.39e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFeddPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRElRNhIA 413
Cdd:cd03301    1 VELENVTKRF---GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD-RD-IA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 414 TVMQDIFLFSD-TIEGNIAFG------APDATMEDVRRMARIADADHFIETMPESydtivgergvgLSGGQKQRISLARA 486
Cdd:cd03301   76 MVFQNYALYPHmTVYDNIAFGlklrkvPKDEIDERVREVAELLQIEHLLDRKPKQ-----------LSGGQRQRVALGRA 144
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 404223395 487 LLKNPSILILDDTTSAVDMETEVKIQGELKKITEN--TTTFIIAH-RISSVKEADEILILNHGEI 548
Cdd:cd03301  145 IVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRlgTTTIYVTHdQVEAMTMADRIAVMNDGQI 209
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
335-546 5.50e-33

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: 125.72  E-value: 5.50e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 335 EFKNVSFHFEDDPntdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKwhvreLRNHIAT 414
Cdd:cd03235    1 EVEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK-----ERKRIGY 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 415 VMQdiflfsdtiEGNIAFGAPdATMEDVRRMARIADADHFIETMPESYDTI------VG-----ERGVG-LSGGQKQRIS 482
Cdd:cd03235   73 VPQ---------RRSIDRDFP-ISVRDVVLMGLYGHKGLFRRLSKADKAKVdealerVGlselaDRQIGeLSGGQQQRVL 142
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 404223395 483 LARALLKNPSILILDDTTSAVDMETEVKIQGELKKIT-ENTTTFIIAHRISSVKE-ADEILILNHG 546
Cdd:cd03235  143 LARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRrEGMTILVVTHDLGLVLEyFDRVLLLNRT 208
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
334-548 1.30e-32

Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages


Pssm-ID: 213259 [Multi-domain]  Cd Length: 214  Bit Score: 124.44  E-value: 1.30e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFEddPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRE---LRN 410
Cdd:cd03292    1 IEFINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipyLRR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 411 HIATVMQDIFLFSD-TIEGNIAFG------APDATMEDVRRMARIADADHFIETMPEsydtivgergvGLSGGQKQRISL 483
Cdd:cd03292   79 KIGVVFQDFRLLPDrNVYENVAFAlevtgvPPREIRKRVPAALELVGLSHKHRALPA-----------ELSGGEQQRVAI 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 404223395 484 ARALLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHRISSVKEA--DEILILNHGEI 548
Cdd:cd03292  148 ARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTtrHRVIALERGKL 214
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
334-553 2.04e-32

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 127.61  E-value: 2.04e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFE-DDPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVREL---R 409
Cdd:PRK11153   2 IELKNISKVFPqGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELrkaR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 410 NHIATVMQDIFLFSD-TIEGNIAF-----GAPDATMEdvrrmARIAD-------ADHfIETMPESydtivgergvgLSGG 476
Cdd:PRK11153  82 RQIGMIFQHFNLLSSrTVFDNVALplelaGTPKAEIK-----ARVTEllelvglSDK-ADRYPAQ-----------LSGG 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 477 QKQRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITE--NTTTFIIAHRISSVKE-ADEILILNHGEIIERGT 553
Cdd:PRK11153 145 QKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRelGLTIVLITHEMDVVKRiCDRVAVIDAGRLVEQGT 224
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
334-548 2.44e-32

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 124.82  E-value: 2.44e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFEDDPntdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDarkwhVRELRNHIA 413
Cdd:COG1121    7 IELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKP-----PRRARRRIG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 414 TVMQDIflfsdtiegNIAFGAPdATMEDVRRMARI--------------ADADHFIET--MPESYDTIVGErgvgLSGGQ 477
Cdd:COG1121   79 YVPQRA---------EVDWDFP-ITVRDVVLMGRYgrrglfrrpsradrEAVDEALERvgLEDLADRPIGE----LSGGQ 144
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 404223395 478 KQRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKIT-ENTTTFIIAHRISSVKE-ADEILILNHGEI 548
Cdd:COG1121  145 QQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRrEGKTILVVTHDLGAVREyFDRVLLLNRGLV 217
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
337-549 3.39e-32

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


Pssm-ID: 213193 [Multi-domain]  Cd Length: 205  Bit Score: 123.14  E-value: 3.39e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 337 KNVSFHFEDdpNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDArkwHVRELRNHIATVM 416
Cdd:cd03226    3 ENISFSYKK--GTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI---KAKERRKSIGYVM 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 417 QDI--FLFSDTIEGNIAFGAPDATmedvrrmARIADADHFIETM---------PESydtivgergvgLSGGQKQRISLAR 485
Cdd:cd03226   78 QDVdyQLFTDSVREELLLGLKELD-------AGNEQAETVLKDLdlyalkerhPLS-----------LSGGQKQRLAIAA 139
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 404223395 486 ALLKNPSILILDDTTSAVD---METEVKIQGELKKitENTTTFIIAHRISSVKE-ADEILILNHGEII 549
Cdd:cd03226  140 ALLSGKDLLIFDEPTSGLDyknMERVGELIRELAA--QGKAVIVITHDYEFLAKvCDRVLLLANGAIV 205
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
334-553 1.01e-31

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


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 125.64  E-value: 1.01e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFeddPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKW-HVRElRNhI 412
Cdd:COG1118    3 IEVRNISKRF---GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNlPPRE-RR-V 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 413 ATVMQDIFLFSD-TIEGNIAFGAPDATM------EDVRRMARIADADHFIETMPESydtivgergvgLSGGQKQRISLAR 485
Cdd:COG1118   78 GFVFQHYALFPHmTVAENIAFGLRVRPPskaeirARVEELLELVQLEGLADRYPSQ-----------LSGGQRQRVALAR 146
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 404223395 486 ALLKNPSILILDDTTSAVDmeTEVK--IQGELKKITENT--TTFIIAH------RIssvkeADEILILNHGEIIERGT 553
Cdd:COG1118  147 ALAVEPEVLLLDEPFGALD--AKVRkeLRRWLRRLHDELggTTVFVTHdqeealEL-----ADRVVVMNQGRIEQVGT 217
ABC_6TM_Sav1866_like cd18554
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ...
22-290 1.30e-31

Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.


Pssm-ID: 349998 [Multi-domain]  Cd Length: 299  Bit Score: 124.45  E-value: 1.30e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  22 FILIFIASGISIIYPLLGGKVIDDVVYQNK-------TNLLIPLLLIMIISTIIRTICRYTYQIMCERIGQNSLFRIRED 94
Cdd:cd18554    5 IVIGLVRFGIPLLLPLILKYIVDDVIQGSSltldekvYKLFTIIGIMFFIFLILRPPVEYYRQYFAQWIANKILYDIRKD 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  95 LYKKLQSLDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENVFLFSFAIIIMAAIDWKLTLALVIVTPLIAILTM 174
Cdd:cd18554   85 LFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLVIFPFYILAVK 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 175 KMSSKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSRTYLPVLDSLAGMLV 254
Cdd:cd18554  165 YFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRALKHTRWNAKTFSAVNTITDLAP 244
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 404223395 255 VITLIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPMR 290
Cdd:cd18554  245 LLVIGFAAYLVIEGNLTVGTLVAFVGYMERMYSPLR 280
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
334-558 2.40e-31

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 121.74  E-value: 2.40e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFEDdpnTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDAR--KWHVRELRNH 411
Cdd:PRK09493   2 IEFKNVSKHFGP---TQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 412 IATVMQDIFLFSD-TIEGNIAFGaP----DATMEDVRRMAR--------IADADHFietmPESydtivgergvgLSGGQK 478
Cdd:PRK09493  79 AGMVFQQFYLFPHlTALENVMFG-PlrvrGASKEEAEKQARellakvglAERAHHY----PSE-----------LSGGQQ 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 479 QRISLARALLKNPSILILDDTTSAVDMET--EV-KIQGELKkiTENTTTFIIAHRISSVKE-ADEILILNHGEIIERGTH 554
Cdd:PRK09493 143 QRVAIARALAVKPKLMLFDEPTSALDPELrhEVlKVMQDLA--EEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDP 220

                 ....
gi 404223395 555 SSLL 558
Cdd:PRK09493 221 QVLI 224
PLN03130 PLN03130
ABC transporter C family member; Provisional
159-559 3.02e-31

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 129.86  E-value: 3.02e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  159 TLALVIVTPLIAILTMKMSSKAqpvfyeiRESFSRLN---SMVEENISGNRVVKAFARED-FEMKKFHEHNED---FKKR 231
Cdd:PLN03130  447 SLMLVLMFPIQTFIISKMQKLT-------KEGLQRTDkriGLMNEVLAAMDTVKCYAWENsFQSKVQTVRDDElswFRKA 519
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  232 NLDSADVSRtylpVLDSLAgmlVVITLI-FGGYLVIKGQMTLGDLVAFNGFLWMLNGPMRMSGWLINDVQRFIASSFKIQ 310
Cdd:PLN03130  520 QLLSAFNSF----ILNSIP---VLVTVVsFGVFTLLGGDLTPARAFTSLSLFAVLRFPLFMLPNLITQAVNANVSLKRLE 592
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  311 DMMATDAKI-----PIHAEKPAPSLqghvefKNVSFHFEDDPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRF 385
Cdd:PLN03130  593 ELLLAEERVllpnpPLEPGLPAISI------KNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGE 666
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  386 YDPTSGEILIdgvdarkwhvreLRNHIATVMQDIFLFSDTIEGNIAFGAP-DAtmEDVRRMARIADADHFIETMPESYDT 464
Cdd:PLN03130  667 LPPRSDASVV------------IRGTVAYVPQVSWIFNATVRDNILFGSPfDP--ERYERAIDVTALQHDLDLLPGGDLT 732
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  465 IVGERGVGLSGGQKQRISLARALLKNPSILILDDTTSAVDMET-----EVKIQGELKKITENTTTFIIaHRISSVkeaDE 539
Cdd:PLN03130  733 EIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVgrqvfDKCIKDELRGKTRVLVTNQL-HFLSQV---DR 808
                         410       420
                  ....*....|....*....|
gi 404223395  540 ILILNHGEIIERGTHSSLLA 559
Cdd:PLN03130  809 IILVHEGMIKEEGTYEELSN 828
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
334-548 4.30e-31

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: 120.33  E-value: 4.30e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFEDDPntdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDG--VDARKWHVRELRNH 411
Cdd:cd03262    1 IEIKNLHKSFGDFH---VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGlkLTDDKKNINELRQK 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 412 IATVMQDIFLFSD-TIEGNIAFG-----------APDATMEDVRRMARIADADHFIETmpesydtivgergvgLSGGQKQ 479
Cdd:cd03262   78 VGMVFQQFNLFPHlTVLENITLApikvkgmskaeAEERALELLEKVGLADKADAYPAQ---------------LSGGQQQ 142
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 404223395 480 RISLARALLKNPSILILDDTTSAVDMET--EV-KIQGELKKitENTTTFIIAHRISSVKE-ADEILILNHGEI 548
Cdd:cd03262  143 RVAIARALAMNPKVMLFDEPTSALDPELvgEVlDVMKDLAE--EGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
352-560 4.83e-31

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: 121.98  E-value: 4.83e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 352 LKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWH---VRELRNH-IATVMQDIFLFSD-TI 426
Cdd:cd03294   40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSrkeLRELRRKkISMVFQSFALLPHrTV 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 427 EGNIAFGapdatME--DVRRMARIADADHFIETMP-ESY-DTIVGErgvgLSGGQKQRISLARALLKNPSILILDDTTSA 502
Cdd:cd03294  120 LENVAFG-----LEvqGVPRAEREERAAEALELVGlEGWeHKYPDE----LSGGMQQRVGLARALAVDPDILLMDEAFSA 190
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 404223395 503 VD------METE-VKIQGELKKitenTTTFIIAHRISSVKEADEILILNHGEIIERGTHSSLLAE 560
Cdd:cd03294  191 LDplirreMQDElLRLQAELQK----TIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTN 251
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
335-559 4.91e-31

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 120.63  E-value: 4.91e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 335 EFKNVSFHFEDDPntdvlKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVD-------ARKwhvre 407
Cdd:COG3840    3 RLDDLTYRYGDFP-----LRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDltalppaERP----- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 408 lrnhIATVMQDIFLFSD-TIEGNIAFG-APDA--TMEDVRRMARIADA---DHFIETMPESydtivgergvgLSGGQKQR 480
Cdd:COG3840   73 ----VSMLFQENNLFPHlTVAQNIGLGlRPGLklTAEQRAQVEQALERvglAGLLDRLPGQ-----------LSGGQRQR 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 481 ISLARALLKNPSILILDDTTSAVD------METEVK-IQGELkkiteNTTTFIIAHRISSVKE-ADEILILNHGEIIERG 552
Cdd:COG3840  138 VALARCLVRKRPILLLDEPFSALDpalrqeMLDLVDeLCRER-----GLTVLMVTHDPEDAARiADRVLLVADGRIAADG 212

                 ....*..
gi 404223395 553 THSSLLA 559
Cdd:COG3840  213 PTAALLD 219
cbiO PRK13637
energy-coupling factor transporter ATPase;
352-560 6.86e-31

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 122.08  E-value: 6.86e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 352 LKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVD--ARKWHVRELRNHIATVMQ--DIFLFSDTIE 427
Cdd:PRK13637  23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDitDKKVKLSDIRKKVGLVFQypEYQLFEETIE 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 428 GNIAFGAPDATMEDVRRMARIADAdhfIETMPESYDTIVGERGVGLSGGQKQRISLARALLKNPSILILDDTTSAVDMET 507
Cdd:PRK13637 103 KDIAFGPINLGLSEEEIENRVKRA---MNIVGLDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKG 179
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 404223395 508 EVKIQGELKKITE--NTTTFIIAHRISSV-KEADEILILNHGEIIERGTHSSLLAE 560
Cdd:PRK13637 180 RDEILNKIKELHKeyNMTIILVSHSMEDVaKLADRIIVMNKGKCELQGTPREVFKE 235
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
334-553 1.06e-30

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: 120.14  E-value: 1.06e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFEDDPntdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRElRNhIA 413
Cdd:cd03296    3 IEVRNVSKRFGDFV---ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE-RN-VG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 414 TVMQDIFLFSD-TIEGNIAFG---------APDATMED-VRRMARIADADHFIETMPESydtivgergvgLSGGQKQRIS 482
Cdd:cd03296   78 FVFQHYALFRHmTVFDNVAFGlrvkprserPPEAEIRAkVHELLKLVQLDWLADRYPAQ-----------LSGGQRQRVA 146
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 404223395 483 LARALLKNPSILILDDTTSAVDMETEVKIQGELKKITENT--TTFIIAHRISSVKE-ADEILILNHGEIIERGT 553
Cdd:cd03296  147 LARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELhvTTVFVTHDQEEALEvADRVVVMNKGRIEQVGT 220
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
162-564 1.43e-30

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


Pssm-ID: 188098 [Multi-domain]  Cd Length: 1522  Bit Score: 127.75  E-value: 1.43e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395   162 LVIVTPLIAILTMKMSSkaqpvfYEIRESFSRLN--SMVEENISGNRVVKAFAREDFEMKKF----HEHNEDFKKRNLDS 235
Cdd:TIGR00957  467 MVLMVPLNAVMAMKTKT------YQVAHMKSKDNriKLMNEILNGIKVLKLYAWELAFLDKVegirQEELKVLKKSAYLH 540
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395   236 ADVSRTYL--PVLDSLAGMLVVITLIFGGylVIKGQMTLGDLVAFNgflwMLNGPMRMSGWLINDVQRFIASSFKIQDMM 313
Cdd:TIGR00957  541 AVGTFTWVctPFLVALITFAVYVTVDENN--ILDAEKAFVSLALFN----ILRFPLNILPMVISSIVQASVSLKRLRIFL 614
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395   314 ATDAKIPIHAE-KPAPSLQGH-VEFKNVSFHF-EDDPNTdvLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTS 390
Cdd:TIGR00957  615 SHEELEPDSIErRTIKPGEGNsITVHNATFTWaRDLPPT--LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVE 692
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395   391 GEILIDGvdarkwhvrelrnHIATVMQDIFLFSDTIEGNIAFGAP------DATMEDVrrmARIADadhfIETMPESYDT 464
Cdd:TIGR00957  693 GHVHMKG-------------SVAYVPQQAWIQNDSLRENILFGKAlnekyyQQVLEAC---ALLPD----LEILPSGDRT 752
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395   465 IVGERGVGLSGGQKQRISLARALLKNPSILILDDTTSAVD-------METEVKIQGELKkiteNTTTFIIAHRISSVKEA 537
Cdd:TIGR00957  753 EIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDahvgkhiFEHVIGPEGVLK----NKTRILVTHGISYLPQV 828
                          410       420
                   ....*....|....*....|....*..
gi 404223395   538 DEILILNHGEIIERGTHSSLLAEKGYY 564
Cdd:TIGR00957  829 DVIIVMSGGKISEMGSYQELLQRDGAF 855
PLN03232 PLN03232
ABC transporter C family member; Provisional
75-557 2.36e-30

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 127.01  E-value: 2.36e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395   75 TYQIMCE-RIGQNSL---FRIREDL----YKKLQSLDFDFFNNTRVGDIMARMTGDTDAIRHFVSwvsynILENVFLFSF 146
Cdd:PLN03232  352 TFGVLCEsQYFQNVGrvgFRLRSTLvaaiFHKSLRLTHEARKNFASGKVTNMITTDANALQQIAE-----QLHGLWSAPF 426
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  147 AIII-MAAIDWKL-------TLALVIVTPLIAILTMKMSSKAqpvfyeiRESFSRLN---SMVEENISGNRVVKAFARE- 214
Cdd:PLN03232  427 RIIVsMVLLYQQLgvaslfgSLILFLLIPLQTLIVRKMRKLT-------KEGLQWTDkrvGIINEILASMDTVKCYAWEk 499
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  215 DFEMKKFHEHNED---FKKRNLDSADVSRtylpVLDSLAgmlVVITLI-FGGYLVIKGQMTLGDLVAFNGFLWMLNGPMR 290
Cdd:PLN03232  500 SFESRIQGIRNEElswFRKAQLLSAFNSF----ILNSIP---VVVTLVsFGVFVLLGGDLTPARAFTSLSLFAVLRSPLN 572
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  291 MSGWLINDVQRFIASSFKIQDMMATDAKI-----PIHAEKPAPSLqghvefKNVSFHFEDDPNTDVLKNISLKASPGQTI 365
Cdd:PLN03232  573 MLPNLLSQVVNANVSLQRIEELLLSEERIlaqnpPLQPGAPAISI------KNGYFSWDSKTSKPTLSDINLEIPVGSLV 646
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  366 AILGETGAGKSTLVNLICRFYDPTSGEILIdgvdarkwhvreLRNHIATVMQDIFLFSDTIEGNIAFGApDATMEDVRRM 445
Cdd:PLN03232  647 AIVGGTGEGKTSLISAMLGELSHAETSSVV------------IRGSVAYVPQVSWIFNATVRENILFGS-DFESERYWRA 713
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  446 ARIADADHFIETMPESYDTIVGERGVGLSGGQKQRISLARALLKNPSILILDDTTSAVDMETEVKI-QGELKKITENTTT 524
Cdd:PLN03232  714 IDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVfDSCMKDELKGKTR 793
                         490       500       510
                  ....*....|....*....|....*....|...
gi 404223395  525 FIIAHRISSVKEADEILILNHGEIIERGTHSSL 557
Cdd:PLN03232  794 VLVTNQLHFLPLMDRIILVSEGMIKEEGTFAEL 826
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
107-564 3.56e-30

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


Pssm-ID: 273530 [Multi-domain]  Cd Length: 1490  Bit Score: 126.56  E-value: 3.56e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395   107 FNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENVFLFSFAIIIMAAIDWKLTLALVIVTPLIAILTMKMSSKAQPVFYE 186
Cdd:TIGR01271  976 LNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGAIFVVSVLQPYIFIAAIPVAVIFIMLRAYFLRTSQQLKQL 1055
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395   187 IRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHehnedfKKRNLDSADvsrtYLPVLDSLAGMLVVITLIF------ 260
Cdd:TIGR01271 1056 ESEARSPIFSHLITSLKGLWTIRAFGRQSYFETLFH------KALNLHTAN----WFLYLSTLRWFQMRIDIIFvfffia 1125
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395   261 ------GGYLVIKGQMTLGDLVAFN---GFLWMLNGPMRMSGWL--INDVQRFI------------ASSFKIQDMMATDA 317
Cdd:TIGR01271 1126 vtfiaiGTNQDGEGEVGIILTLAMNilsTLQWAVNSSIDVDGLMrsVSRVFKFIdlpqeeprpsggGGKYQLSTVLVIEN 1205
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395   318 KipiHAEKPAPSlQGHVEFKNVSFHFEDDPNTdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDpTSGEILIDG 397
Cdd:TIGR01271 1206 P---HAQKCWPS-GGQMDVQGLTAKYTEAGRA-VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDG 1279
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395   398 VDARKWHVRELRNHIATVMQDIFLFSDTIEGNIAfgaPDA--TMEDVRRMARIADADHFIETMPESYDTIVGERGVGLSG 475
Cdd:TIGR01271 1280 VSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLD---PYEqwSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSN 1356
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395   476 GQKQRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHRISSVKEADEILILNHGEIIERGTHS 555
Cdd:TIGR01271 1357 GHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQ 1436

                   ....*....
gi 404223395   556 SLLAEKGYY 564
Cdd:TIGR01271 1437 KLLNETSLF 1445
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
334-552 4.62e-30

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


Pssm-ID: 213231 [Multi-domain]  Cd Length: 211  Bit Score: 117.29  E-value: 4.62e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFeddPNTDVLKNISLKASPGQTiAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKwHVRELRNHIA 413
Cdd:cd03264    1 LQLENLTKRY---GKKRALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 414 TVMQDIFLFSD-TIEGNIAFGAPDATMEDVRRMARIadaDHFIE--TMPESYDTIVGergvGLSGGQKQRISLARALLKN 490
Cdd:cd03264   76 YLPQEFGVYPNfTVREFLDYIAWLKGIPSKEVKARV---DEVLElvNLGDRAKKKIG----SLSGGMRRRVGIAQALVGD 148
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 404223395 491 PSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHRISSVKE-ADEILILNHGEIIERG 552
Cdd:cd03264  149 PSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
ABC_6TM_ABCB10_like cd18573
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ...
22-278 7.80e-30

Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.


Pssm-ID: 350017 [Multi-domain]  Cd Length: 294  Bit Score: 119.16  E-value: 7.80e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  22 FILIFIASGISIIYPLLGGKVIDdVVYQNKTNLLIPLLLIMIISTI------IRTICRYTYQIMCERIGQNSLFRIREDL 95
Cdd:cd18573    2 LALLLVSSAVTMSVPFAIGKLID-VASKESGDIEIFGLSLKTFALAllgvfvVGAAANFGRVYLLRIAGERIVARLRKRL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  96 YKKLQSLDFDFFNNTRVGDIMARMTGDTDAI-RHFVSWVSyNILENVFLFSFAIIIMAAIDWKLTLALVIVTPLIAILTM 174
Cdd:cd18573   81 FKSILRQDAAFFDKNKTGELVSRLSSDTSVVgKSLTQNLS-DGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 175 KMSSKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSRTYLPVLdSLAGMLV 254
Cdd:cd18573  160 FYGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGST-GFSGNLS 238
                        250       260
                 ....*....|....*....|....*
gi 404223395 255 VIT-LIFGGYLVIKGQMTLGDLVAF 278
Cdd:cd18573  239 LLSvLYYGGSLVASGELTVGDLTSF 263
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
332-564 8.10e-30

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


Pssm-ID: 213256 [Multi-domain]  Cd Length: 275  Bit Score: 118.42  E-value: 8.10e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 332 GHVEFKNVSFHFEDDPNTdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDpTSGEILIDGVDARKWHVRELRNH 411
Cdd:cd03289    1 GQMTVKDLTAKYTEGGNA-VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 412 IATVMQDIFLFSDTIEGNI-AFGApdATMEDVRRMARIADADHFIETMPESYDTIVGERGVGLSGGQKQRISLARALLKN 490
Cdd:cd03289   79 FGVIPQKVFIFSGTFRKNLdPYGK--WSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSK 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 404223395 491 PSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHRISSVKEADEILILNHGEIIERGTHSSLLAEKGYY 564
Cdd:cd03289  157 AKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHF 230
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
334-550 9.56e-30

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 122.82  E-value: 9.56e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFeddPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNH-I 412
Cdd:COG1129    5 LEMRGISKSF---GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAgI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 413 ATVMQDIFLFSD-TIEGNIAFGAPDATMEDVRRMARIADADHFIETM--PESYDTIVGErgvgLSGGQKQRISLARALLK 489
Cdd:COG1129   82 AIIHQELNLVPNlSVAENIFLGREPRRGGLIDWRAMRRRARELLARLglDIDPDTPVGD----LSVAQQQLVEIARALSR 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 404223395 490 NPSILILDDTTSAVDmETEV----KIQGELKKitENTTTFIIAHRISSVKE-ADEILILNHGEIIE 550
Cdd:COG1129  158 DARVLILDEPTASLT-EREVerlfRIIRRLKA--QGVAIIYISHRLDEVFEiADRVTVLRDGRLVG 220
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
334-553 2.61e-29

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 119.67  E-value: 2.61e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFEDdpnTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARkwHVRELRNHIA 413
Cdd:PRK09452  15 VELRGISKSFDG---KEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT--HVPAENRHVN 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 414 TVMQDIFLFSD-TIEGNIAFG-----APDATME----DVRRMARIadaDHFIETMPESydtivgergvgLSGGQKQRISL 483
Cdd:PRK09452  90 TVFQSYALFPHmTVFENVAFGlrmqkTPAAEITprvmEALRMVQL---EEFAQRKPHQ-----------LSGGQQQRVAI 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 404223395 484 ARALLKNPSILILDDTTSAVDMETEVKIQGELKKITENT-TTFI-IAHrisSVKEA----DEILILNHGEIIERGT 553
Cdd:PRK09452 156 ARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLgITFVfVTH---DQEEAltmsDRIVVMRDGRIEQDGT 228
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
334-552 4.02e-29

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


Pssm-ID: 213180 [Multi-domain]  Cd Length: 194  Bit Score: 114.19  E-value: 4.02e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSF---HFEDDPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLIC--RFYDPTSGEILIDGVDARKwhvREL 408
Cdd:cd03213    4 LSFRNLTVtvkSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPLDK---RSF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 409 RNHIATVMQ-DIFLFSDTIEGNIAFGApdatmeDVRrmariadadhfietmpesydtivgergvGLSGGQKQRISLARAL 487
Cdd:cd03213   81 RKIIGYVPQdDILHPTLTVRETLMFAA------KLR----------------------------GLSGGERKRVSIALEL 126
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 404223395 488 LKNPSILILDDTTSAVDMETEVKIQGELKKIT-ENTTTFIIAHRISS--VKEADEILILNHGEIIERG 552
Cdd:cd03213  127 VSNPSLLFLDEPTSGLDSSSALQVMSLLRRLAdTGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
334-553 6.28e-29

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


Pssm-ID: 440213 [Multi-domain]  Cd Length: 320  Bit Score: 117.08  E-value: 6.28e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFEDDPNT-DVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDP---TSGEILIDGVDARKWHVRELR 409
Cdd:COG0444    2 LEVRNLKVYFPTRRGVvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 410 ----NHIATVMQD-----------IFLFSDTIEgnIAFGAPDAtmeDVRRMAR-------IADADHFIETMP-Esydtiv 466
Cdd:COG0444   82 kirgREIQMIFQDpmtslnpvmtvGDQIAEPLR--IHGGLSKA---EARERAIellervgLPDPERRLDRYPhE------ 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 467 gergvgLSGGQKQRISLARALLKNPSILILDDTTSAVDmeteVKIQGE----LKKITE--NTTTFIIAHRISSVKE-ADE 539
Cdd:COG0444  151 ------LSGGMRQRVMIARALALEPKLLIADEPTTALD----VTIQAQilnlLKDLQRelGLAILFITHDLGVVAEiADR 220
                        250
                 ....*....|....
gi 404223395 540 ILILNHGEIIERGT 553
Cdd:COG0444  221 VAVMYAGRIVEEGP 234
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
334-549 1.11e-28

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


Pssm-ID: 213183 [Multi-domain]  Cd Length: 163  Bit Score: 111.75  E-value: 1.11e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFeddPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNH-I 412
Cdd:cd03216    1 LELRGITKRF---GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAgI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 413 ATVMQdiflfsdtiegniafgapdatmedvrrmariadadhfietmpesydtivgergvgLSGGQKQRISLARALLKNPS 492
Cdd:cd03216   78 AMVYQ-------------------------------------------------------LSVGERQMVEIARALARNAR 102
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 493 ILILDDTTSAV-DMETEvKIQGELKKITENTTTFI-IAHRISSVKE-ADEILILNHGEII 549
Cdd:cd03216  103 LLILDEPTAALtPAEVE-RLFKVIRRLRAQGVAVIfISHRLDEVFEiADRVTVLRDGRVV 161
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
352-552 1.28e-28

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


Pssm-ID: 213264 [Multi-domain]  Cd Length: 214  Bit Score: 113.16  E-value: 1.28e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 352 LKNISLKAS---PGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGV---DARK-WHVRELRNHIATVMQDIFLFSD 424
Cdd:cd03297   10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfDSRKkINLPPQQRKIGLVFQQYALFPH 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 425 -TIEGNIAFGAP-DATMEDVRRMARIADADHFietmpesyDTIVGERGVGLSGGQKQRISLARALLKNPSILILDDTTSA 502
Cdd:cd03297   90 lNVRENLAFGLKrKRNREDRISVDELLDLLGL--------DHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSA 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 404223395 503 VDMETEVKIQGELKKITE--NTTTFIIAHRISSV-KEADEILILNHGEIIERG 552
Cdd:cd03297  162 LDRALRLQLLPELKQIKKnlNIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
PTZ00243 PTZ00243
ABC transporter; Provisional
72-553 2.18e-28

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 121.04  E-value: 2.18e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395   72 CRYTYQIMceRIGQNSLFRireDLYKKLQSLDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENVFLFSFAIIIM 151
Cdd:PTZ00243 1019 FFLSYEAM--RRGSRNMHR---DLLRSVSRGTMSFFDTTPLGRILNRFSRDIDILDNTLPMSYLYLLQCLFSICSSILVT 1093
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  152 AAIDWKLTLALVIVTPLIAILTMKMSSKAQpvfyEIRESFSRLNS----MVEENISGNRVVKAFAREDFEMKK-FHEHNE 226
Cdd:PTZ00243 1094 SASQPFVLVALVPCGYLYYRLMQFYNSANR----EIRRIKSVAKSpvftLLEEALQGSATITAYGKAHLVMQEaLRRLDV 1169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  227 DFKKRNLDsaDVSRTYLPVLDSLAGMLVVITLIFGGylvIKGQMTLGD-----LVAFNGFLWM-----LNGPMRMSGWL- 295
Cdd:PTZ00243 1170 VYSCSYLE--NVANRWLGVRVEFLSNIVVTVIALIG---VIGTMLRATsqeigLVSLSLTMAMqttatLNWLVRQVATVe 1244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  296 --INDVQRFIASSFKI--QDMMATDAKI--------------------PIHAEKPAP-SLQ-GHVEFKNVSFHFEDD-PN 348
Cdd:PTZ00243 1245 adMNSVERLLYYTDEVphEDMPELDEEVdalerrtgmaadvtgtvviePASPTSAAPhPVQaGSLVFEGVQMRYREGlPL 1324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  349 tdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIATVMQDIFLFSDTIEG 428
Cdd:PTZ00243 1325 --VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQ 1402
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  429 NIafgAP--DATMEDVRRMARIADADHFIETMPESYDTIVGERGVGLSGGQKQRISLARALLKNPSILIL-DDTTSAVDM 505
Cdd:PTZ00243 1403 NV---DPflEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSGFILmDEATANIDP 1479
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 404223395  506 ETEVKIQGELKKITENTTTFIIAHRISSVKEADEILILNHGEIIERGT 553
Cdd:PTZ00243 1480 ALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGS 1527
ABC_6TM_bac_exporter_ABCB8_10_like cd18575
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ...
82-278 2.95e-28

Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.


Pssm-ID: 350019 [Multi-domain]  Cd Length: 289  Bit Score: 114.50  E-value: 2.95e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  82 RIGQNSLFRIREDLYKKLQSLDFDFFNNTRVGDIMARMTGDTDAIRHFV-SWVSYnILENVFLFSFAIIIMAAIDWKLTL 160
Cdd:cd18575   62 WLGERVVADLRKAVFAHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVgSSLSI-ALRNLLLLIGGLVMLFITSPKLTL 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 161 ALVIVTPLIAILTM-------KMSSKAQpvfyeirESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEdfkkrnl 233
Cdd:cd18575  141 LVLLVIPLVVLPIIlfgrrvrRLSRASQ-------DRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVE------- 206
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 404223395 234 DSADVSRTYLPVLDSLAGmlVVITLIF---------GGYLVIKGQMTLGDLVAF 278
Cdd:cd18575  207 AAFAAALRRIRARALLTA--LVIFLVFgaivfvlwlGAHDVLAGRMSAGELSQF 258
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
351-553 4.79e-28

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


Pssm-ID: 213186 [Multi-domain]  Cd Length: 236  Bit Score: 112.53  E-value: 4.79e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 351 VLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNH-IATVMQDIFLFSD-TIEG 428
Cdd:cd03219   15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLgIGRTFQIPRLFPElTVLE 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 429 NIAFGAPDATME------DVRRMARIAD-ADHFIETM--PESYDTIVGErgvgLSGGQKQRISLARALLKNPSILILDDT 499
Cdd:cd03219   95 NVMVAAQARTGSglllarARREEREARErAEELLERVglADLADRPAGE----LSYGQQRRLEIARALATDPKLLLLDEP 170
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 404223395 500 TSAVDMETEVKIQGELKKITENTTTF-IIAHRISSVKE-ADEILILNHGEIIERGT 553
Cdd:cd03219  171 AAGLNPEETEELAELIRELRERGITVlLVEHDMDVVMSlADRVTVLDQGRVIAEGT 226
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
334-553 4.97e-28

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 113.63  E-value: 4.97e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFEDDpnTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDG--VDARKWHVRELRNH 411
Cdd:PRK13639   2 LETRDLKYSYPDG--TEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepIKYDKKSLLEVRKT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 412 IATVMQ--DIFLFSDTIEGNIAFGAPDA--TMEDVRRmaRIADA------DHFIETMPESydtivgergvgLSGGQKQRI 481
Cdd:PRK13639  80 VGIVFQnpDDQLFAPTVEEDVAFGPLNLglSKEEVEK--RVKEAlkavgmEGFENKPPHH-----------LSGGQKKRV 146
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 404223395 482 SLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIA-HRISSV-KEADEILILNHGEIIERGT 553
Cdd:PRK13639 147 AIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIIStHDVDLVpVYADKVYVMSDGKIIKEGT 220
SapF COG4167
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
335-559 9.87e-28

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


Pssm-ID: 443328 [Multi-domain]  Cd Length: 265  Bit Score: 112.24  E-value: 9.87e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 335 EFKNVSFHFED------DPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVREL 408
Cdd:COG4167    6 EVRNLSKTFKYrtglfrRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKYR 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 409 RNHIATVMQDIflfSDTIEGNIAFG----AP---DATMEDVRRMARIadadhfIETMpesydtivgeRGVGL-------- 473
Cdd:COG4167   86 CKHIRMIFQDP---NTSLNPRLNIGqileEPlrlNTDLTAEEREERI------FATL----------RLVGLlpehanfy 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 474 ----SGGQKQRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITENT-TTFI-IAHRISSVKE-ADEILILNHG 546
Cdd:COG4167  147 phmlSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLgISYIyVSQHLGIVKHiSDKVLVMHQG 226
                        250
                 ....*....|...
gi 404223395 547 EIIERGTHSSLLA 559
Cdd:COG4167  227 EVVEYGKTAEVFA 239
cbiO PRK13650
energy-coupling factor transporter ATPase;
334-548 1.88e-27

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 111.75  E-value: 1.88e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFEDDPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIA 413
Cdd:PRK13650   5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 414 TVMQ--DIFLFSDTIEGNIAFGAPDATMEDVRRMARIADADHFIETMpeSYDTIVGERgvgLSGGQKQRISLARALLKNP 491
Cdd:PRK13650  85 MVFQnpDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQ--DFKEREPAR---LSGGQKQRVAIAGAVAMRP 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 404223395 492 SILILDDTTSAVDMETEVKIQGELKKITE--NTTTFIIAHRISSVKEADEILILNHGEI 548
Cdd:PRK13650 160 KIIILDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQV 218
ABC_6TM_ABCB9_like cd18784
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ...
22-278 1.91e-27

Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit.


Pssm-ID: 350057 [Multi-domain]  Cd Length: 289  Bit Score: 112.02  E-value: 1.91e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  22 FILIFIASGISIIYPLLGGKVIDDVVYQNKTNLLIPLLLIMIISTIIRTICR----YTYQIMCERIGqnslFRIREDLYK 97
Cdd:cd18784    2 FFFLLAAAVGEIFIPYYTGQVIDGIVIEKSQDKFSRAIIIMGLLAIASSVAAgirgGLFTLAMARLN----IRIRNLLFR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  98 KLQSLDFDFFNNTRVGDIMARMTGDTDAIrhfVSWVSYNIleNVFLFSF-----AIIIMAAIDWKLTLALVIVTPLIAIL 172
Cdd:cd18784   78 SIVSQEIGFFDTVKTGDITSRLTSDTTTM---SDTVSLNL--NIFLRSLvkaigVIVFMFKLSWQLSLVTLIGLPLIAIV 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 173 T-------MKMSSKAQpvfyeirESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSRTYLPV 245
Cdd:cd18784  153 SkvygdyyKKLSKAVQ-------DSLAKANEVAEETISSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEALAYGGYVWS 225
                        250       260       270
                 ....*....|....*....|....*....|...
gi 404223395 246 LDSLAGMLVVITLIFGGYLVIKGQMTLGDLVAF 278
Cdd:cd18784  226 NELTELALTVSTLYYGGHLVITGQISGGNLISF 258
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
336-576 3.74e-27

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


Pssm-ID: 273530 [Multi-domain]  Cd Length: 1490  Bit Score: 117.32  E-value: 3.74e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395   336 FKNVSFHFeddpnTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGvdarkwhvrelrnHIATV 415
Cdd:TIGR01271  431 FSNFSLYV-----TPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFS 492
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395   416 MQDIFLFSDTIEGNIAFGApdaTMEDVRRMARI--ADADHFIETMPESYDTIVGERGVGLSGGQKQRISLARALLKNPSI 493
Cdd:TIGR01271  493 PQTSWIMPGTIKDNIIFGL---SYDEYRYTSVIkaCQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADL 569
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395   494 LILDDTTSAVDMETEVKI-QGELKKITENTTTFIIAHRISSVKEADEILILNHGEIIERGTHSSLLAEKGyyfDIYNKQL 572
Cdd:TIGR01271  570 YLLDSPFTHLDVVTEKEIfESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRP---DFSSLLL 646

                   ....
gi 404223395   573 GTEA 576
Cdd:TIGR01271  647 GLEA 650
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
334-553 4.50e-27

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 110.88  E-value: 4.50e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFEDDpNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIA 413
Cdd:PRK13635   6 IRVEHISFRYPDA-ATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 414 TVMQ--DIFLFSDTIEGNIAFGAPDATMEDVRRMARIADADH------FIETMPESydtivgergvgLSGGQKQRISLAR 485
Cdd:PRK13635  85 MVFQnpDNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRqvgmedFLNREPHR-----------LSGGQKQRVAIAG 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 486 ALLKNPSILILDDTTSAVDMETEVKIQGELKKITENT--TTFIIAHRISSVKEADEILILNHGEIIERGT 553
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKgiTVLSITHDLDEAAQADRVIVMNKGEILEEGT 223
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
319-552 9.98e-27

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 112.24  E-value: 9.98e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 319 IPIHAEKPAPSLQGHVEFKNVSFHFEDDPNTDvlkNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGV 398
Cdd:PRK11607   5 IPRPQAKTRKALTPLLEIRNLTKSFDGQHAVD---DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 399 DARkwHVRELRNHIATVMQDIFLFSD-TIEGNIAFG-----APDATMED-VRRMARIADADHFIETMPESydtivgergv 471
Cdd:PRK11607  82 DLS--HVPPYQRPINMMFQSYALFPHmTVEQNIAFGlkqdkLPKAEIASrVNEMLGLVHMQEFAKRKPHQ---------- 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 472 gLSGGQKQRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITE--NTTTFIIAH-RISSVKEADEILILNHGEI 548
Cdd:PRK11607 150 -LSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILErvGVTCVMVTHdQEEAMTMAGRIAIMNRGKF 228

                 ....
gi 404223395 549 IERG 552
Cdd:PRK11607 229 VQIG 232
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
327-561 1.11e-26

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


Pssm-ID: 213258 [Multi-domain]  Cd Length: 282  Bit Score: 109.95  E-value: 1.11e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 327 APSLQGHVEFKNVSFHfeddpNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGvdarkwhvr 406
Cdd:cd03291   33 HSSDDNNLFFSNLCLV-----GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG--------- 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 407 elrnHIATVMQDIFLFSDTIEGNIAFGApdaTMEDVRRMARI--ADADHFIETMPESYDTIVGERGVGLSGGQKQRISLA 484
Cdd:cd03291   99 ----RISFSSQFSWIMPGTIKENIIFGV---SYDEYRYKSVVkaCQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLA 171
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 404223395 485 RALLKNPSILILDDTTSAVDMETEVKI-QGELKKITENTTTFIIAHRISSVKEADEILILNHGEIIERGTHSSLLAEK 561
Cdd:cd03291  172 RAVYKDADLYLLDSPFGYLDVFTEKEIfESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLR 249
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
334-553 3.36e-26

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 110.17  E-value: 3.36e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFEddpNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRElrNHIA 413
Cdd:PRK10851   3 IEIANIKKSFG---RTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD--RKVG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 414 TVMQDIFLFSD-TIEGNIAFG--------APDATM--EDVRRMARIADADHFIETMPESydtivgergvgLSGGQKQRIS 482
Cdd:PRK10851  78 FVFQHYALFRHmTVFDNIAFGltvlprreRPNAAAikAKVTQLLEMVQLAHLADRYPAQ-----------LSGGQKQRVA 146
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 404223395 483 LARALLKNPSILILDDTTSAVDMETEVKIQGELKKITEN---TTTFIIAHRISSVKEADEILILNHGEIIERGT 553
Cdd:PRK10851 147 LARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEElkfTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGT 220
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
352-553 4.76e-26

Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213232 [Multi-domain]  Cd Length: 220  Bit Score: 106.30  E-value: 4.76e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 352 LKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKwHVRELRNHIATVMQDIFLfSDTIEG--N 429
Cdd:cd03265   16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLSV-DDELTGweN 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 430 IAFGAPDATMEDVRRMARIADADHFIETMpESYDTIVGErgvgLSGGQKQRISLARALLKNPSILILDDTTSAVDMETEV 509
Cdd:cd03265   94 LYIHARLYGVPGAERRERIDELLDFVGLL-EAADRLVKT----YSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRA 168
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 404223395 510 KIQGELKKI--TENTTTFIIAHRISSVKE-ADEILILNHGEIIERGT 553
Cdd:cd03265  169 HVWEYIEKLkeEFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGT 215
nickel_nikE TIGR02769
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ...
351-550 5.03e-26

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


Pssm-ID: 131816 [Multi-domain]  Cd Length: 265  Bit Score: 107.58  E-value: 5.03e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  351 VLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKW---HVRELRNHIATVMQD---IFLFSD 424
Cdd:TIGR02769  26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLdrkQRRAFRRDVQLVFQDspsAVNPRM 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  425 TIEGNIafGAPDATMEDVRRMARIADADHFIETMpESYDTIVGERGVGLSGGQKQRISLARALLKNPSILILDDTTSAVD 504
Cdd:TIGR02769 106 TVRQII--GEPLRHLTSLDESEQKARIAELLDMV-GLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLD 182
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 404223395  505 METEVKIQGELKKITE--NTTTFIIAHRISSVKE-ADEILILNHGEIIE 550
Cdd:TIGR02769 183 MVLQAVILELLRKLQQafGTAYLFITHDLRLVQSfCQRVAVMDKGQIVE 231
TauB COG4525
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
333-551 6.58e-26

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


Pssm-ID: 443596 [Multi-domain]  Cd Length: 262  Bit Score: 106.87  E-value: 6.58e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 333 HVEFKNVSFHFE-DDPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGV-----DARKwhvr 406
Cdd:COG4525    3 MLTVRHVSVRYPgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVpvtgpGADR---- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 407 elrnhiATVMQDIFLFS--DTIEgNIAFGApdaTMEDVRRMARIADADHFIEtmpesydtIVGERGVG------LSGGQK 478
Cdd:COG4525   79 ------GVVFQKDALLPwlNVLD-NVAFGL---RLRGVPKAERRARAEELLA--------LVGLADFArrriwqLSGGMR 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 479 QRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKI--TENTTTFIIAHrisSVKEA----DEILIL--NHGEIIE 550
Cdd:COG4525  141 QRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVwqRTGKGVFLITH---SVEEAlflaTRLVVMspGPGRIVE 217

                 .
gi 404223395 551 R 551
Cdd:COG4525  218 R 218
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
334-553 1.18e-25

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 106.37  E-value: 1.18e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFEDDPNTdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIA 413
Cdd:PRK13648   8 IVFKNVSFQYQSDASF-TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 414 TVMQDI---FLFSdTIEGNIAFG-----APDATM--------EDVRRMARiadADHfietMPESydtivgergvgLSGGQ 477
Cdd:PRK13648  87 IVFQNPdnqFVGS-IVKYDVAFGlenhaVPYDEMhrrvsealKQVDMLER---ADY----EPNA-----------LSGGQ 147
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 404223395 478 KQRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITE--NTTTFIIAHRISSVKEADEILILNHGEIIERGT 553
Cdd:PRK13648 148 KQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSehNITIISITHDLSEAMEADHVIVMNKGTVYKEGT 225
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
334-558 1.37e-25

ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];


Pssm-ID: 440736 [Multi-domain]  Cd Length: 250  Bit Score: 105.94  E-value: 1.37e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFEDdpnTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSG-EILIDGVDARKWHVRELRNHI 412
Cdd:COG1119    4 LELRNVTVRRGG---KTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKRI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 413 ATV---MQDIFLFSDTIE--------GNIA-FGAPDATMED-VRRMARIADADHFIETmpeSYDTivgergvgLSGGQKQ 479
Cdd:COG1119   81 GLVspaLQLRFPRDETVLdvvlsgffDSIGlYREPTDEQRErARELLELLGLAHLADR---PFGT--------LSQGEQR 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 480 RISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFII--AHRISSVKEA-DEILILNHGEIIERGTHSS 556
Cdd:COG1119  150 RVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVlvTHHVEEIPPGiTHVLLLKDGRVVAAGPKEE 229

                 ..
gi 404223395 557 LL 558
Cdd:COG1119  230 VL 231
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
352-558 1.63e-25

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


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 108.97  E-value: 1.63e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 352 LKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVREL----RNHIATVMQDIFLFSD-TI 426
Cdd:PRK10070  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELrevrRKKIAMVFQSFALMPHmTV 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 427 EGNIAFGAPDATMEDVRRMARIADA------DHFIETMPESydtivgergvgLSGGQKQRISLARALLKNPSILILDDTT 500
Cdd:PRK10070 124 LDNTAFGMELAGINAEERREKALDAlrqvglENYAHSYPDE-----------LSGGMRQRVGLARALAINPDILLMDEAF 192
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 404223395 501 SAVDMETEVKIQGELKKIT---ENTTTFIIAHRISSVKEADEILILNHGEIIERGTHSSLL 558
Cdd:PRK10070 193 SALDPLIRTEMQDELVKLQakhQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
351-549 4.85e-25

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


Pssm-ID: 440718 [Multi-domain]  Cd Length: 264  Bit Score: 104.40  E-value: 4.85e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 351 VLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKW--HVRElrNHIATVMQDIFL---FSDT 425
Cdd:COG1101   21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLpeYKRA--KYIGRVFQDPMMgtaPSMT 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 426 IEGNIAFgapdATMEDVRRMARIA----DADHFIET-------MPESYDTIVGErgvgLSGGQKQRISLARALLKNPSIL 494
Cdd:COG1101   99 IEENLAL----AYRRGKRRGLRRGltkkRRELFRELlatlglgLENRLDTKVGL----LSGGQRQALSLLMATLTKPKLL 170
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 404223395 495 ILDDTTSAVD-------METEVKIQGElkkitENTTTFIIAHrisSVKEA----DEILILNHGEII 549
Cdd:COG1101  171 LLDEHTAALDpktaalvLELTEKIVEE-----NNLTTLMVTH---NMEQAldygNRLIMMHEGRII 228
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
334-553 8.83e-25

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


Pssm-ID: 213230 [Multi-domain]  Cd Length: 220  Bit Score: 102.58  E-value: 8.83e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFEDDPNTdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKwHVRELRNHIA 413
Cdd:cd03263    1 LQIRNLTKTYKKGTKP-AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 414 TVMQDIFLFSD-TIEGNIAFGAPdatMEDVRRMARIADADHFIETM-PESY-DTIVGErgvgLSGGQKQRISLARALLKN 490
Cdd:cd03263   79 YCPQFDALFDElTVREHLRFYAR---LKGLPKSEIKEEVELLLRVLgLTDKaNKRART----LSGGMKRKLSLAIALIGG 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 404223395 491 PSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHrisSVKEA----DEILILNHGEIIERGT 553
Cdd:cd03263  152 PSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTH---SMDEAealcDRIAIMSDGKLRCIGS 215
cbiO PRK13640
energy-coupling factor transporter ATPase;
334-553 1.08e-24

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 104.11  E-value: 1.08e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFEDDPNTdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGE---ILIDGVDARKWHVRELRN 410
Cdd:PRK13640   6 VEFKHVSFTYPDSKKP-ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAKTVWDIRE 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 411 HIATVMQ--DIFLFSDTIEGNIAFG-----APDATMED-VRRMARIADADHFIETMPESydtivgergvgLSGGQKQRIS 482
Cdd:PRK13640  85 KVGIVFQnpDNQFVGATVGDDVAFGlenraVPRPEMIKiVRDVLADVGMLDYIDSEPAN-----------LSGGQKQRVA 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 404223395 483 LARALLKNPSILILDDTTSAVDMETEVKIQGELKKITE--NTTTFIIAHRISSVKEADEILILNHGEIIERGT 553
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGS 226
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
324-552 1.09e-24

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


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 103.19  E-value: 1.09e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 324 EKPAPSLQGHVEFKNVSFHFEDDPntdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYD--P---TSGEILIDGV 398
Cdd:COG1117    2 TAPASTLEPKIEVRNLNVYYGDKQ---ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPgarVEGEILLDGE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 399 D--ARKWHVRELRNHIATVMQDIFLFSDTIEGNIAFGAP----------DATMEDVRRMARIADadhfietmpESYDTIv 466
Cdd:COG1117   79 DiyDPDVDVVELRRRVGMVFQKPNPFPKSIYDNVAYGLRlhgikskselDEIVEESLRKAALWD---------EVKDRL- 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 467 GERGVGLSGGQKQRISLARALLKNPSILILDDTTSAVD-METEvKIQ---GELKKiteNTTTFIIAH------RISsvke 536
Cdd:COG1117  149 KKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDpISTA-KIEeliLELKK---DYTIVIVTHnmqqaaRVS---- 220
                        250
                 ....*....|....*.
gi 404223395 537 aDEILILNHGEIIERG 552
Cdd:COG1117  221 -DYTAFFYLGELVEFG 235
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
342-546 1.53e-24

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


Pssm-ID: 213257 [Multi-domain]  Cd Length: 218  Bit Score: 102.02  E-value: 1.53e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 342 HFEDDPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGV--DARKWHVRELRNH--IATVMQ 417
Cdd:cd03290    7 YFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKneSEPSFEATRSRNRysVAYAAQ 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 418 DIFLFSDTIEGNIAFGAPdatmEDVRRMARIADADHF---IETMPESYDTIVGERGVGLSGGQKQRISLARALLKNPSIL 494
Cdd:cd03290   87 KPWLLNATVEENITFGSP----FNKQRYKAVTDACSLqpdIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIV 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 404223395 495 ILDDTTSAVD--METEVKIQGELKKITENTTTFI-IAHRISSVKEADEILILNHG 546
Cdd:cd03290  163 FLDDPFSALDihLSDHLMQEGILKFLQDDKRTLVlVTHKLQYLPHADWIIAMKDG 217
cbiO PRK13646
energy-coupling factor transporter ATPase;
334-563 2.16e-24

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 103.32  E-value: 2.16e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFEDDP--NTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVD----ARKWHVRE 407
Cdd:PRK13646   3 IRFDNVSYTYQKGTpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITithkTKDKYIRP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 408 LRNHIATVMQ--DIFLFSDTIEGNIAFGAPDATM--EDVRrmariADADHFIETMPESYDtIVGERGVGLSGGQKQRISL 483
Cdd:PRK13646  83 VRKRIGMVFQfpESQLFEDTVEREIIFGPKNFKMnlDEVK-----NYAHRLLMDLGFSRD-VMSQSPFQMSGGQMRKIAI 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 484 ARALLKNPSILILDDTTSAVDMETEVKIQGELKKIT--ENTTTFIIAHRISSV-KEADEILILNHGEIIERGTHSSLLAE 560
Cdd:PRK13646 157 VSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFKD 236

                 ...
gi 404223395 561 KGY 563
Cdd:PRK13646 237 KKK 239
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
362-552 2.64e-24

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


Pssm-ID: 213265 [Multi-domain]  Cd Length: 211  Bit Score: 101.03  E-value: 2.64e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 362 GQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARkwHVRELRNHIATVMQDIFLFSD-TIEGNIAFG-APD--A 437
Cdd:cd03298   24 GEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVT--AAPPADRPVSMLFQENNLFAHlTVEQNVGLGlSPGlkL 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 438 TMEDVRRMARIA---DADHFIETMPESydtivgergvgLSGGQKQRISLARALLKNPSILILDDTTSAVDMETEVKIQGE 514
Cdd:cd03298  102 TAEDRQAIEVALarvGLAGLEKRLPGE-----------LSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDL 170
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 404223395 515 LKKITENT--TTFIIAHRISSVKE-ADEILILNHGEIIERG 552
Cdd:cd03298  171 VLDLHAETkmTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
349-560 2.90e-24

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


Pssm-ID: 213191 [Multi-domain]  Cd Length: 222  Bit Score: 100.97  E-value: 2.90e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 349 TDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKW--HVReLRNHIATVMQDIFLFSD-T 425
Cdd:cd03224   13 SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLppHER-ARAGIGYVPEGRRIFPElT 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 426 IEGNIAFGApdatmeDVRRMARIAdadhfiETMPESYDT--IVGER----GVGLSGGQKQRISLARALLKNPSILILDDT 499
Cdd:cd03224   92 VEENLLLGA------YARRRAKRK------ARLERVYELfpRLKERrkqlAGTLSGGEQQMLAIARALMSRPKLLLLDEP 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 404223395 500 T-----SAVDmetevKIQGELKKI-TENTTTFIIAHRISSVKE-ADEILILNHGEIIERGTHSSLLAE 560
Cdd:cd03224  160 SeglapKIVE-----EIFEAIRELrDEGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLAD 222
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
334-560 2.93e-24

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 102.14  E-value: 2.93e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFEDDpntDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSG-----EILIDG---VDARKWHV 405
Cdd:PRK11264   4 IEVKNLVKKFHGQ---TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGtirvgDITIDTarsLSQQKGLI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 406 RELRNHIATVMQDIFLF------SDTIEGN-IAFGAPDatmEDVRRMARIADADHFIETMPESYDtivgERgvgLSGGQK 478
Cdd:PRK11264  81 RQLRQHVGFVFQNFNLFphrtvlENIIEGPvIVKGEPK---EEATARARELLAKVGLAGKETSYP----RR---LSGGQQ 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 479 QRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKIT-ENTTTFIIAHRISSVKE-ADEILILNHGEIIERGTHSS 556
Cdd:PRK11264 151 QRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAqEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKA 230

                 ....
gi 404223395 557 LLAE 560
Cdd:PRK11264 231 LFAD 234
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
331-549 3.35e-24

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


Pssm-ID: 213201 [Multi-domain]  Cd Length: 226  Bit Score: 101.19  E-value: 3.35e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 331 QGHVEFKNV-SFHFEDDPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLI-CRFYDP--TSGEILIDGVDARKWHVR 406
Cdd:cd03234    1 QRVLPWWDVgLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAIsGRVEGGgtTSGQILFNGQPRKPDQFQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 407 ElrnHIATVMQ-DIFLFSDTIEGNIAFGAPDAT---MEDVRRMARIADadhfiETMPESYDTIVG-ERGVGLSGGQKQRI 481
Cdd:cd03234   81 K---CVAYVRQdDILLPGLTVRETLTYTAILRLprkSSDAIRKKRVED-----VLLRDLALTRIGgNLVKGISGGERRRV 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 404223395 482 SLARALLKNPSILILDDTTSAVDMETEVKIQGELKKI-TENTTTFIIAH--RISSVKEADEILILNHGEII 549
Cdd:cd03234  153 SIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLaRRNRIVILTIHqpRSDLFRLFDRILLLSSGEIV 223
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
352-553 5.22e-24

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


Pssm-ID: 443332 [Multi-domain]  Cd Length: 533  Bit Score: 105.92  E-value: 5.22e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 352 LKNISLKASPGQTIAILGETGAGKSTL----VNLIcrfydPTSGEILIDGVD---ARKWHVRELRNHIATVMQDIF---- 420
Cdd:COG4172  302 VDGVSLTLRRGETLGLVGESGSGKSTLglalLRLI-----PSEGEIRFDGQDldgLSRRALRPLRRRMQVVFQDPFgsls 376
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 421 --LfsdTIEGNIAFG----APDATMEDvrRMARIADAdhfietMPEsydtivgergVGL------------SGGQKQRIS 482
Cdd:COG4172  377 prM---TVGQIIAEGlrvhGPGLSAAE--RRARVAEA------LEE----------VGLdpaarhryphefSGGQRQRIA 435
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 404223395 483 LARALLKNPSILILDDTTSAVDMETEVKIQGELKKITE--NTTTFIIAHRISSVKE-ADEILILNHGEIIERGT 553
Cdd:COG4172  436 IARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQRehGLAYLFISHDLAVVRAlAHRVMVMKDGKVVEQGP 509
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
354-552 6.19e-24

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


Pssm-ID: 443658 [Multi-domain]  Cd Length: 329  Bit Score: 102.89  E-value: 6.19e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 354 NISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVD---ARKWHVRELRNHIATVMQDIFLFSD---TIE 427
Cdd:COG4608   36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDitgLSGRELRPLRRRMQMVFQDPYASLNprmTVG 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 428 GNIAFGApdatmeDVRRMARIADADHFIETMPESydtivgergVGL------------SGGQKQRISLARALLKNPSILI 495
Cdd:COG4608  116 DIIAEPL------RIHGLASKAERRERVAELLEL---------VGLrpehadryphefSGGQRQRIGIARALALNPKLIV 180
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 404223395 496 LDDTTSAVDmeteVKIQ-------GELKKitE-NTTTFIIAHRISSVKE-ADEILILNHGEIIERG 552
Cdd:COG4608  181 CDEPVSALD----VSIQaqvlnllEDLQD--ElGLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIA 240
ABC_6TM_Pgp_ABCB1_D1_like cd18577
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ...
67-277 6.80e-24

Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.


Pssm-ID: 350021 [Multi-domain]  Cd Length: 300  Bit Score: 102.17  E-value: 6.80e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  67 IIRTICRYTYQIMCERIGQNSLFRIREDLYKKLQSLDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENVFLFSF 146
Cdd:cd18577   58 IGSFVLSYIQTACWTITGERQARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIA 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 147 AIIIMAAIDWKLTLALVIVTPLIAILTMKMSSKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNE 226
Cdd:cd18577  138 GFIIAFIYSWKLTLVLLATLPLIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALE 217
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 404223395 227 D-----FKKRNLDSAdvsrtylpvldSLAGMLVVITLIF------GGYLVIKGQMTLGDLVA 277
Cdd:cd18577  218 KarkagIKKGLVSGL-----------GLGLLFFIIFAMYalafwyGSRLVRDGEISPGDVLT 268
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
352-546 1.09e-23

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


Pssm-ID: 130252 [Multi-domain]  Cd Length: 230  Bit Score: 99.85  E-value: 1.09e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  352 LKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDarkwhVRELRNHIATVMQDIFLFS-DTIEGNI 430
Cdd:TIGR01184   1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQ-----ITEPGPDRMVVFQNYSLLPwLTVRENI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  431 AFgAPDATMEDVRRMARIADADHFIET--MPESYDTIVGErgvgLSGGQKQRISLARALLKNPSILILDDTTSAVDMETE 508
Cdd:TIGR01184  76 AL-AVDRVLPDLSKSERRAIVEEHIALvgLTEAADKRPGQ----LSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTR 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 404223395  509 VKIQGELKKITENT--TTFIIAHRI-SSVKEADEILILNHG 546
Cdd:TIGR01184 151 GNLQEELMQIWEEHrvTVLMVTHDVdEALLLSDRVVMLTNG 191
cbiO PRK13644
energy-coupling factor transporter ATPase;
334-560 1.15e-23

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 100.83  E-value: 1.15e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFEDdpNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKW-HVRELRNHI 412
Cdd:PRK13644   2 IRLENVSYSYPD--GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFsKLQGIRKLV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 413 ATVMQ--DIFLFSDTIEGNIAFGAPDATMEDVRRMARIADAdhFIETMPESYDTivgERGVGLSGGQKQRISLARALLKN 490
Cdd:PRK13644  80 GIVFQnpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRA--LAEIGLEKYRH---RSPKTLSGGQGQCVALAGILTME 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 404223395 491 PSILILDDTTSAVDMETEVKIQGELKKITENTTTFI-IAHRISSVKEADEILILNHGEIIERGTHSSLLAE 560
Cdd:PRK13644 155 PECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVyITHNLEELHDADRIIVMDRGKIVLEGEPENVLSD 225
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
334-504 1.54e-23

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


Pssm-ID: 443308 [Multi-domain]  Cd Length: 206  Bit Score: 98.71  E-value: 1.54e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFEDDPntdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKwHVRELRNHIA 413
Cdd:COG4133    3 LEAENLSCRRGERL---LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-AREDYRRRLA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 414 TVMQDIFLFSD-TIEGNIAFGA----PDATMEDVRRMARIADADHFIetmpesyDTIVGErgvgLSGGQKQRISLARALL 488
Cdd:COG4133   79 YLGHADGLKPElTVRENLRFWAalygLRADREAIDEALEAVGLAGLA-------DLPVRQ----LSAGQKRRVALARLLL 147
                        170
                 ....*....|....*.
gi 404223395 489 KNPSILILDDTTSAVD 504
Cdd:COG4133  148 SPAPLWLLDEPFTALD 163
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
356-504 1.97e-23

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 99.27  E-value: 1.97e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 356 SLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDarkwHVRE--LRNHIATVMQDIFLFSD-TIEGNIAF 432
Cdd:PRK10771  19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD----HTTTppSRRPVSMLFQENNLFSHlTVAQNIGL 94
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 404223395 433 G-AP-----DATMEDVRRMARIADADHFIETMPesydtivGErgvgLSGGQKQRISLARALLKNPSILILDDTTSAVD 504
Cdd:PRK10771  95 GlNPglklnAAQREKLHAIARQMGIEDLLARLP-------GQ----LSGGQRQRVALARCLVREQPILLLDEPFSALD 161
COG4559 COG4559
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
337-553 2.13e-23

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


Pssm-ID: 443620 [Multi-domain]  Cd Length: 258  Bit Score: 99.80  E-value: 2.13e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 337 KNVSFHFeddPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIAtVM 416
Cdd:COG4559    5 ENLSVRL---GGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRA-VL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 417 -QDIFL-FSDTIE-----GNIAFGAPDATMED-VRRMARIADADHFIETmpeSYDTivgergvgLSGGQKQRISLARALL 488
Cdd:COG4559   81 pQHSSLaFPFTVEevvalGRAPHGSSAAQDRQiVREALALVGLAHLAGR---SYQT--------LSGGEQQRVQLARVLA 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 489 -------KNPSILILDDTTSAVD-------METevkiqgeLKKIT-ENTTTFIIAHRIS-SVKEADEILILNHGEIIERG 552
Cdd:COG4559  150 qlwepvdGGPRWLFLDEPTSALDlahqhavLRL-------ARQLArRGGGVVAVLHDLNlAAQYADRILLLHQGRLVAQG 222

                 .
gi 404223395 553 T 553
Cdd:COG4559  223 T 223
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
334-549 2.53e-23

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 103.57  E-value: 2.53e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFeddPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGvdaRKWHVRE----LR 409
Cdd:COG3845    6 LELRGITKRF---GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDG---KPVRIRSprdaIA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 410 NHIATVMQDIFLFSD-TIEGNIAFGAPDATmedvRRMARIADADHFIETMPESY------DTIVGErgvgLSGGQKQRIS 482
Cdd:COG3845   80 LGIGMVHQHFMLVPNlTVAENIVLGLEPTK----GGRLDRKAARARIRELSERYgldvdpDAKVED----LSVGEQQRVE 151
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 404223395 483 LARALLKNPSILILDDTTsAV--DMETEvKIQGELKKITENTTTFI-IAHRISSVKE-ADEILILNHGEII 549
Cdd:COG3845  152 ILKALYRGARILILDEPT-AVltPQEAD-ELFEILRRLAAEGKSIIfITHKLREVMAiADRVTVLRRGKVV 220
cbiO PRK13642
energy-coupling factor transporter ATPase;
334-559 4.26e-23

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 99.40  E-value: 4.26e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFEDDPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIA 413
Cdd:PRK13642   5 LEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 414 TVMQ--DIFLFSDTIEGNIAFGAPDATMEDVRRMARIADADHFIETMpeSYDTIVGERgvgLSGGQKQRISLARALLKNP 491
Cdd:PRK13642  85 MVFQnpDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNML--DFKTREPAR---LSGGQKQRVAVAGIIALRP 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 492 SILILDDTTSAVDMETEVKIQGELKKITE--NTTTFIIAHRISSVKEADEILILNHGEIIERGTHSSLLA 559
Cdd:PRK13642 160 EIIILDESTSMLDPTGRQEIMRVIHEIKEkyQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
348-553 4.56e-23

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 99.11  E-value: 4.56e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 348 NTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIATVMQ--DIFLFSDT 425
Cdd:PRK13652  16 SKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQnpDDQIFSPT 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 426 IEGNIAFGAPDATMEDVRRMARIADADHFIETmpESYDTIVGERgvgLSGGQKQRISLARALLKNPSILILDDTTSAVDM 505
Cdd:PRK13652  96 VEQDIAFGPINLGLDEETVAHRVSSALHMLGL--EELRDRVPHH---LSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDP 170
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 404223395 506 ETEVKIQGELKKITEN--TTTFIIAHRISSVKE-ADEILILNHGEIIERGT 553
Cdd:PRK13652 171 QGVKELIDFLNDLPETygMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGT 221
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
351-559 5.79e-23

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


Pssm-ID: 440179 [Multi-domain]  Cd Length: 236  Bit Score: 97.75  E-value: 5.79e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 351 VLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVREL-RNHIATVMQDIFLFSD-TIEG 428
Cdd:COG0410   18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIaRLGIGYVPEGRRIFPSlTVEE 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 429 NIAFGAPdatmedVRRmariaDADHFIETMPESYDT--IVGER----GVGLSGGQKQRISLARALLKNPSILILDDTT-- 500
Cdd:COG0410   98 NLLLGAY------ARR-----DRAEVRADLERVYELfpRLKERrrqrAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSlg 166
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 404223395 501 ---SAVDmetevKIQGELKKITENTTTFII----AHRISSVkeADEILILNHGEIIERGTHSSLLA 559
Cdd:COG0410  167 lapLIVE-----EIFEIIRRLNREGVTILLveqnARFALEI--ADRAYVLERGRIVLEGTAAELLA 225
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
334-561 1.13e-22

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 97.88  E-value: 1.13e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFEDDpnTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIA 413
Cdd:PRK13647   5 IEVEDLHFRYKDG--TKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 414 TVMQDI--FLFSDTIEGNIAFG------APDATMEDVRRMARIADADHFIETMPESydtivgergvgLSGGQKQRISLAR 485
Cdd:PRK13647  83 LVFQDPddQVFSSTVWDDVAFGpvnmglDKDEVERRVEEALKAVRMWDFRDKPPYH-----------LSYGQKKRVAIAG 151
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 404223395 486 ALLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIA-HRISSVKE-ADEILILNHGEIIERGTHSSLLAEK 561
Cdd:PRK13647 152 VLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDLAAEwADQVIVLKEGRVLAEGDKSLLTDED 229
ABC_6TM_AtABCB27_like cd18780
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ...
22-309 1.34e-22

Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.


Pssm-ID: 350053 [Multi-domain]  Cd Length: 295  Bit Score: 98.09  E-value: 1.34e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  22 FILIFIASGISIIYPLLGGKVIDDVVYQNKTNLLIPLLLIMII-------------STIIRTicrYTYQIMCERIgqnsL 88
Cdd:cd18780    2 TIALLVSSGTNLALPYFFGQVIDAVTNHSGSGGEEALRALNQAvlillgvvligsiATFLRS---WLFTLAGERV----V 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  89 FRIREDLYKKLQSLDFDFFNNTRVGDIMARMTGDTDAIRhfvSWVSYNI---LENVFLFSFAIIIMAAIDWKLTLALVIV 165
Cdd:cd18780   75 ARLRKRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQ---NAVTVNLsmlLRYLVQIIGGLVFMFTTSWKLTLVMLSV 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 166 TPLIAILTMKMSSKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSRTYLPV 245
Cdd:cd18780  152 VPPLSIGAVIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGF 231
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 404223395 246 LDSLAGMLVVITLIFGGYLVIKGQMTLGDLVAFNgfLWMLNGPMRMSGW--LINDVQRFIASSFKI 309
Cdd:cd18780  232 MGAAAQLAIVLVLWYGGRLVIDGELTTGLLTSFL--LYTLTVAMSFAFLssLYGDFMQAVGASVRV 295
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...
351-553 1.60e-22

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


Pssm-ID: 440180 [Multi-domain]  Cd Length: 257  Bit Score: 97.03  E-value: 1.60e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 351 VLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNH-IATVMQDIFLFSD-TIEG 428
Cdd:COG0411   19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLgIARTFQNPRLFPElTVLE 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 429 NIAFGA-------PDATMEDVRRMAR-----IADADHFIET--MPESYDTIVGErgvgLSGGQKQRISLARALLKNPSIL 494
Cdd:COG0411   99 NVLVAAharlgrgLLAALLRLPRARReereaRERAEELLERvgLADRADEPAGN----LSYGQQRRLEIARALATEPKLL 174
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 404223395 495 ILDDTTSAVDM-ETEvKIQGELKKITE--NTTTFIIAHRISSVKE-ADEILILNHGEIIERGT 553
Cdd:COG0411  175 LLDEPAAGLNPeETE-ELAELIRRLRDerGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGT 236
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
351-550 1.65e-22

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 97.45  E-value: 1.65e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 351 VLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDA---RKWHVRELRNHIATVMQDiflfsdtie 427
Cdd:PRK10419  27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLaklNRAQRKAFRRDIQMVFQD--------- 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 428 gniAFGAPDA----------------TMEDVRRMARIADADHFIETMPESYDTIVGErgvgLSGGQKQRISLARALLKNP 491
Cdd:PRK10419  98 ---SISAVNPrktvreiireplrhllSLDKAERLARASEMLRAVDLDDSVLDKRPPQ----LSGGQLQRVCLARALAVEP 170
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 404223395 492 SILILDDTTSAVDMETEVKIQGELKKITENTTT--FIIAHRISSVKE-ADEILILNHGEIIE 550
Cdd:PRK10419 171 KLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTacLFITHDLRLVERfCQRVMVMDNGQIVE 232
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
351-553 1.79e-22

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 97.15  E-value: 1.79e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 351 VLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIATVMQDIFL-FSDTIEGN 429
Cdd:PRK13548  17 LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFTVEEV 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 430 IAFGA------PDATMEDVRRMARIADADHFIEtmpESYDTivgergvgLSGGQKQRISLARALL------KNPSILILD 497
Cdd:PRK13548  97 VAMGRaphglsRAEDDALVAAALAQVDLAHLAG---RDYPQ--------LSGGEQQRVQLARVLAqlwepdGPPRWLLLD 165
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 498 DTTSAVDM---ETEVKIQGELKKiTENTTTFIIAHRIS-SVKEADEILILNHGEIIERGT 553
Cdd:PRK13548 166 EPTSALDLahqHHVLRLARQLAH-ERGLAVIVVLHDLNlAARYADRIVLLHQGRLVADGT 224
ABC_6TM_PrtD_LapB_HlyB_like cd18782
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ...
15-293 2.47e-22

uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.


Pssm-ID: 350055 [Multi-domain]  Cd Length: 294  Bit Score: 97.28  E-value: 2.47e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  15 RLLMIGVFILIFIASGISIIYPLLGGKVIDDVVYQNKTNLLIPLLL----IMIISTIIRTICRYTYQIMCERIGQNSLFR 90
Cdd:cd18782    1 RRALIEVLALSFVVQLLGLANPLLFQVIIDKVLVQQDLATLYVIGVvmlvAALLEAVLTALRTYLFTDTANRIDLELGGT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  91 IredlYKKLQSLDFDFFNNTRVGDIMARmTGDTDAIRHF-VSWVSYNILENVFLFsFAIIIMAAIDWKLTLALVIVTPLI 169
Cdd:cd18782   81 I----IDHLLRLPLGFFDKRPVGELSTR-ISELDTIRGFlTGTALTTLLDVLFSV-IYIAVLFSYSPLLTLVVLATVPLQ 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 170 AILTMKMSSKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEH-----NEDFKKRNLDSAdvSRTYLP 244
Cdd:cd18782  155 LLLTFLFGPILRRQIRRRAEASAKTQSYLVESLTGIQTVKAQNAELKARWRWQNRyarslGEGFKLTVLGTT--SGSLSQ 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 404223395 245 VLDSLAGMLVvitLIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPM-RMSG 293
Cdd:cd18782  233 FLNKLSSLLV---LWVGAYLVLRGELTLGQLIAFRILSGYVTGPIlRLST 279
ABC_6TM_CyaB_HlyB_like cd18588
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ...
95-301 3.07e-22

Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunits of T1SS, such as CyaG and HlyB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. Additionally, CyaB is part of the three T1SS complex proteins for adenylate cyclase toxin CyaA, which is a primary virulence factor in Bordetella pertussis: CyaB (an ABC transporter) CyaD (a membrane fusion protein), and CyaE (an outer membrane protein).


Pssm-ID: 350032 [Multi-domain]  Cd Length: 294  Bit Score: 97.18  E-value: 3.07e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  95 LYKKLQSLDFDFFNNTRVGDIMARMtGDTDAIRHFVSWVSYN-ILENVFLFSFaIIIMAAIDWKLTLALVIVTPLIAILt 173
Cdd:cd18588   81 LFRHLLRLPLSYFESRQVGDTVARV-RELESIRQFLTGSALTlVLDLVFSVVF-LAVMFYYSPTLTLIVLASLPLYALL- 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 174 mkmSSKAQPVF-YEIRESF---SRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSRTYLPVLDSL 249
Cdd:cd18588  158 ---SLLVTPILrRRLEEKFqrgAENQSFLVETVTGIETVKSLAVEPQFQRRWEELLARYVKASFKTANLSNLASQIVQLI 234
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 404223395 250 AGMLVVITLIFGGYLVIKGQMTLGDLVAFNGFLWMLNGP-MRMSGwLINDVQR 301
Cdd:cd18588  235 QKLTTLAILWFGAYLVMDGELTIGQLIAFNMLAGQVSQPvLRLVQ-LWQDFQQ 286
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
351-552 3.70e-22

ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.


Pssm-ID: 213235 [Multi-domain]  Cd Length: 208  Bit Score: 94.59  E-value: 3.70e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 351 VLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHvrELRNHIATVmqdiflfsdtIEGNI 430
Cdd:cd03268   15 VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNI--EALRRIGAL----------IEAPG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 431 AFGAPDAtMEDVRRMARIADADHfiETMPESYDtIVGERGVG------LSGGQKQRISLARALLKNPSILILDDTTSAVD 504
Cdd:cd03268   83 FYPNLTA-RENLRLLARLLGIRK--KRIDEVLD-VVGLKDSAkkkvkgFSLGMKQRLGIALALLGNPDLLILDEPTNGLD 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 404223395 505 METEVKIQGELKKITENTTTFIIA-HRISSV-KEADEILILNHGEIIERG 552
Cdd:cd03268  159 PDGIKELRELILSLRDQGITVLISsHLLSEIqKVADRIGIINKGKLIEEG 208
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
338-551 3.95e-22

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 95.92  E-value: 3.95e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 338 NVSFHFEDDPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVdarkwHVRELRNHIATVMQ 417
Cdd:PRK11248   3 QISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGK-----PVEGPGAERGVVFQ 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 418 DIFLFS-DTIEGNIAFGAPDATMEdvrRMARIADADHFIEtmpesydtIVGERGVG------LSGGQKQRISLARALLKN 490
Cdd:PRK11248  78 NEGLLPwRNVQDNVAFGLQLAGVE---KMQRLEIAHQMLK--------KVGLEGAEkryiwqLSGGQRQRVGIARALAAN 146
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 404223395 491 PSILILDDTTSAVDMETEVKIQGELKKITENT--TTFIIAHRI-SSVKEADEILIL--NHGEIIER 551
Cdd:PRK11248 147 PQLLLLDEPFGALDAFTREQMQTLLLKLWQETgkQVLLITHDIeEAVFMATELVLLspGPGRVVER 212
ABC_6TM_ABCB8_like cd18574
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ...
21-278 5.00e-22

Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.


Pssm-ID: 350018 [Multi-domain]  Cd Length: 295  Bit Score: 96.46  E-value: 5.00e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  21 VFILIFIASGISIIYPLLGGKVIDdVVYQNKTNLLIPLLLIMIISTI-------IRTICRYTYQIMCERIGQNSLFRIRE 93
Cdd:cd18574    1 AVLSALAAALVNIQIPLLLGDLVN-VISRSLKETNGDFIEDLKKPALkllglylLQSLLTFAYISLLSVVGERVAARLRN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  94 DLYKKLQSLDFDFFNNTRVGDIMARMTGDTDAIRH-FVSWVSYNiLENVFLFSFAIIIMAAIDWKLTLALVIVTP-LIAI 171
Cdd:cd18574   80 DLFSSLLRQDIAFFDTHRTGELVNRLTADVQEFKSsFKQCVSQG-LRSVTQTVGCVVSLYLISPKLTLLLLVIVPvVVLV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 172 LTM------KMSSKAQpvfyeirESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNldsadvsrTYLPV 245
Cdd:cd18574  159 GTLygsflrKLSRRAQ-------AQVAKATGVADEALGNIRTVRAFAMEDRELELYEEEVEKAAKLN--------EKLGL 223
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 404223395 246 -------LDSLA-GMLVVITLIFGGYLVIKGQMTLGDLVAF 278
Cdd:cd18574  224 gigifqgLSNLAlNGIVLGVLYYGGSLVSRGELTAGDLMSF 264
PTZ00243 PTZ00243
ABC transporter; Provisional
316-548 5.97e-22

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 101.01  E-value: 5.97e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  316 DAKIPIHAEKPAPSLQGHVEFKNVSFHFEDDPNTdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEIli 395
Cdd:PTZ00243  641 GGTGGGHEATPTSERSAKTPKMKTDDFFELEPKV-LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-- 717
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  396 dgvdarkWHVRElrnhIATVMQDIFLFSDTIEGNIAFGAPD--ATMEDVRRMARIaDADhfIETMPESYDTIVGERGVGL 473
Cdd:PTZ00243  718 -------WAERS----IAYVPQQAWIMNATVRGNILFFDEEdaARLADAVRVSQL-EAD--LAQLGGGLETEIGEKGVNL 783
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  474 SGGQKQRISLARALLKNPSILILDDTTSAVDMET-----EVKIQGELKKITENTTTfiiaHRISSVKEADEILILNHGEI 548
Cdd:PTZ00243  784 SGGQKARVSLARAVYANRDVYLLDDPLSALDAHVgervvEECFLGALAGKTRVLAT----HQVHVVPRADYVVALGDGRV 859
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
335-504 1.10e-21

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 94.01  E-value: 1.10e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 335 EFKNVSFHFEDdpnTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIAT 414
Cdd:PRK10247   9 QLQNVGYLAGD---AKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSY 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 415 VMQDIFLFSDTIEGNIAF------GAPDATmedvrrmARIADADHFieTMPEsydTIVGERGVGLSGGQKQRISLARALL 488
Cdd:PRK10247  86 CAQTPTLFGDTVYDNLIFpwqirnQQPDPA-------IFLDDLERF--ALPD---TILTKNIAELSGGEKQRISLIRNLQ 153
                        170
                 ....*....|....*.
gi 404223395 489 KNPSILILDDTTSAVD 504
Cdd:PRK10247 154 FMPKVLLLDEITSALD 169
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
336-507 1.76e-21

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 97.83  E-value: 1.76e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 336 FKNVSFHFEDDPntdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGvDARkwhvrelrnhIATV 415
Cdd:COG0488    1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-GLR----------IGYL 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 416 MQDIFLFSD-TIEGNIAFG----------------APDATMEDVRRMARIA---------DADHFIETM-------PESY 462
Cdd:COG0488   67 PQEPPLDDDlTVLDTVLDGdaelraleaeleeleaKLAEPDEDLERLAELQeefealggwEAEARAEEIlsglgfpEEDL 146
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 404223395 463 DTIVGErgvgLSGGQKQRISLARALLKNPSILILDDTTSAVDMET 507
Cdd:COG0488  147 DRPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES 187
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
350-559 3.28e-21

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 93.70  E-value: 3.28e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 350 DVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDG--VDARKWHVRELRnhIATVMQDiflfsdtie 427
Cdd:PRK15112  27 EAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDhpLHFGDYSYRSQR--IRMIFQD--------- 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 428 gniafgaPDATMEDVRRMARIADADHFIETMPES-------YDTIvgeRGVGL------------SGGQKQRISLARALL 488
Cdd:PRK15112  96 -------PSTSLNPRQRISQILDFPLRLNTDLEPeqrekqiIETL---RQVGLlpdhasyyphmlAPGQKQRLGLARALI 165
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 404223395 489 KNPSILILDDTTSAVDMETEVKIQG---ELKKITENTTTFIIAHrISSVKE-ADEILILNHGEIIERGTHSSLLA 559
Cdd:PRK15112 166 LRPKVIIADEALASLDMSMRSQLINlmlELQEKQGISYIYVTQH-LGMMKHiSDQVLVMHQGEVVERGSTADVLA 239
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
254-543 4.95e-21

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 96.80  E-value: 4.95e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 254 VVITLIFGGYLVIKGQMTLGDLV----AFNgflwMLNGPMRmsgWLIN---DVQRFIAS-----SFkiQDMMATDAKIPI 321
Cdd:COG4178  280 VIFPILVAAPRYFAGEITLGGLMqaasAFG----QVQGALS---WFVDnyqSLAEWRATvdrlaGF--EEALEAADALPE 350
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 322 HAEKPAPSLQGHVEFKNVSFHfedDPNTDVL-KNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILidgvda 400
Cdd:COG4178  351 AASRIETSEDGALALEDLTLR---TPDGRPLlEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIA------ 421
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 401 rkwhvrelRNHIATVM---QDIFLFSDTIEGNIAFGAPDATMEDvrrmARIADA------DHFIETMPESYDtivgeRGV 471
Cdd:COG4178  422 --------RPAGARVLflpQRPYLPLGTLREALLYPATAEAFSD----AELREAleavglGHLAERLDEEAD-----WDQ 484
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 404223395 472 GLSGGQKQRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHRISSVKEADEILIL 543
Cdd:COG4178  485 VLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLEL 556
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
334-553 5.65e-21

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 93.23  E-value: 5.65e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFEDDPNTD---VLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKW-HVRELR 409
Cdd:PRK13633   5 IKCKNVSYKYESNEESTeklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEeNLWDIR 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 410 NHIATVMQ--DIFLFSDTIEGNIAFG------APDATMEDVRRMARIADADHFIETMPESydtivgergvgLSGGQKQRI 481
Cdd:PRK13633  85 NKAGMVFQnpDNQIVATIVEEDVAFGpenlgiPPEEIRERVDESLKKVGMYEYRRHAPHL-----------LSGGQKQRV 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 404223395 482 SLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITEN--TTTFIIAHRISSVKEADEILILNHGEIIERGT 553
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKygITIILITHYMEEAVEADRIIVMDSGKVVMEGT 227
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
334-553 6.60e-21

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 93.76  E-value: 6.60e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFEDDPNTD--VLKNISLKASPGQTIAILGETGAGKSTLVN-----LICRFYDPTSGEILI----DGVDARK 402
Cdd:PRK13631  22 LRVKNLYCVFDEKQENElvALNNISYTFEKNKIYFIIGNSGSGKSTLVThfnglIKSKYGTIQVGDIYIgdkkNNHELIT 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 403 WHV-------RELRNHIATVMQ--DIFLFSDTIEGNIAFG--APDATMEDVRRMARiadadHFIETMPESYDTIvgERG- 470
Cdd:PRK13631 102 NPYskkiknfKELRRRVSMVFQfpEYQLFKDTIEKDIMFGpvALGVKKSEAKKLAK-----FYLNKMGLDDSYL--ERSp 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 471 VGLSGGQKQRISLARALLKNPSILILDDTTSAVDMETE---VKIQGELKKitENTTTFIIAHRISSVKE-ADEILILNHG 546
Cdd:PRK13631 175 FGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEhemMQLILDAKA--NNKTVFVITHTMEHVLEvADEVIVMDKG 252

                 ....*..
gi 404223395 547 EIIERGT 553
Cdd:PRK13631 253 KILKTGT 259
SufC COG0396
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ...
335-563 7.01e-21

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


Pssm-ID: 440165 [Multi-domain]  Cd Length: 245  Bit Score: 92.05  E-value: 7.01e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 335 EFKNVSFHFEDdpnTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRF--YDPTSGEILIDGVD---------ARKw 403
Cdd:COG0396    2 EIKNLHVSVEG---KEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDilelspderARA- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 404 hvrelrnhiatvmqDIFL---------------FSDTIEGNIAFGAPDAT--MEDVRRMARIADadhfietMPESYdtiv 466
Cdd:COG0396   78 --------------GIFLafqypveipgvsvsnFLRTALNARRGEELSARefLKLLKEKMKELG-------LDEDF---- 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 467 GERGV--GLSGGQKQRISLARALLKNPSILILDDTTSAVDMETeVKIQGE-LKKI-TENTTTFIIAH--RISSVKEADEI 540
Cdd:COG0396  133 LDRYVneGFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDA-LRIVAEgVNKLrSPDRGILIITHyqRILDYIKPDFV 211
                        250       260
                 ....*....|....*....|....*
gi 404223395 541 LILNHGEIIERGTHS--SLLAEKGY 563
Cdd:COG0396  212 HVLVDGRIVKSGGKElaLELEEEGY 236
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
334-557 8.97e-21

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 94.02  E-value: 8.97e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFEDdpNTdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKwhvRELRNH-I 412
Cdd:PRK11432   7 VVLKNITKRFGS--NT-VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH---RSIQQRdI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 413 ATVMQDIFLFSD-TIEGNIAFGAPDATMEDVRRMARIADADHFI--ETMPESY-DTIvgergvglSGGQKQRISLARALL 488
Cdd:PRK11432  81 CMVFQSYALFPHmSLGENVGYGLKMLGVPKEERKQRVKEALELVdlAGFEDRYvDQI--------SGGQQQRVALARALI 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 404223395 489 KNPSILILDDTTSAVDMETEVKIQgelKKITE-----NTTTFIIAHRISsvkEA----DEILILNHGEIIERGTHSSL 557
Cdd:PRK11432 153 LKPKVLLFDEPLSNLDANLRRSMR---EKIRElqqqfNITSLYVTHDQS---EAfavsDTVIVMNKGKIMQIGSPQEL 224
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
334-561 9.32e-21

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 92.60  E-value: 9.32e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFEDdpNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDG--VDARKWHVRELRNH 411
Cdd:PRK13636   6 LKVEELNYNYSD--GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRES 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 412 IATVMQ--DIFLFSDTIEGNIAFGAPDATM--EDVRRMARIADADHFIETMPESYDTivgergvGLSGGQKQRISLARAL 487
Cdd:PRK13636  84 VGMVFQdpDNQLFSASVYQDVSFGAVNLKLpeDEVRKRVDNALKRTGIEHLKDKPTH-------CLSFGQKKRVAIAGVL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 488 LKNPSILILDDTTSAVD-------METEVKIQGELkkiteNTTTFIIAHRISSVK-EADEILILNHGEIIERGTHSSLLA 559
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDpmgvseiMKLLVEMQKEL-----GLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFA 231

                 ..
gi 404223395 560 EK 561
Cdd:PRK13636 232 EK 233
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
352-553 1.06e-20

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


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 95.88  E-value: 1.06e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  352 LKNISLKASPGQTIAILGETGAGKSTLVNLICrFYDPT----SGEILIDG--VDARKWHVRElrnhiATVMQ-DIFLFSD 424
Cdd:TIGR00955  41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKgvkgSGSVLLNGmpIDAKEMRAIS-----AYVQQdDLFIPTL 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  425 TIEGNIAFGAP---DATMEDVRRMARIadaDHFIETMP--ESYDTIVGERGV--GLSGGQKQRISLARALLKNPSILILD 497
Cdd:TIGR00955 115 TVREHLMFQAHlrmPRRVTKKEKRERV---DEVLQALGlrKCANTRIGVPGRvkGLSGGERKRLAFASELLTDPPLLFCD 191
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 404223395  498 DTTSAVD--METEVkIQgELKKITENTTTFIIA-HRISS--VKEADEILILNHGEIIERGT 553
Cdd:TIGR00955 192 EPTSGLDsfMAYSV-VQ-VLKGLAQKGKTIICTiHQPSSelFELFDKIILMAEGRVAYLGS 250
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
352-553 1.67e-20

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 92.72  E-value: 1.67e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 352 LKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVD---ARKWHVRELRNHIATVMQDIF-------- 420
Cdd:PRK11308  31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDllkADPEAQKLLRQKIQIVFQNPYgslnprkk 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 421 ---LFSDTIEGNIAFGAPDatmedvrRMARIADADHFIETMPESYDtivgeRGVGL-SGGQKQRISLARALLKNPSILIL 496
Cdd:PRK11308 111 vgqILEEPLLINTSLSAAE-------RREKALAMMAKVGLRPEHYD-----RYPHMfSGGQRQRIAIARALMLDPDVVVA 178
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 404223395 497 DDTTSAVDMETEVKI-------QGELkkiteNTTTFIIAHRISSVKE-ADEILILNHGEIIERGT 553
Cdd:PRK11308 179 DEPVSALDVSVQAQVlnlmmdlQQEL-----GLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGT 238
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
352-561 1.88e-20

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


Pssm-ID: 131197 [Multi-domain]  Cd Length: 354  Bit Score: 93.25  E-value: 1.88e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  352 LKNISLKAS---PGQTI-AILGETGAGKSTLVNLICRFYDPTSGEILIDGV---DARKW-----HVRElrnhIATVMQDI 419
Cdd:TIGR02142   9 LGDFSLDADftlPGQGVtAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtlfDSRKGiflppEKRR----IGYVFQEA 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  420 FLFSD-TIEGNIAFGAPDATMEDVR-RMARIADA---DHFIEtmpesydtivgeRGVG-LSGGQKQRISLARALLKNPSI 493
Cdd:TIGR02142  85 RLFPHlSVRGNLRYGMKRARPSERRiSFERVIELlgiGHLLG------------RLPGrLSGGEKQRVAIGRALLSSPRL 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 404223395  494 LILDDTTSAVDMETEVKIQGELKKITENTTTFI--IAHRISSVKE-ADEILILNHGEIIERGTHSSLLAEK 561
Cdd:TIGR02142 153 LLMDEPLAALDDPRKYEILPYLERLHAEFGIPIlyVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWASP 223
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
333-552 3.15e-20

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


Pssm-ID: 213233 [Multi-domain]  Cd Length: 218  Bit Score: 89.35  E-value: 3.15e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 333 HVEFKNVSFHFEddpntdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKwHVRELRNHI 412
Cdd:cd03266    8 TKRFRDVKKTVQ------AVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 413 ATVMQDIFLFSD-TIEGNIAFGA------PDATMEDVRRMARIADADHFIEtmpesydtivgERGVGLSGGQKQRISLAR 485
Cdd:cd03266   81 GFVSDSTGLYDRlTARENLEYFAglyglkGDELTARLEELADRLGMEELLD-----------RRVGGFSTGMRQKVAIAR 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 404223395 486 ALLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIA-HRISSVKE-ADEILILNHGEIIERG 552
Cdd:cd03266  150 ALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFStHIMQEVERlCDRVVVLHRGRVVYEG 218
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
350-559 3.84e-20

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 90.41  E-value: 3.84e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 350 DVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDAR-------------KWHVRELRNHIATVM 416
Cdd:PRK10619  19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvadKNQLRLLRTRLTMVF 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 417 QDIFLFSD-TIEGNIaFGAP---------DATMEDVRRMARIADADHFIETMPesydtivgergVGLSGGQKQRISLARA 486
Cdd:PRK10619  99 QHFNLWSHmTVLENV-MEAPiqvlglskqEARERAVKYLAKVGIDERAQGKYP-----------VHLSGGQQQRVSIARA 166
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 404223395 487 LLKNPSILILDDTTSAVDMEtevkIQGELKKIT-----ENTTTFIIAHRISSVKE-ADEILILNHGEIIERGTHSSLLA 559
Cdd:PRK10619 167 LAMEPEVLLFDEPTSALDPE----LVGEVLRIMqqlaeEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLFG 241
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
334-561 4.77e-20

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 90.92  E-value: 4.77e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFEDDPNTD--VLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWH------- 404
Cdd:PRK13651   3 IKVKNIVKIFNKKLPTElkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKktkekek 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 405 -----------------VRELRNHIATVMQ--DIFLFSDTIEGNIAFGAPDATMEDVRRMARIADadhFIET--MPESYd 463
Cdd:PRK13651  83 vleklviqktrfkkikkIKEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSKEEAKKRAAK---YIELvgLDESY- 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 464 tiVGERGVGLSGGQKQRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIA-HRISSVKE-ADEIL 541
Cdd:PRK13651 159 --LQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVtHDLDNVLEwTKRTI 236
                        250       260
                 ....*....|....*....|.
gi 404223395 542 ILNHGEIIERG-THSSLLAEK 561
Cdd:PRK13651 237 FFKDGKIIKDGdTYDILSDNK 257
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
334-556 6.37e-20

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 89.30  E-value: 6.37e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFEddpNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDG--------VDARKwhV 405
Cdd:PRK11124   3 IQLNGINCFYG---AHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsktPSDKA--I 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 406 RELRNHIATVMQDIFLFSD-TIEGNIAfgapDATMEdVRRMAR---IADADHFIETMpeSYDTIVGERGVGLSGGQKQRI 481
Cdd:PRK11124  78 RELRRNVGMVFQQYNLWPHlTVQQNLI----EAPCR-VLGLSKdqaLARAEKLLERL--RLKPYADRFPLHLSGGQQQRV 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 404223395 482 SLARALLKNPSILILDDTTSAVDMETE---VKIQGELKKIteNTTTFIIAHRIS-SVKEADEILILNHGEIIERGTHSS 556
Cdd:PRK11124 151 AIARALMMEPQVLLFDEPTAALDPEITaqiVSIIRELAET--GITQVIVTHEVEvARKTASRVVYMENGHIVEQGDASC 227
ABC_6TM_HetC_like cd18568
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ...
21-288 8.43e-20

Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.


Pssm-ID: 350012 [Multi-domain]  Cd Length: 294  Bit Score: 89.93  E-value: 8.43e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  21 VFILIFIASGI----SIIYPLLGGKVIDDVVYQNKTNLLIPLLLIMIISTIIRTICRYTYQIMCERIGQNSLFRIREDLY 96
Cdd:cd18568    3 LLAEILLASLLlqllGLALPLFTQIILDRVLVHKNISLLNLILIGLLIVGIFQILLSAVRQYLLDYFANRIDLSLLSDFY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  97 KKLQSLDFDFFNNTRVGDIMARMtGDTDAIRHFVSWVSYNILENVFLFSFAIIIMAAIDWKLTLALVIVTPLIAILTMKM 176
Cdd:cd18568   83 KHLLSLPLSFFASRKVGDIITRF-QENQKIRRFLTRSALTTILDLLMVFIYLGLMFYYNLQLTLIVLAFIPLYVLLTLLS 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 177 SSKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDfemkKFHEHNEDFKKRNLDSADVSRTYLPVLDSLAGMLVVI 256
Cdd:cd18568  162 SPKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAER----PIRWRWENKFAKALNTRFRGQKLSIVLQLISSLINHL 237
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 404223395 257 TLI----FGGYLVIKGQMTLGDLVAFNGFLWMLNGP 288
Cdd:cd18568  238 GTIavlwYGAYLVISGQLTIGQLVAFNMLFGSVINP 273
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
334-559 9.00e-20

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


Pssm-ID: 132313 [Multi-domain]  Cd Length: 520  Bit Score: 92.56  E-value: 9.00e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  334 VEFKNVSFHFEDdpnTDVLKNISLKASPGQTIAILGETGAGKSTLVNLI--CRFYDPTSGEIL----------------- 394
Cdd:TIGR03269   1 IEVKNLTKKFDG---KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIIyhvalcekcgyverpsk 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  395 ----------------IDGVDARKWHVRELRNHIATVMQDIFLF--SDTIEGNIAFGAPDATMEDVRRMARIADadhFIE 456
Cdd:TIGR03269  78 vgepcpvcggtlepeeVDFWNLSDKLRRRIRKRIAIMLQRTFALygDDTVLDNVLEALEEIGYEGKEAVGRAVD---LIE 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  457 TMPESYDTIVGERGvgLSGGQKQRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKK-ITENTTTFIIAHRISSVK 535
Cdd:TIGR03269 155 MVQLSHRITHIARD--LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEaVKASGISMVLTSHWPEVI 232
                         250       260
                  ....*....|....*....|....*.
gi 404223395  536 E--ADEILILNHGEIIERGTHSSLLA 559
Cdd:TIGR03269 233 EdlSDKAIWLENGEIKEEGTPDEVVA 258
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
351-552 9.89e-20

ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.


Pssm-ID: 213187 [Multi-domain]  Cd Length: 224  Bit Score: 87.97  E-value: 9.89e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 351 VLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGvdarkwhvrelrnhiatvmqdiflfsdTIEGNI 430
Cdd:cd03220   37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG---------------------------RVSSLL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 431 AFGA---PDAT-MEDVRRMARIADADhfIETMPESYDTIVGERGVG---------LSGGQKQRISLARALLKNPSILILD 497
Cdd:cd03220   90 GLGGgfnPELTgRENIYLNGRLLGLS--RKEIDEKIDEIIEFSELGdfidlpvktYSSGMKARLAFAIATALEPDILLID 167
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 404223395 498 DTTSAVDMETEVKIQGELKKITENTTTFIIA-HRISSVKE-ADEILILNHGEIIERG 552
Cdd:cd03220  168 EVLAVGDAAFQEKCQRRLRELLKQGKTVILVsHDPSSIKRlCDRALVLEKGKIRFDG 224
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
351-559 1.30e-19

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


Pssm-ID: 213185 [Multi-domain]  Cd Length: 232  Bit Score: 87.98  E-value: 1.30e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 351 VLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHV-RELRNHIATVMQDIFLFSD-TIEG 428
Cdd:cd03218   15 VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMhKRARLGIGYLPQEASIFRKlTVEE 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 429 NIafgapDATME--DVRRMARIADADHFIETMpeSYDTIVGERGVGLSGGQKQRISLARALLKNPSILILDDTTSAVDME 506
Cdd:cd03218   95 NI-----LAVLEirGLSKKEREEKLEELLEEF--HITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPI 167
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 404223395 507 TEVKIQGELKKITE-NTTTFIIAHrisSVKE----ADEILILNHGEIIERGTHSSLLA 559
Cdd:cd03218  168 AVQDIQKIIKILKDrGIGVLITDH---NVREtlsiTDRAYIIYEGKVLAEGTPEEIAA 222
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
341-559 1.45e-19

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 88.91  E-value: 1.45e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 341 FHFEDDPntdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDG--VDARKWHVRELRNHIATVMQD 418
Cdd:PRK13638   9 FRYQDEP---VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRGLLALRQQVATVFQD 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 419 ----IFlFSDtIEGNIAF-----GAPDAtmEDVRRMAR---IADADHFIETMPESydtivgergvgLSGGQKQRISLARA 486
Cdd:PRK13638  86 peqqIF-YTD-IDSDIAFslrnlGVPEA--EITRRVDEaltLVDAQHFRHQPIQC-----------LSHGQKKRVAIAGA 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 404223395 487 LLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFII-AHRISSVKE-ADEILILNHGEIIERGTHSSLLA 559
Cdd:PRK13638 151 LVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIIsSHDIDLIYEiSDAVYVLRQGQILTHGAPGEVFA 225
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
354-559 1.61e-19

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


Pssm-ID: 443319 [Multi-domain]  Cd Length: 358  Bit Score: 90.16  E-value: 1.61e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 354 NISLKASPGQTIAILGETGAGKSTLVNLI---CRfydPTSGEILIDG---VDARKWHVR--ELRnHIATVMQDIFLFSD- 424
Cdd:COG4148   17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIaglER---PDSGRIRLGGevlQDSARGIFLppHRR-RIGYVFQEARLFPHl 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 425 TIEGNIAFGApdatmedvRRMARIADADHFietmpesyDTIVG--------ERGVG-LSGGQKQRISLARALLKNPSILI 495
Cdd:COG4148   93 SVRGNLLYGR--------KRAPRAERRISF--------DEVVEllgighllDRRPAtLSGGERQRVAIGRALLSSPRLLL 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 496 LDDTTSAVDMETEVKIQGELKKITENTTTFII--AHrisSVKE----ADEILILNHGEIIERGTHSSLLA 559
Cdd:COG4148  157 MDEPLAALDLARKAEILPYLERLRDELDIPILyvSH---SLDEvarlADHVVLLEQGRVVASGPLAEVLS 223
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
351-552 1.68e-19

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 92.08  E-value: 1.68e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 351 VLKNISLKASPGQTIAILGETGAGKST----LVNLIcrfydPTSGEILIDGVDARKWHVREL---RNHIATVMQDIFLFS 423
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDPNSSL 375
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 424 D---TIEGNIAFG--APDATMEDVRRMARIADADHFIETMPESYDTIVGErgvgLSGGQKQRISLARALLKNPSILILDD 498
Cdd:PRK15134 376 NprlNVLQIIEEGlrVHQPTLSAAQREQQVIAVMEEVGLDPETRHRYPAE----FSGGQRQRIAIARALILKPSLIILDE 451
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 404223395 499 TTSAVDMETEVKIQGELKKITEN--TTTFIIAHRISSVKE-ADEILILNHGEIIERG 552
Cdd:PRK15134 452 PTSSLDKTVQAQILALLKSLQQKhqLAYLFISHDLHVVRAlCHQVIVLRQGEVVEQG 508
ABC_6TM_Pgp_ABCB1_D2_like cd18578
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ...
8-319 1.77e-19

Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.


Pssm-ID: 350022 [Multi-domain]  Cd Length: 317  Bit Score: 89.43  E-value: 1.77e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395   8 WQYVRKYRLLMIgvfiLIFIASGIS-IIYPLLG---GKVIDdvVYQNkTNLLIPLLLIMIIST------IIRTICRYTYQ 77
Cdd:cd18578    1 LKLNKPEWPLLL----LGLIGAIIAgAVFPVFAilfSKLIS--VFSL-PDDDELRSEANFWALmflvlaIVAGIAYFLQG 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  78 IMCERIGQNSLFRIREDLYKKLQSLDFDFF---NNTrVGDIMARMTGDTDAIRHFVSWVSYNILENVFLFSFAIIIMAAI 154
Cdd:cd18578   74 YLFGIAGERLTRRLRKLAFRAILRQDIAWFddpENS-TGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVY 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 155 DWKLTLALVIVTPLIAILT---MKMSSKAQpvfYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKR 231
Cdd:cd18578  153 GWKLALVGLATVPLLLLAGylrMRLLSGFE---EKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKK 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 232 NLDSADVSRTYLPVLDSLagMLVVITLIF--GGYLVIKGQMTLGD-LVAFNGFLWMLNGPMRMSGwLINDVQRFIASSFK 308
Cdd:cd18578  230 GLRRALISGLGFGLSQSL--TFFAYALAFwyGGRLVANGEYTFEQfFIVFMALIFGAQSAGQAFS-FAPDIAKAKAAAAR 306
                        330
                 ....*....|.
gi 404223395 309 IQDMMATDAKI 319
Cdd:cd18578  307 IFRLLDRKPEI 317
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
331-552 3.05e-19

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 87.28  E-value: 3.05e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 331 QGHVEFKNVSFHFEDdpnTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYD-----PTSGEILIDGVDARKWHV 405
Cdd:PRK14247   1 MNKIEIRDLKVSFGQ---VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 406 RELRNHIATVMQ------DIFLFSdtiegNIAFGAPDATMEDVRR--MARIADADHFIETMPESYDTIVGERGvGLSGGQ 477
Cdd:PRK14247  78 IELRRRVQMVFQipnpipNLSIFE-----NVALGLKLNRLVKSKKelQERVRWALEKAQLWDEVKDRLDAPAG-KLSGGQ 151
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 404223395 478 KQRISLARALLKNPSILILDDTTSAVDMETEVKIQG---ELKKitENTTTFIIAHRISSVKEADEILILNHGEIIERG 552
Cdd:PRK14247 152 QQRLCIARALAFQPEVLLADEPTANLDPENTAKIESlflELKK--DMTIVLVTHFPQQAARISDYVAFLYKGQIVEWG 227
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
351-553 3.08e-19

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


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 87.06  E-value: 3.08e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 351 VLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGvdarkwhvR-----ELR---NHIATVMQDIFLF 422
Cdd:COG1134   41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG--------RvsallELGagfHPELTGRENIYLN 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 423 sdtieGNIaFGAPDATMEdvRRMARIAD-AD--HFIEtMP-ESYdtivgergvglSGGQKQRISLARALLKNPSILILDD 498
Cdd:COG1134  113 -----GRL-LGLSRKEID--EKFDEIVEfAElgDFID-QPvKTY-----------SSGMRARLAFAVATAVDPDILLVDE 172
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 404223395 499 TTSAVDMETEVKIQGELKKITENTTTFIIA-HRISSVKE-ADEILILNHGEIIERGT 553
Cdd:COG1134  173 VLAVGDAAFQKKCLARIRELRESGRTVIFVsHSMGAVRRlCDRAIWLEKGRLVMDGD 229
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
334-559 3.17e-19

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


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 87.24  E-value: 3.17e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFEddpNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHV-RELRNHI 412
Cdd:PRK11614   6 LSFDKVSAHYG---KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTaKIMREAV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 413 ATVMQDIFLFSD-TIEGNIAFGAPDATMEDVR-RMARIADadhfieTMPESYDTIVgERGVGLSGGQKQRISLARALLKN 490
Cdd:PRK11614  83 AIVPEGRRVFSRmTVEENLAMGGFFAERDQFQeRIKWVYE------LFPRLHERRI-QRAGTMSGGEQQMLAIGRALMSQ 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 404223395 491 PSILILDDTTSAVDMETEVKIQGELKKI-TENTTTFIIAHRIS-SVKEADEILILNHGEIIERGTHSSLLA 559
Cdd:PRK11614 156 PRLLLLDEPSLGLAPIIIQQIFDTIEQLrEQGMTIFLVEQNANqALKLADRGYVLENGHVVLEDTGDALLA 226
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
351-548 3.65e-19

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 87.43  E-value: 3.65e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 351 VLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILidgvdARKWHVRELRNHIATVMQDIFLFS-DTIEGN 429
Cdd:PRK11247  27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL-----AGTAPLAEAREDTRLMFQDARLLPwKKVIDN 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 430 IAFGAPDATMEDVRR-MARIADADHfietmpesydtiVGERGVGLSGGQKQRISLARALLKNPSILILDDTTSAVDMETE 508
Cdd:PRK11247 102 VGLGLKGQWRDAALQaLAAVGLADR------------ANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTR 169
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 404223395 509 VKIQGELKKI--TENTTTFIIAHRIS-SVKEADEILILNHGEI 548
Cdd:PRK11247 170 IEMQDLIESLwqQHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
334-558 5.32e-19

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 89.52  E-value: 5.32e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFEDdpnTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIA 413
Cdd:PRK09536   4 IDVSDLSVEFGD---TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 414 TVMQDIflfsdtiegNIAFgapDATMEDVRRMARIADADHFiETMPESYDTIVGE------------RGV-GLSGGQKQR 480
Cdd:PRK09536  81 SVPQDT---------SLSF---EFDVRQVVEMGRTPHRSRF-DTWTETDRAAVERamertgvaqfadRPVtSLSGGERQR 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 481 ISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIA-HRIS-SVKEADEILILNHGEIIERGTHSSLL 558
Cdd:PRK09536 148 VLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAiHDLDlAARYCDELVLLADGRVRAAGPPADVL 227
cbiO PRK13645
energy-coupling factor transporter ATPase;
329-553 6.65e-19

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 87.37  E-value: 6.65e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 329 SLQGHVEFKNVSFHFEDDPNTD--VLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILID------GVDA 400
Cdd:PRK13645   2 DFSKDIILDNVSYTYAKKTPFEfkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGdyaipaNLKK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 401 RKwHVRELRNHIATVMQ--DIFLFSDTIEGNIAFGAPDATMEDVRRMARIADADHFIEtMPESYdtiVGERGVGLSGGQK 478
Cdd:PRK13645  82 IK-EVKRLRKEIGLVFQfpEYQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQ-LPEDY---VKRSPFELSGGQK 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 404223395 479 QRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFII--AHRISSV-KEADEILILNHGEIIERGT 553
Cdd:PRK13645 157 RRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIImvTHNMDQVlRIADEVIVMHEGKVISIGS 234
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
335-549 9.79e-19

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 89.78  E-value: 9.79e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 335 EFKNVSFHFED-DPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVREL----R 409
Cdd:PRK10535   6 ELKDIRRSYPSgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrR 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 410 NHIATVMQDIFLFSD-TIEGNIAFGAPDATMEDVRRMARiadADHFIETMpeSYDTIVGERGVGLSGGQKQRISLARALL 488
Cdd:PRK10535  86 EHFGFIFQRYHLLSHlTAAQNVEVPAVYAGLERKQRLLR---AQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALM 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 404223395 489 KNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFII-AHRISSVKEADEILILNHGEII 549
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIvTHDPQVAAQAERVIEIRDGEIV 222
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
331-557 1.01e-18

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 89.20  E-value: 1.01e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 331 QGHVEFKNVSFHFeddPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRN 410
Cdd:PRK11288   2 SPYLSFDGIGKTF---PGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 411 H-IATVMQDIFLFSD-TIEGNIAFGAPDATMEDVRRMARIADADHFIETMPESYD--TIVGErgvgLSGGQKQRISLARA 486
Cdd:PRK11288  79 AgVAIIYQELHLVPEmTVAENLYLGQLPHKGGIVNRRLLNYEAREQLEHLGVDIDpdTPLKY----LSIGQRQMVEIAKA 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 404223395 487 LLKNPSILILDDTTSAVDM-ETEV--KIQGELKKitENTTTFIIAHRISSVKE-ADEILILNHGEIIErgTHSSL 557
Cdd:PRK11288 155 LARNARVIAFDEPTSSLSArEIEQlfRVIRELRA--EGRVILYVSHRMEEIFAlCDAITVFKDGRYVA--TFDDM 225
cbiO PRK13643
energy-coupling factor transporter ATPase;
334-560 1.13e-18

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 86.71  E-value: 1.13e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFEddPNTD----VLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGV----DARKWHV 405
Cdd:PRK13643   2 IKFEKVNYTYQ--PNSPfasrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIvvssTSKQKEI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 406 RELRNHIATVMQ--DIFLFSDTIEGNIAFGAPD--ATMEDVRRMAriADADHFIETMPESYDTIVGErgvgLSGGQKQRI 481
Cdd:PRK13643  80 KPVRKKVGVVFQfpESQLFEETVLKDVAFGPQNfgIPKEKAEKIA--AEKLEMVGLADEFWEKSPFE----LSGGQMRRV 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 482 SLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITEN-TTTFIIAHRISSVKE-ADEILILNHGEIIERGTHSSLLA 559
Cdd:PRK13643 154 AIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSgQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVFQ 233

                 .
gi 404223395 560 E 560
Cdd:PRK13643 234 E 234
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
334-552 1.19e-18

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


Pssm-ID: 213236 [Multi-domain]  Cd Length: 210  Bit Score: 84.64  E-value: 1.19e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFEDdpnTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDG--VDArkwhvrELRNH 411
Cdd:cd03269    1 LEVENVTKRFGR---VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGkpLDI------AARNR 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 412 IATVMQDIFLFSDT--IEGNIAFgapdATMEDVRRMARIADADHFIETMP-ESYDTIVGERgvgLSGGQKQRISLARALL 488
Cdd:cd03269   72 IGYLPEERGLYPKMkvIDQLVYL----AQLKGLKKEEARRRIDEWLERLElSEYANKRVEE---LSKGNQQKVQFIAAVI 144
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 404223395 489 KNPSILILDDTTSAVD-METEVkIQGELKKITENTTTFII-AHRISSVKE-ADEILILNHGEIIERG 552
Cdd:cd03269  145 HDPELLILDEPFSGLDpVNVEL-LKDVIRELARAGKTVILsTHQMELVEElCDRVLLLNKGRAVLYG 210
CeuD COG4604
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ...
334-553 1.47e-18

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


Pssm-ID: 443654 [Multi-domain]  Cd Length: 252  Bit Score: 85.52  E-value: 1.47e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFEDDPntdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIA 413
Cdd:COG4604    2 IEIKNVSKRYGGKV---VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 414 TVMQDIFLFSD-TIEGNIAFG-------APdaTMEDVRrmaRIADADHFIETMP--ESY-DTivgergvgLSGGQKQRIS 482
Cdd:COG4604   79 ILRQENHINSRlTVRELVAFGrfpyskgRL--TAEDRE---IIDEAIAYLDLEDlaDRYlDE--------LSGGQRQRAF 145
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 404223395 483 LARALLKNPSILILDDTTSAVDMETEVKIQGELKKITE--NTTTFIIAHRI---SSVkeADEILILNHGEIIERGT 553
Cdd:COG4604  146 IAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADelGKTVVIVLHDInfaSCY--ADHIVAMKDGRVVAQGT 219
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
352-552 1.67e-18

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 85.21  E-value: 1.67e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 352 LKNISLKASPGQTIAILGETGAGKSTLVNLICRFYD-----PTSGEILIDGVD--ARKWHVRELRNHIATVMQDIFLFSD 424
Cdd:PRK14239  21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNiySPRTDTVDLRKEIGMVFQQPNPFPM 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 425 TIEGNIAFG----------APDATMEDVRRMARIADadhfiETMPESYDTivgerGVGLSGGQKQRISLARALLKNPSIL 494
Cdd:PRK14239 101 SIYENVVYGlrlkgikdkqVLDEAVEKSLKGASIWD-----EVKDRLHDS-----ALGLSGGQQQRVCIARVLATSPKII 170
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 404223395 495 ILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHrisSVKEADEI-----LILNhGEIIERG 552
Cdd:PRK14239 171 LLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTR---SMQQASRIsdrtgFFLD-GDLIEYN 229
ABC_6TM_TAP2 cd18590
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ...
90-278 1.85e-18

Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.


Pssm-ID: 350034 [Multi-domain]  Cd Length: 289  Bit Score: 85.85  E-value: 1.85e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  90 RIREDLYKKLQSLDFDFFNNTRVGDIMARMTGDTDAIRHfvsWVSYNIleNVFLFSFA-----IIIMAAIDWKLTLALVI 164
Cdd:cd18590   70 RLRHQLFSSLVQQDIGFFEKTKTGDLTSRLSTDTTLMSR---SVALNA--NVLLRSLVktlgmLGFMLSLSWQLTLLTLI 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 165 VTPLIAILTMKMSSKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDfKKRNLDSADVSRTYLP 244
Cdd:cd18590  145 EMPLTAIAQKVYNTYHQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALER-TYNLKDRRDTVRAVYL 223
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 404223395 245 VLDSLAGMLV-VITLIFGGYLVIKGQMTLGDLVAF 278
Cdd:cd18590  224 LVRRVLQLGVqVLMLYCGRQLIQSGHLTTGSLVSF 258
cbiO PRK13641
energy-coupling factor transporter ATPase;
334-561 1.90e-18

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 86.04  E-value: 1.90e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFEddPNTDV----LKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDG----VDARKWHV 405
Cdd:PRK13641   3 IKFENVDYIYS--PGTPMekkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitPETGNKNL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 406 RELRNHIATVMQ--DIFLFSDTIEGNIAFGA-------PDATMEDVRRMARIADADHFIETMPesydtivgergVGLSGG 476
Cdd:PRK13641  81 KKLRKKVSLVFQfpEAQLFENTVLKDVEFGPknfgfseDEAKEKALKWLKKVGLSEDLISKSP-----------FELSGG 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 477 QKQRISLARALLKNPSILILDDTTSAVDMETevkiQGELKKITENT-----TTFIIAHRISSVKE-ADEILILNHGEIIE 550
Cdd:PRK13641 150 QMRRVAIAGVMAYEPEILCLDEPAAGLDPEG----RKEMMQLFKDYqkaghTVILVTHNMDDVAEyADDVLVLEHGKLIK 225
                        250
                 ....*....|.
gi 404223395 551 RGTHSSLLAEK 561
Cdd:PRK13641 226 HASPKEIFSDK 236
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
348-561 1.95e-18

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 85.07  E-value: 1.95e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 348 NTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIATVMQdIFLfsdTIE 427
Cdd:PRK11231  14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQ-HHL---TPE 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 428 GN-----IAFG-APDATMedvrrMARIADADHFIET--MPESYDTIVGERGV-GLSGGQKQRISLARALLKNPSILILDD 498
Cdd:PRK11231  90 GItvrelVAYGrSPWLSL-----WGRLSAEDNARVNqaMEQTRINHLADRRLtDLSGGQRQRAFLAMVLAQDTPVVLLDE 164
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 404223395 499 TTSAVDMETEVKIQGELKKITENTTTFI-IAHRIS-SVKEADEILILNHGEIIERGTHSSLLAEK 561
Cdd:PRK11231 165 PTTYLDINHQVELMRLMRELNTQGKTVVtVLHDLNqASRYCDHLVVLANGHVMAQGTPEEVMTPG 229
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
352-549 2.05e-18

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 88.45  E-value: 2.05e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 352 LKNISLKASPGQTIAILGETGAGKSTLVNLICRFYdPT---SGEILIDGVDARKWHVREL-RNHIATVMQDIFLFSD-TI 426
Cdd:PRK13549  21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQASNIRDTeRAGIAIIHQELALVKElSV 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 427 EGNIAFGA---PDATMEDVRRMARiadADHFIE--TMPESYDTIVGErgvgLSGGQKQRISLARALLKNPSILILDDTTS 501
Cdd:PRK13549 100 LENIFLGNeitPGGIMDYDAMYLR---AQKLLAqlKLDINPATPVGN----LGLGQQQLVEIAKALNKQARLLILDEPTA 172
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 404223395 502 AV-DMETEV--KIQGELKKitENTTTFIIAHRISSVKE-ADEILILNHGEII 549
Cdd:PRK13549 173 SLtESETAVllDIIRDLKA--HGIACIYISHKLNEVKAiSDTICVIRDGRHI 222
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
351-558 2.25e-18

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 85.10  E-value: 2.25e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 351 VLKNISLKASPGQTIAILGETGAGKSTLVNLICRF---YDP---TSGEILIDGVDARKWHVRELRNHIATVMQDIFLFSD 424
Cdd:PRK14246  25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiYDSkikVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNPFPH 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 425 -TIEGNIAFGAPDATMEDVRRMARIADAD-HFIETMPESYDTIvGERGVGLSGGQKQRISLARALLKNPSILILDDTTSA 502
Cdd:PRK14246 105 lSIYDNIAYPLKSHGIKEKREIKKIVEEClRKVGLWKEVYDRL-NSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSM 183
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 404223395 503 VDMETEVKIQGELKKITENTTTFIIAHRISSV-KEADEILILNHGEIIERGTHSSLL 558
Cdd:PRK14246 184 IDIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEIF 240
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
349-529 3.01e-18

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 84.10  E-value: 3.01e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 349 TDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVR---ELRNH-IATVMQDIFLFSD 424
Cdd:PRK11629  22 TDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAakaELRNQkLGFIYQFHHLLPD 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 425 -TIEGNIAF------GAPDATMEDVRRMARIADADHFIETMPESydtivgergvgLSGGQKQRISLARALLKNPSILILD 497
Cdd:PRK11629 102 fTALENVAMplligkKKPAEINSRALEMLAAVGLEHRANHRPSE-----------LSGGERQRVAIARALVNNPRLVLAD 170
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 404223395 498 DTTSAVDMETEVKI---QGELkKITENTTTFIIAH 529
Cdd:PRK11629 171 EPTGNLDARNADSIfqlLGEL-NRLQGTAFLVVTH 204
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
352-580 6.02e-18

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 84.06  E-value: 6.02e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 352 LKNISLKASPGQTIAILGETGAGKSTLVNLICRFYD--PT---SGEILIDGVDARKWHVR--ELRNHIATVMQDIFLFSD 424
Cdd:PRK14243  26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGfrvEGKVTFHGKNLYAPDVDpvEVRRRIGMVFQKPNPFPK 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 425 TIEGNIAFGAP--------DATMEDVRRMARIADadhfietmpESYDTIvGERGVGLSGGQKQRISLARALLKNPSILIL 496
Cdd:PRK14243 106 SIYDNIAYGARingykgdmDELVERSLRQAALWD---------EVKDKL-KQSGLSLSGGQQQRLCIARAIAVQPEVILM 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 497 DDTTSAVDMETEVKIQGELKKITENTTTFIIAHRISSVKEADEILILNHGEIIERGTHSSLLAEKGYYFDIYN--KQLGT 574
Cdd:PRK14243 176 DEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFNVELTEGGGRYGYLVEFDRTEKIFNspQQQAT 255

                 ....*.
gi 404223395 575 EANVNG 580
Cdd:PRK14243 256 RDYVSG 261
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
338-553 6.91e-18

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 87.22  E-value: 6.91e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 338 NVSFHfEDDPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARK--WHVRELRNHIATV 415
Cdd:PRK10261  19 NIAFM-QEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRrsRQVIELSEQSAAQ 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 416 MQDI------FLFSDTIEG-NIAFGAPDATMEDVR------RMARIADADHFIET--MPESyDTIVGERGVGLSGGQKQR 480
Cdd:PRK10261  98 MRHVrgadmaMIFQEPMTSlNPVFTVGEQIAESIRlhqgasREEAMVEAKRMLDQvrIPEA-QTILSRYPHQLSGGMRQR 176
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 404223395 481 ISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITENTT--TFIIAHRISSVKE-ADEILILNHGEIIERGT 553
Cdd:PRK10261 177 VMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEiADRVLVMYQGEAVETGS 252
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
351-563 7.52e-18

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


Pssm-ID: 213184 [Multi-domain]  Cd Length: 200  Bit Score: 82.19  E-value: 7.52e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 351 VLKNISLKASPGQTIAILGETGAGKSTLVNLICRF--YDPTSGEILIDGVD---------ARKwhvrelrnhiatvmqDI 419
Cdd:cd03217   15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDitdlppeerARL---------------GI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 420 FLfsdtiegniAFGAPdATMEDVRRMariadadHFIETMpesydtivgerGVGLSGGQKQRISLARALLKNPSILILDDT 499
Cdd:cd03217   80 FL---------AFQYP-PEIPGVKNA-------DFLRYV-----------NEGFSGGEKKRNEILQLLLLEPDLAILDEP 131
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 404223395 500 TSAVDMETEVKIQGELKKI-TENTTTFIIAH--RISSVKEADEILILNHGEIIERGTHS--SLLAEKGY 563
Cdd:cd03217  132 DSGLDIDALRLVAEVINKLrEEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGDKElaLEIEKKGY 200
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
334-552 8.21e-18

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 85.47  E-value: 8.21e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFEDdpnTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDgvDARKWHVRELRNHIA 413
Cdd:PRK11000   4 VTLRNVTKAYGD---VVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIG--EKRMNDVPPAERGVG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 414 TVMQDIFLFSD-TIEGNIAFGAPDATMED------VRRMARIADADHFIETMPESydtivgergvgLSGGQKQRISLARA 486
Cdd:PRK11000  79 MVFQSYALYPHlSVAENMSFGLKLAGAKKeeinqrVNQVAEVLQLAHLLDRKPKA-----------LSGGQRQRVAIGRT 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 404223395 487 LLKNPSILILDDTTSAVDMETEVKIQGELKKITE--NTTTFIIAH-RISSVKEADEILILNHGEIIERG 552
Cdd:PRK11000 148 LVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVG 216
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
334-562 1.22e-17

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 83.53  E-value: 1.22e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFEddPNT----DVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILI------DGVDARKw 403
Cdd:PRK13634   3 ITFQKVEHRYQ--YKTpferRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitAGKKNKK- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 404 hVRELRNHIATVMQdiF----LFSDTIEGNIAFGAPD--ATMEDVRRMARiadadHFIET--MPESydtIVGERGVGLSG 475
Cdd:PRK13634  80 -LKPLRKKVGIVFQ--FpehqLFEETVEKDICFGPMNfgVSEEDAKQKAR-----EMIELvgLPEE---LLARSPFELSG 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 476 GQKQRISLARALLKNPSILILDDTTSAVD-------METEVKIQGElkkitENTTTFIIAHRISSV-KEADEILILNHGE 547
Cdd:PRK13634 149 GQMRRVAIAGVLAMEPEVLVLDEPTAGLDpkgrkemMEMFYKLHKE-----KGLTTVLVTHSMEDAaRYADQIVVMHKGT 223
                        250       260
                 ....*....|....*....|.
gi 404223395 548 IIERGT------HSSLLAEKG 562
Cdd:PRK13634 224 VFLQGTpreifaDPDELEAIG 244
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
334-545 1.44e-17

ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).


Pssm-ID: 213190 [Multi-domain]  Cd Length: 166  Bit Score: 80.28  E-value: 1.44e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHfeDDPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEIlidgvdarkwhVRELRNHIA 413
Cdd:cd03223    1 IELENLSLA--TPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI-----------GMPEGEDLL 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 414 TVMQDIFLfsdtiegniafgaPDATMEDVrrmarIAdadhfietmpesY--DTIvgergvgLSGGQKQRISLARALLKNP 491
Cdd:cd03223   68 FLPQRPYL-------------PLGTLREQ-----LI------------YpwDDV-------LSGGEQQRLAFARLLLHKP 110
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 404223395 492 SILILDDTTSAVDMETEVKIqgeLKKITENTTTFI-IAHRISSVKEADEILILNH 545
Cdd:cd03223  111 KFVFLDEATSALDEESEDRL---YQLLKELGITVIsVGHRPSLWKFHDRVLDLDG 162
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
334-553 1.53e-17

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 82.78  E-value: 1.53e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFEddpNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDpTSGEILIDG--------VDARKWHV 405
Cdd:PRK14258   8 IKVNNLSFYYD---TQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEGrveffnqnIYERRVNL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 406 RELRNHIATVMQDIFLFSDTIEGNIAFGA------PDATMEDVRRMArIADADHFIETMPESYDTivgerGVGLSGGQKQ 479
Cdd:PRK14258  84 NRLRRQVSMVHPKPNLFPMSVYDNVAYGVkivgwrPKLEIDDIVESA-LKDADLWDEIKHKIHKS-----ALDLSGGQQQ 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 480 RISLARALLKNPSILILDDTTSAVDMETEVKIQGELK--KITENTTTFIIAHRISSVKEADEILILNHG------EIIER 551
Cdd:PRK14258 158 RLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenrigQLVEF 237

                 ..
gi 404223395 552 GT 553
Cdd:PRK14258 238 GL 239
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
316-507 1.55e-17

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 85.89  E-value: 1.55e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 316 DAKIPIHAEKPAPSlqGH--VEFKNVSFHFEDDPntdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEI 393
Cdd:COG0488  298 DKTVEIRFPPPERL--GKkvLELEGLSKSYGDKT---LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV 372
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 394 lidgvdarKWHVReLRnhIATV--MQDIFLFSDTIEGNIAFGAPDATMEDVRrmariadadHFIETM---PESYDTIVGE 468
Cdd:COG0488  373 --------KLGET-VK--IGYFdqHQEELDPDKTVLDELRDGAPGGTEQEVR---------GYLGRFlfsGDDAFKPVGV 432
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 404223395 469 rgvgLSGGQKQRISLARALLKNPSILILDDTTSAVDMET 507
Cdd:COG0488  433 ----LSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIET 467
cbiO PRK13649
energy-coupling factor transporter ATPase;
334-573 1.84e-17

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 82.87  E-value: 1.84e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFEDDPNTD--VLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGV----DARKWHVRE 407
Cdd:PRK13649   3 INLQNVSYTYQAGTPFEgrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTlitsTSKNKDIKQ 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 408 LRNHIATVMQ--DIFLFSDTIEGNIAFGAPD--ATMEDVRRMAR-----IADADHFIETMPesydtivgergVGLSGGQK 478
Cdd:PRK13649  83 IRKKVGLVFQfpESQLFEETVLKDVAFGPQNfgVSQEEAEALAReklalVGISESLFEKNP-----------FELSGGQM 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 479 QRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFI-IAHRISSVKE-ADEILILNHGEIIERGTHSS 556
Cdd:PRK13649 152 RRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVlVTHLMDDVANyADFVYVLEKGKLVLSGKPKD 231
                        250
                 ....*....|....*..
gi 404223395 557 LLAEKGYyfdIYNKQLG 573
Cdd:PRK13649 232 IFQDVDF---LEEKQLG 245
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
350-548 2.00e-17

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


Pssm-ID: 213182 [Multi-domain]  Cd Length: 182  Bit Score: 80.17  E-value: 2.00e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 350 DVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNH-IATVMQD-----IFLfS 423
Cdd:cd03215   14 GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVPEDrkregLVL-D 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 424 DTIEGNIAFGapdatmedvrrmariadadhfietmpesydtivgergVGLSGGQKQRISLARALLKNPSILILDDTTSAV 503
Cdd:cd03215   93 LSVAENIALS-------------------------------------SLLSGGNQQKVVLARWLARDPRVLILDEPTRGV 135
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 404223395 504 DMETEVKIQGELKKITENTTTFIIahrISS-----VKEADEILILNHGEI 548
Cdd:cd03215  136 DVGAKAEIYRLIRELADAGKAVLL---ISSeldelLGLCDRILVMYEGRI 182
ABC_6TM_TAP1 cd18589
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ...
65-278 2.08e-17

Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.


Pssm-ID: 350033 [Multi-domain]  Cd Length: 289  Bit Score: 82.90  E-value: 2.08e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  65 STIIRTICRYTYQIMCERIGQnslfRIREDLYKKLQSLDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENVFLF 144
Cdd:cd18589   49 SAVSEFVCDLIYNITMSRIHS----RLQGLVFAAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARG 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 145 SFAIIIMAAIDWKLTLALVIVTPLIAILTMKMSSKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEH 224
Cdd:cd18589  125 LFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEEGEAQRYRQR 204
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 404223395 225 NEDFKKRNLDSAdVSRTYLPVLDSLAGM-LVVITLIFGGYLVIKGQMTLGDLVAF 278
Cdd:cd18589  205 LQKTYRLNKKEA-AAYAVSMWTSSFSGLaLKVGILYYGGQLVTAGTVSSGDLVTF 258
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
334-553 2.43e-17

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


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 82.85  E-value: 2.43e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFEDdpnTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHvrelRNHIA 413
Cdd:COG4152    2 LELKGLTKRFGD---KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED----RRRIG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 414 ------------TVM-QDIFLfsdtiegniafgapdATMEDVRRMARIADADHFIET--MPESYDTIVGErgvgLSGGQK 478
Cdd:COG4152   75 ylpeerglypkmKVGeQLVYL---------------ARLKGLSKAEAKRRADEWLERlgLGDRANKKVEE----LSKGNQ 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 479 QRISLARALLKNPSILILDDTTS-----AVDMetevkIQGELKKITENTTTfII--AHRISSVKE-ADEILILNHGEIIE 550
Cdd:COG4152  136 QKVQLIAALLHDPELLILDEPFSgldpvNVEL-----LKDVIRELAAKGTT-VIfsSHQMELVEElCDRIVIINKGRKVL 209

                 ...
gi 404223395 551 RGT 553
Cdd:COG4152  210 SGS 212
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
334-545 3.73e-17

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 81.31  E-value: 3.73e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFEddpNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILidgvdarkwHVRELRnhIA 413
Cdd:PRK09544   5 VSLENVSVSFG---QRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK---------RNGKLR--IG 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 414 TVMQDIFLfsdtiegniafgapDATME-DVRRMARI------AD---------ADHFIETMPESydtivgergvgLSGGQ 477
Cdd:PRK09544  71 YVPQKLYL--------------DTTLPlTVNRFLRLrpgtkkEDilpalkrvqAGHLIDAPMQK-----------LSGGE 125
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 404223395 478 KQRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITE--NTTTFIIAHRISSV-KEADEILILNH 545
Cdd:PRK09544 126 TQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRelDCAVLMVSHDLHLVmAKTDEVLCLNH 196
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
335-557 3.81e-17

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 82.83  E-value: 3.81e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 335 EFKNVSFHFE--DD-------PNT-DVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARK-- 402
Cdd:PRK15079  10 EVADLKVHFDikDGkqwfwqpPKTlKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGmk 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 403 ---WhvRELRNHIATVMQDIfLFS--------DTIEGNIAFGAPDATMEDVRR-----MARIADADHFIETMPESYdtiv 466
Cdd:PRK15079  90 ddeW--RAVRSDIQMIFQDP-LASlnprmtigEIIAEPLRTYHPKLSRQEVKDrvkamMLKVGLLPNLINRYPHEF---- 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 467 gergvglSGGQKQRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKIT-ENTTTFI-IAHRISSVKE-ADEILIL 543
Cdd:PRK15079 163 -------SGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQrEMGLSLIfIAHDLAVVKHiSDRVLVM 235
                        250
                 ....*....|....
gi 404223395 544 NHGEIIERGTHSSL 557
Cdd:PRK15079 236 YLGHAVELGTYDEV 249
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
352-504 4.04e-17

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 80.69  E-value: 4.04e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 352 LKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRE---LRNHIATVMQDIFLFSD-TIE 427
Cdd:PRK10908  18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQIGMIFQDHHLLMDrTVY 97
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 404223395 428 GNIAFG--APDATMEDVRRmaRIADADHFIETMPESYDTivgerGVGLSGGQKQRISLARALLKNPSILILDDTTSAVD 504
Cdd:PRK10908  98 DNVAIPliIAGASGDDIRR--RVSAALDKVGLLDKAKNF-----PIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLD 169
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
361-505 4.48e-17

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 83.00  E-value: 4.48e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 361 PGQTI-AILGETGAGKSTLVNLICRFYDPTSGEILIDG---VDARK--WHVRELRnHIATVMQDIFLFSD-TIEGNIAFG 433
Cdd:PRK11144  22 PAQGItAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlFDAEKgiCLPPEKR-RIGYVFQDARLFPHyKVRGNLRYG 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 434 apdatmedvrrMARiadadhfieTMPESYDTIVGERGVG---------LSGGQKQRISLARALLKNPSILILDDTTSAVD 504
Cdd:PRK11144 101 -----------MAK---------SMVAQFDKIVALLGIEplldrypgsLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160

                 .
gi 404223395 505 M 505
Cdd:PRK11144 161 L 161
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
350-550 6.38e-17

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


Pssm-ID: 443338 [Multi-domain]  Cd Length: 233  Bit Score: 80.17  E-value: 6.38e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 350 DVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVD---------ARkwhVRelRNHIATVMQDIF 420
Cdd:COG4181   26 TILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDlfaldedarAR---LR--ARHVGFVFQSFQ 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 421 LF-SDTIEGNIAFGAPDATMEDVRRMARIA--------DADHFietmPesydtivgergVGLSGGQKQRISLARALLKNP 491
Cdd:COG4181  101 LLpTLTALENVMLPLELAGRRDARARARALlervglghRLDHY----P-----------AQLSGGEQQRVALARAFATEP 165
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 404223395 492 SILILDDTTSAVDMETEVKIQG---ELKKiTENTTTFIIAHRISSVKEADEILILNHGEIIE 550
Cdd:COG4181  166 AILFADEPTGNLDAATGEQIIDllfELNR-ERGTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
352-564 7.27e-17

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


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 81.67  E-value: 7.27e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 352 LKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKwHVRELRNHIATVM----QdifLFSD--T 425
Cdd:COG4586   38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFK-RRKEFARRIGVVFgqrsQ---LWWDlpA 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 426 IEgniafgapdaTMEDVRRMARIADADhFIETMpesyDTIVGERGVG---------LSGGQKQRISLARALLKNPSILIL 496
Cdd:COG4586  114 ID----------SFRLLKAIYRIPDAE-YKKRL----DELVELLDLGelldtpvrqLSLGQRMRCELAAALLHRPKILFL 178
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 404223395 497 DDTTSAVDMETEVKIQGELKKI--TENTTTFIIAHRISSVKE-ADEILILNHGEIIERGTHSSLLAEKGYY 564
Cdd:COG4586  179 DEPTIGLDVVSKEAIREFLKEYnrERGTTILLTSHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKERFGPY 249
ABC_6TM_ATM1_ABCB7 cd18582
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ...
22-294 1.02e-16

Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1/ABCB7 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia.


Pssm-ID: 350026 [Multi-domain]  Cd Length: 292  Bit Score: 81.01  E-value: 1.02e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  22 FILIFIASGISIIYPLLGGKVIDDVvyqnkTNLLIPLLLIMIISTIIRTICRYTYQIMCE-------RIGQNSLFRIRED 94
Cdd:cd18582    2 LLLLVLAKLLNVAVPFLLKYAVDAL-----SAPASALLAVPLLLLLAYGLARILSSLFNElrdalfaRVSQRAVRRLALR 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  95 LYKKLQSLDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENVFLFSFAIIIMAAI-DWKLTLALVIVTPLIAILT 173
Cdd:cd18582   77 VFRHLHSLSLRFHLSRKTGALSRAIERGTRGIEFLLRFLLFNILPTILELLLVCGILWYLyGWSYALITLVTVALYVAFT 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 174 MKMSskaqpvfyEIRESFSRLNSMVEENISGNRV--------VKAFAREDFEMKKFHEHNEDFKKRNLDSAdVSRTYLPV 245
Cdd:cd18582  157 IKVT--------EWRTKFRREMNEADNEANAKAVdsllnyetVKYFNNEEYEAERYDKALAKYEKAAVKSQ-TSLALLNI 227
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 404223395 246 LDSL---AGMLVVitLIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPMRMSGW 294
Cdd:cd18582  228 GQALiisLGLTAI--MLLAAQGVVAGTLTVGDFVLVNTYLLQLYQPLNFLGF 277
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
338-559 1.16e-16

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


Pssm-ID: 443332 [Multi-domain]  Cd Length: 533  Bit Score: 83.20  E-value: 1.16e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 338 NVSFHfEDDPNTDVLKNISLKASPGQTIAILGETGAGKS----TLVNLICRFYDPTSGEILIDGVDARKWHVRELR---- 409
Cdd:COG4172   13 SVAFG-QGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRrirg 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 410 NHIAtvMqdIF---------LFsdTIEGNIAfgapdATMEDVRRMARIADADHFIETMPEsydtiVG----ERGVG---- 472
Cdd:COG4172   92 NRIA--M--IFqepmtslnpLH--TIGKQIA-----EVLRLHRGLSGAAARARALELLER-----VGipdpERRLDayph 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 473 -LSGGQKQRISLARALLKNPSILILDDTTSAVDmeteVKIQG-------ELKKiTENTTTFIIAHRISSVKE-ADEILIL 543
Cdd:COG4172  156 qLSGGQRQRVMIAMALANEPDLLIADEPTTALD----VTVQAqildllkDLQR-ELGMALLLITHDLGVVRRfADRVAVM 230
                        250
                 ....*....|....*.
gi 404223395 544 NHGEIIERGTHSSLLA 559
Cdd:COG4172  231 RQGEIVEQGPTAELFA 246
ABC_6TM_T1SS_like cd18555
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ...
15-303 1.85e-16

Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.


Pssm-ID: 349999 [Multi-domain]  Cd Length: 294  Bit Score: 80.25  E-value: 1.85e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  15 RLLMIGVFILIFIASGISIIYPLLGGKVIDDVVYQNKTNLLIPLLLIMIISTIIRTICRYTYQIMCERIgQNSL-FRIRE 93
Cdd:cd18555    1 KKLLISILLLSLLLQLLTLLIPILTQYVIDNVIVPGNLNLLNVLGIGILILFLLYGLFSFLRGYIIIKL-QTKLdKSLMS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  94 DLYKKLQSLDFDFFNNTRVGDIMARMtGDTDAIRHFVSWVSYNILENVFLFSFAIIIMAAIDWKLTLALVIVTPLIAILT 173
Cdd:cd18555   80 DFFEHLLKLPYSFFENRSSGDLLFRA-NSNVYIRQILSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLLL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 174 MKMSSKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSRTYLPVLDSLAGML 253
Cdd:cd18555  159 LLTRKKIKKLNQEEIVAQTKVQSYLTETLYGIETIKSLGSEKNIYKKWENLFKKQLKAFKKKERLSNILNSISSSIQFIA 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 404223395 254 VVITLIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPMrMSgwLINDVQRFI 303
Cdd:cd18555  239 PLLILWIGAYLVINGELTLGELIAFSSLAGSFLTPI-VS--LINSYNQFI 285
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
334-547 4.04e-16

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


Pssm-ID: 213188 [Multi-domain]  Cd Length: 144  Bit Score: 75.56  E-value: 4.04e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFEDDPntdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGvdarkwhvrelRNHIA 413
Cdd:cd03221    1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS-----------TVKIG 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 414 TVMQdiflfsdtiegniafgapdatmedvrrmariadadhfietmpesydtivgergvgLSGGQKQRISLARALLKNPSI 493
Cdd:cd03221   67 YFEQ-------------------------------------------------------LSGGEKMRLALAKLLLENPNL 91
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 404223395 494 LILDDTTSAVDMETEVKIQGELKKitENTTTFIIAH-R--ISSVkeADEILILNHGE 547
Cdd:cd03221   92 LLLDEPTNHLDLESIEALEEALKE--YPGTVILVSHdRyfLDQV--ATKIIELEDGK 144
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
350-549 4.42e-16

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 81.22  E-value: 4.42e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 350 DVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRE-LRNHIATVMQD-----IFLfS 423
Cdd:COG1129  266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDaIRAGIAYVPEDrkgegLVL-D 344
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 424 DTIEGNIAFgapdATMEDVRRMARI------ADADHFIETM---PESYDTIVGErgvgLSGGQKQRISLARALLKNPSIL 494
Cdd:COG1129  345 LSIRENITL----ASLDRLSRGGLLdrrrerALAEEYIKRLrikTPSPEQPVGN----LSGGNQQKVVLAKWLATDPKVL 416
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 404223395 495 ILDDTTSAVDMETEVKIQGELKKITENTTTFIIahrISSvkEADE-------ILILNHGEII 549
Cdd:COG1129  417 ILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIV---ISS--ELPEllglsdrILVMREGRIV 473
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
337-558 1.07e-15

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 77.52  E-value: 1.07e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 337 KNVSFHFeddPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIATVM 416
Cdd:PRK10575  15 RNVSFRV---PGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLP 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 417 QDIflfsdtiegniafgaPDATMEDVRR------------MARIADADHfiETMPESYdTIVG-----ERGV-GLSGGQK 478
Cdd:PRK10575  92 QQL---------------PAAEGMTVRElvaigrypwhgaLGRFGAADR--EKVEEAI-SLVGlkplaHRLVdSLSGGER 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 479 QRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIA--HRIS-SVKEADEILILNHGEIIERGTHS 555
Cdd:PRK10575 154 QRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAvlHDINmAARYCDYLVALRGGEMIAQGTPA 233

                 ...
gi 404223395 556 SLL 558
Cdd:PRK10575 234 ELM 236
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
351-552 1.54e-15

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


Pssm-ID: 213234 [Multi-domain]  Cd Length: 236  Bit Score: 76.22  E-value: 1.54e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 351 VLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNhIATVM-QDIFLFSDTiegn 429
Cdd:cd03267   36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRR-IGVVFgQKTQLWWDL---- 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 430 iafgAPDATMEDVRRMARIaDADHFIETMPESYDTIVGERGV-----GLSGGQKQRISLARALLKNPSILILDDTTSAVD 504
Cdd:cd03267  111 ----PVIDSFYLLAAIYDL-PPARFKKRLDELSELLDLEELLdtpvrQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLD 185
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 404223395 505 METEVKIQGELKKITENTTTFII--AHRISSV-KEADEILILNHGEIIERG 552
Cdd:cd03267  186 VVAQENIRNFLKEYNRERGTTVLltSHYMKDIeALARRVLVIDKGRLLYDG 236
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
334-549 2.02e-15

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


Pssm-ID: 131681 [Multi-domain]  Cd Length: 500  Bit Score: 79.10  E-value: 2.02e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  334 VEFKNVSFHFEDdpnTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFY--DPTSGEILIDGVDARKWHVREL-RN 410
Cdd:TIGR02633   2 LEMKGIVKTFGG---VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSPLKASNIRDTeRA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  411 HIATVMQDIFLFSD-TIEGNIAFG----APDATMEDVRRMARiadADHFIETMpeSYDTIVGERGVG-LSGGQKQRISLA 484
Cdd:TIGR02633  79 GIVIIHQELTLVPElSVAENIFLGneitLPGGRMAYNAMYLR---AKNLLREL--QLDADNVTRPVGdYGGGQQQLVEIA 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  485 RALLKNPSILILDDTTSAVdmeTEVKIQGELKKITE----NTTTFIIAHRISSVKE-ADEILILNHGEII 549
Cdd:TIGR02633 154 KALNKQARLLILDEPSSSL---TEKETEILLDIIRDlkahGVACVYISHKLNEVKAvCDTICVIRDGQHV 220
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
351-504 2.46e-15

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


Pssm-ID: 443809 [Multi-domain]  Cd Length: 229  Bit Score: 75.55  E-value: 2.46e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 351 VLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEIL-------IDGVDARKWHVRELRNH-IATVMQdiFLf 422
Cdd:COG4778   26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILvrhdggwVDLAQASPREILALRRRtIGYVSQ--FL- 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 423 sDTI----------EGNIAFGAPDATMED-VRRM-ARIAdadhfietmpesydtiVGERGVGL-----SGGQKQRISLAR 485
Cdd:COG4778  103 -RVIprvsaldvvaEPLLERGVDREEARArARELlARLN----------------LPERLWDLppatfSGGEQQRVNIAR 165
                        170
                 ....*....|....*....
gi 404223395 486 ALLKNPSILILDDTTSAVD 504
Cdd:COG4778  166 GFIADPPLLLLDEPTASLD 184
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
351-559 2.74e-15

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 76.29  E-value: 2.74e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 351 VLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSG-----EILIDGVDARKWH-VRELRNHIATVMQDIFLFSD 424
Cdd:PRK14271  36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRdVLEFRRRVGMLFQRPNPFPM 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 425 TIEGNIAFGAPDATMEDVRRMARIADADHFIETMPESYDTIVGERGVGLSGGQKQRISLARALLKNPSILILDDTTSAVD 504
Cdd:PRK14271 116 SIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALD 195
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 404223395 505 METEVKIQGELKKITENTTTFIIAHRIS-SVKEADEILILNHGEIIERGTHSSLLA 559
Cdd:PRK14271 196 PTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQLFS 251
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
305-561 6.86e-15

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 76.02  E-value: 6.86e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 305 SSFKIQDMMATDAKIPIHAEKPAPSlqghVEFKNVSFHFEDDPntdVLKNISLKASPGQTIAILGETGAGKSTLVNLICR 384
Cdd:PRK13536  17 SPIERKHQGISEAKASIPGSMSTVA----IDLAGVSKSYGDKA---VVNGLSFTVASGECFGLLGPNGAGKSTIARMILG 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 385 FYDPTSGEILIDGVDARKwHVRELRNHIATVMQ-DIFLFSDTIEGNIA-----FGAPDATMEDV-------RRMARIADA 451
Cdd:PRK13536  90 MTSPDAGKITVLGVPVPA-RARLARARIGVVPQfDNLDLEFTVRENLLvfgryFGMSTREIEAVipsllefARLESKADA 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 452 dhfietmpesydtivgeRGVGLSGGQKQRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHRI 531
Cdd:PRK13536 169 -----------------RVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHF 231
                        250       260       270
                 ....*....|....*....|....*....|..
gi 404223395 532 SSVKE--ADEILILNHGEIIERGTHSSLLAEK 561
Cdd:PRK13536 232 MEEAErlCDRLCVLEAGRKIAEGRPHALIDEH 263
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
351-504 8.87e-15

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 73.37  E-value: 8.87e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 351 VLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIATvmQDIFLFSDTIEGNI 430
Cdd:PRK13539  17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLGH--RNAMKPALTVAENL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 431 AF---------GAPDATMEDVrRMARIADadhfietMPESYdtivgergvgLSGGQKQRISLARALLKNPSILILDDTTS 501
Cdd:PRK13539  95 EFwaaflggeeLDIAAALEAV-GLAPLAH-------LPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPTA 156

                 ...
gi 404223395 502 AVD 504
Cdd:PRK13539 157 ALD 159
PRK10522 PRK10522
multidrug transporter membrane component/ATP-binding component; Provisional
334-550 1.14e-14

multidrug transporter membrane component/ATP-binding component; Provisional


Pssm-ID: 236707 [Multi-domain]  Cd Length: 547  Bit Score: 76.93  E-value: 1.14e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFEDdpNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDG--VDARKWHvrELRNH 411
Cdd:PRK10522 323 LELRNVTFAYQD--NGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGkpVTAEQPE--DYRKL 398
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 412 IATVMQDIFLFSDTIEgniafgaPDATMEDVrrmariADADHFIETMP-ESYDTIVGER--GVGLSGGQKQRISLARALL 488
Cdd:PRK10522 399 FSAVFTDFHLFDQLLG-------PEGKPANP------ALVEKWLERLKmAHKLELEDGRisNLKLSKGQKKRLALLLALA 465
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 404223395 489 KNPSILILDDTtsAVDME------------TEVKIQGElkkitentTTFIIAHRISSVKEADEILILNHGEIIE 550
Cdd:PRK10522 466 EERDILLLDEW--AADQDphfrrefyqvllPLLQEMGK--------TIFAISHDDHYFIHADRLLEMRNGQLSE 529
PLN03211 PLN03211
ABC transporter G-25; Provisional
351-566 1.67e-14

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 76.46  E-value: 1.67e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 351 VLKNISLKASPGQTIAILGETGAGKSTLVNLIC-RFYDPT-SGEILIDGvdaRKwHVRELRNHIATVMQDIFLFSD-TIE 427
Cdd:PLN03211  83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgRIQGNNfTGTILANN---RK-PTKQILKRTGFVTQDDILYPHlTVR 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 428 GNIAFGAPDATMEDVRRMARIADADHFIETM--PESYDTIVGERGV-GLSGGQKQRISLARALLKNPSILILDDTTSAVD 504
Cdd:PLN03211 159 ETLVFCSLLRLPKSLTKQEKILVAESVISELglTKCENTIIGNSFIrGISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 404223395 505 METEVKIQGELKKITENTTTFIIA-HRISS--VKEADEILILNHGEIIERGTHSSLLAekgyYFD 566
Cdd:PLN03211 239 ATAAYRLVLTLGSLAQKGKTIVTSmHQPSSrvYQMFDSVLVLSEGRCLFFGKGSDAMA----YFE 299
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
351-559 1.89e-14

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 76.28  E-value: 1.89e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 351 VLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYdPT------SGEILIDG---VDARKWHVRELR-NHIATVMQDIF 420
Cdd:PRK15134  24 VVNDVSLQIEAGETLALVGESGSGKSVTALSILRLL-PSppvvypSGDIRFHGeslLHASEQTLRGVRgNKIAMIFQEPM 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 421 LFSD---TIEGNIAfgapdatmeDV----RRMARIADADHFIETMPEsydtiVGERGVG---------LSGGQKQRISLA 484
Cdd:PRK15134 103 VSLNplhTLEKQLY---------EVlslhRGMRREAARGEILNCLDR-----VGIRQAAkrltdyphqLSGGERQRVMIA 168
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 404223395 485 RALLKNPSILILDDTTSAVDMETEVKIQGELKKITE--NTTTFIIAHRISSVKE-ADEILILNHGEIIERGTHSSLLA 559
Cdd:PRK15134 169 MALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKlADRVAVMQNGRCVEQNRAATLFS 246
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
351-552 2.81e-14

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 73.10  E-value: 2.81e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 351 VLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIATVMQDIFLFSD-TIEGN 429
Cdd:PRK10253  22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDiTVQEL 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 430 IAFGA-PDATM------EDVRRMARIADADHFIETMPESYDTivgergvgLSGGQKQRISLARALLKNPSILILDDTTSA 502
Cdd:PRK10253 102 VARGRyPHQPLftrwrkEDEEAVTKAMQATGITHLADQSVDT--------LSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 404223395 503 VDMETEVKIQGELKKI--TENTTTFIIAHRIS-SVKEADEILILNHGEIIERG 552
Cdd:PRK10253 174 LDISHQIDLLELLSELnrEKGYTLAAVLHDLNqACRYASHLIALREGKIVAQG 226
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
351-548 4.02e-14

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 75.09  E-value: 4.02e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 351 VLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGvdARKWHVRELRNH---IATVMQDIFLFSD-TI 426
Cdd:PRK15439  26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGG--NPCARLTPAKAHqlgIYLVPQEPLLFPNlSV 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 427 EGNIAFGAPdATMEDVRRMARIADA--DHFIETMPESydtivgergvGLSGGQKQRISLARALLKNPSILILDDTTSAVD 504
Cdd:PRK15439 104 KENILFGLP-KRQASMQKMKQLLAAlgCQLDLDSSAG----------SLEVADRQIVEILRGLMRDSRILILDEPTASLT 172
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 404223395 505 -METE---VKIQGELKKiteNTTTFIIAHRISSVKE-ADEILILNHGEI 548
Cdd:PRK15439 173 pAETErlfSRIRELLAQ---GVGIVFISHKLPEIRQlADRISVMRDGTI 218
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
334-546 4.45e-14

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 74.82  E-value: 4.45e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFeddPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKW-HVRELRNHI 412
Cdd:PRK09700   6 ISMAGIGKSF---GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLdHKLAAQLGI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 413 ATVMQDIFLFSD-TIEGNI---------AFGAPdatMEDVRRMARIADADHFIETMPESYDTIVGErgvgLSGGQKQRIS 482
Cdd:PRK09700  83 GIIYQELSVIDElTVLENLyigrhltkkVCGVN---IIDWREMRVRAAMMLLRVGLKVDLDEKVAN----LSISHKQMLE 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 404223395 483 LARALLKNPSILILDD-TTSAVDMETE--VKIQGELKKitENTTTFIIAHRISSVKE-ADEILILNHG 546
Cdd:PRK09700 156 IAKTLMLDAKVIIMDEpTSSLTNKEVDylFLIMNQLRK--EGTAIVYISHKLAEIRRiCDRYTVMKDG 221
ABC_6TM_PrtD_LapB_HlyB_like cd18566
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ...
90-294 6.13e-14

Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.


Pssm-ID: 350010 [Multi-domain]  Cd Length: 294  Bit Score: 72.62  E-value: 6.13e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  90 RIREDLYKKLQSLDFDFFNNTRVGDIMARMTgDTDAIRHFVSWVSYN-ILENVFLFSFaIIIMAAIDWKLTLALVIVTPL 168
Cdd:cd18566   76 RLSNAAFEHLLSLPLSFFEREPSGAHLERLN-SLEQIREFLTGQALLaLLDLPFVLIF-LGLIWYLGGKLVLVPLVLLGL 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 169 IAILTMKMSSKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSRTYLPVLDS 248
Cdd:cd18566  154 FVLVAILLGPILRRALKERSRADERRQNFLIETLTGIHTIKAMAMEPQMLRRYERLQANAAYAGFKVAKINAVAQTLGQL 233
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 404223395 249 LAGMLVVITLIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPMR--MSGW 294
Cdd:cd18566  234 FSQVSMVAVVAFGALLVINGDLTVGALIACTMLSGRVLQPLQraFGLW 281
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
334-553 1.05e-13

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


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 72.57  E-value: 1.05e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFedDPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDarkwhVREL----R 409
Cdd:PRK11650   4 LKLQAVRKSY--DGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRV-----VNELepadR 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 410 NhIATVMQDIFLFSD-TIEGNIAFGAPDATMEDVRRMARIADA------DHFIETMPESydtivgergvgLSGGQKQRIS 482
Cdd:PRK11650  77 D-IAMVFQNYALYPHmSVRENMAYGLKIRGMPKAEIEERVAEAarilelEPLLDRKPRE-----------LSGGQRQRVA 144
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 404223395 483 LARALLKNPSILILDDTTSAVDMETEVKIQGELKKITE--NTTTFIIAH-RISSVKEADEILILNHGEIIERGT 553
Cdd:PRK11650 145 MGRAIVREPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRrlKTTSLYVTHdQVEAMTLADRVVVMNGGVAEQIGT 218
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
334-557 1.14e-13

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 71.33  E-value: 1.14e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFEDDPntdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDA---RKWHVRELRN 410
Cdd:PRK11831   8 VDMRGVSFTRGNRC---IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamSRSRLYTVRK 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 411 HIATVMQDIFLFSD-TIEGNIAFgapdatmeDVRRMARIADAdhFIETMPESYDTIVGERGVG------LSGGQKQRISL 483
Cdd:PRK11831  85 RMSMLFQSGALFTDmNVFDNVAY--------PLREHTQLPAP--LLHSTVMMKLEAVGLRGAAklmpseLSGGMARRAAL 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 404223395 484 ARALLKNPSILILDDTTSAVD---METEVKIQGELKKiTENTTTFIIAHRISSVKE-ADEILILNHGEIIERGTHSSL 557
Cdd:PRK11831 155 ARAIALEPDLIMFDEPFVGQDpitMGVLVKLISELNS-ALGVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQAL 231
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
354-553 1.54e-13

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


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 70.79  E-value: 1.54e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 354 NISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVD---------ARK------WHVRELRNHIAT---- 414
Cdd:PRK11300  23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHieglpghqiARMgvvrtfQHVRLFREMTVIenll 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 415 VMQDIFLFSDTIEGniAFGAPdatmeDVRRMAR--IADADHFIETMPEsydTIVGERGVG-LSGGQKQRISLARALLKNP 491
Cdd:PRK11300 103 VAQHQQLKTGLFSG--LLKTP-----AFRRAESeaLDRAATWLERVGL---LEHANRQAGnLAYGQQRRLEIARCMVTQP 172
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 492 SILILDDTTSAVD-METEvkiqgELKK-ITE-----NTTTFIIAHRISSVKE-ADEILILNHGEIIERGT 553
Cdd:PRK11300 173 EILMLDEPAAGLNpKETK-----ELDElIAElrnehNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGT 237
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
351-559 1.62e-13

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


Pssm-ID: 440752 [Multi-domain]  Cd Length: 240  Bit Score: 70.44  E-value: 1.62e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 351 VLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKW--HVRElRNHIATVMQD--IF--Lfsd 424
Cdd:COG1137   18 VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLpmHKRA-RLGIGYLPQEasIFrkL--- 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 425 TIEGNIAfgapdATME--DVRRMARIADADHFIEtmpE-SYDTIVGERGVGLSGGQKQRISLARALLKNPSILILDDTTS 501
Cdd:COG1137   94 TVEDNIL-----AVLElrKLSKKEREERLEELLE---EfGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFA 165
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 404223395 502 AVDMETEVKIQG---ELKK------ITEntttfiiaHrisSVKEADEIL----ILNHGEIIERGTHSSLLA 559
Cdd:COG1137  166 GVDPIAVADIQKiirHLKErgigvlITD--------H---NVRETLGICdrayIISEGKVLAEGTPEEILN 225
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
336-549 1.87e-13

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


Pssm-ID: 213200 [Multi-domain]  Cd Length: 202  Bit Score: 69.21  E-value: 1.87e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 336 FKNVSFHF-EDDPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLIC---RFYDPTSGEILIDGVDARKWHVRELRNH 411
Cdd:cd03233    6 WRNISFTTgKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALAnrtEGNVSVEGDIHYNGIPYKEFAEKYPGEI 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 412 IATVMQDIFLFSDTIEgniafgapdATMEDVRRMariaDADHFIetmpesydtivgeRGVglSGGQKQRISLARALLKNP 491
Cdd:cd03233   86 IYVSEEDVHFPTLTVR---------ETLDFALRC----KGNEFV-------------RGI--SGGERKRVSIAEALVSRA 137
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 404223395 492 SILILDDTTSAVDMETEVKIQGELKKIT--ENTTTFIIAHRISS--VKEADEILILNHGEII 549
Cdd:cd03233  138 SVLCWDNSTRGLDSSTALEILKCIRTMAdvLKTTTFVSLYQASDeiYDLFDKVLVLYEGRQI 199
ycf16 CHL00131
sulfate ABC transporter protein; Validated
348-563 1.90e-13

sulfate ABC transporter protein; Validated


Pssm-ID: 214372 [Multi-domain]  Cd Length: 252  Bit Score: 70.44  E-value: 1.90e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 348 NTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRF--YDPTSGEILIDGVDARKWHVrELRNHIAtvmqdIFL-FSD 424
Cdd:CHL00131  19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEP-EERAHLG-----IFLaFQY 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 425 TIEgniafgAPDATMEDVRRMARIA----------DADHFIETMPESYDtIVG------ERGV--GLSGGQKQRISLARA 486
Cdd:CHL00131  93 PIE------IPGVSNADFLRLAYNSkrkfqglpelDPLEFLEIINEKLK-LVGmdpsflSRNVneGFSGGEKKRNEILQM 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 487 LLKNPSILILDDTTSAVDMETEVKIQGELKKI-TENTTTFIIAH--RISSVKEADEILILNHGEIIERGTHS--SLLAEK 561
Cdd:CHL00131 166 ALLDSELAILDETDSGLDIDALKIIAEGINKLmTSENSIILITHyqRLLDYIKPDYVHVMQNGKIIKTGDAElaKELEKK 245

                 ..
gi 404223395 562 GY 563
Cdd:CHL00131 246 GY 247
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
354-560 2.46e-13

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


Pssm-ID: 132313 [Multi-domain]  Cd Length: 520  Bit Score: 72.53  E-value: 2.46e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  354 NISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILI----DGVDARKWHVRE---LRNHIATVMQDIFLFSD-T 425
Cdd:TIGR03269 302 NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGPDGrgrAKRYIGILHQEYDLYPHrT 381
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  426 IEGN----IAFGAPD--ATMEDVRRMARIA-DADHFIETMPESYDTivgergvgLSGGQKQRISLARALLKNPSILILDD 498
Cdd:TIGR03269 382 VLDNlteaIGLELPDelARMKAVITLKMVGfDEEKAEEILDKYPDE--------LSEGERHRVALAQVLIKEPRIVILDE 453
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 404223395  499 TTSAVDMETEVKIQGELKKITE--NTTTFIIAHRISSVKE-ADEILILNHGEIIERGTHSSLLAE 560
Cdd:TIGR03269 454 PTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIVEE 518
ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 cd18560
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ...
22-282 2.63e-13

Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group represents the Atm1/ABCB7/HMT1/ABCB6 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia. ABCB6 is originally identified as a porphyrin transporter present in the outer membrane of mitochondria. It is highly expressed in cells resistance to arsenic and protects against arsenic cytotoxicity. Moreover, Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster.


Pssm-ID: 350004 [Multi-domain]  Cd Length: 292  Bit Score: 70.72  E-value: 2.63e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  22 FILIFIASGISIIYPLLGGKVIDDVVY--QNKTNLLIPLLLIMIISTIIRTICRYTYQIMCERIGQNSLFRIREDLYKKL 99
Cdd:cd18560    2 LLLLILGKACNVLAPLFLGRAVNALTLakVKDLESAVTLILLYALLRFSSKLLKELRSLLYRRVQQNAYRELSLKTFAHL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 100 QSLDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENVFLFSFAIIIMAAI-DWKLTLALVIVTPLIAILTMKMSs 178
Cdd:cd18560   82 HSLSLDWHLSKKTGEVVRIMDRGTESANTLLSYLVFYLVPTLLELIVVSVVFAFHfGAWLALIVFLSVLLYGVFTIKVT- 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 179 kaqpvfyEIRESFSRLnSMVEENISGNRV---------VKAFAREDFEMKKFHEHNEDFKKRNLdSADVSRTYLPVLDSL 249
Cdd:cd18560  161 -------EWRTKFRRA-ANKKDNEAHDIAvdsllnfetVKYFTNEKYEVDRYGEAVKEYQKSSV-KVQASLSLLNVGQQL 231
                        250       260       270
                 ....*....|....*....|....*....|....
gi 404223395 250 A-GMLVVITLIFGGYLVIKGQMTLGDLVAFNGFL 282
Cdd:cd18560  232 IiQLGLTLGLLLAGYRVVDGGLSVGDFVAVNTYI 265
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
352-552 5.82e-13

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 71.81  E-value: 5.82e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 352 LKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEIL-----IDGVDARKwhVRELRNHIATVMQDIFLfsdTI 426
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIfngqrIDTLSPGK--LQALRRDIQFIFQDPYA---SL 414
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 427 EGNIAFGapDATMEDVR---------RMARIADADHFIETMPESYDTIVGErgvgLSGGQKQRISLARALLKNPSILILD 497
Cdd:PRK10261 415 DPRQTVG--DSIMEPLRvhgllpgkaAAARVAWLLERVGLLPEHAWRYPHE----FSGGQRQRICIARALALNPKVIIAD 488
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 404223395 498 DTTSAVDMETEVKIQGELKKITEN--TTTFIIAHRISSVKE-ADEILILNHGEIIERG 552
Cdd:PRK10261 489 EAVSALDVSIRGQIINLLLDLQRDfgIAYLFISHDMAVVERiSHRVAVMYLGQIVEIG 546
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
352-560 7.88e-13

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 69.14  E-value: 7.88e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 352 LKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKwhvrELR-NHIATVMQdiflfSDTIEGNI 430
Cdd:PRK15056  23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ----ALQkNLVAYVPQ-----SEEVDWSF 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 431 AfgapdATMEDVRRMAR--------IADA-DHFIET-------MPESYDTIVGErgvgLSGGQKQRISLARALLKNPSIL 494
Cdd:PRK15056  94 P-----VLVEDVVMMGRyghmgwlrRAKKrDRQIVTaalarvdMVEFRHRQIGE----LSGGQKKRVFLARAIAQQGQVI 164
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 404223395 495 ILDDTTSAVDMETEVKIQGELKKI-TENTTTFIIAHRISSVKEADEILILNHGEIIERG-THSSLLAE 560
Cdd:PRK15056 165 LLDEPFTGVDVKTEARIISLLRELrDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGpTETTFTAE 232
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
347-561 8.80e-13

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


Pssm-ID: 274744 [Multi-domain]  Cd Length: 552  Bit Score: 70.73  E-value: 8.80e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  347 PNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILI-DGV-----------DARKwHVRElrnhiaT 414
Cdd:TIGR03719  16 PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPqPGIkvgylpqepqlDPTK-TVRE------N 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  415 VMQDIFLFSDTI----EGNIAFGAPDATMEDV-RRMARI------ADA---DHFIETMPES-----YDTIVGErgvgLSG 475
Cdd:TIGR03719  89 VEEGVAEIKDALdrfnEISAKYAEPDADFDKLaAEQAELqeiidaADAwdlDSQLEIAMDAlrcppWDADVTK----LSG 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  476 GQKQRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITenTTTFIIAH-RISSVKEADEILILNHGEIIE-RGT 553
Cdd:TIGR03719 165 GERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYP--GTVVAVTHdRYFLDNVAGWILELDRGRGIPwEGN 242

                  ....*...
gi 404223395  554 HSSLLAEK 561
Cdd:TIGR03719 243 YSSWLEQK 250
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
328-559 9.88e-13

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 69.06  E-value: 9.88e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 328 PSLQGHVEFKNVSFHFEDdpnTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGvDARKWHVRE 407
Cdd:PRK13537   2 PMSVAPIDFRNVEKRYGD---KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCG-EPVPSRARH 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 408 LRNHIATVMQDIFLFSD-TIEGNIA-----FGAPDATMEdvrrmARIADADHFIEtMPESYDTIVGErgvgLSGGQKQRI 481
Cdd:PRK13537  78 ARQRVGVVPQFDNLDPDfTVRENLLvfgryFGLSAAAAR-----ALVPPLLEFAK-LENKADAKVGE----LSGGMKRRL 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 482 SLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHRISSVKE--ADEILILNHGEIIERGTHSSLLA 559
Cdd:PRK13537 148 TLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAErlCDRLCVIEEGRKIAEGAPHALIE 227
BtuD COG4138
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ...
352-561 2.26e-12

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


Pssm-ID: 443313 [Multi-domain]  Cd Length: 248  Bit Score: 67.17  E-value: 2.26e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 352 LKNISLKASPGQTIAILGETGAGKSTLVNLICRFYdPTSGEILIDGVDARKWHVRELRNHIATVMQ--------DIFLFs 423
Cdd:COG4138   12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELARHRAYLSQqqsppfamPVFQY- 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 424 dtiegnIAFGAPDATMEDV--RRMARIADADHFIETMPesydtivgeRGVG-LSGGQKQRISLARALLK-----NPS--I 493
Cdd:COG4138   90 ------LALHQPAGASSEAveQLLAQLAEALGLEDKLS---------RPLTqLSGGEWQRVRLAAVLLQvwptiNPEgqL 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 494 LILDDTTSAVDMETEVKIQGELKKITENTTTFII-AHRIS-SVKEADEILILNHGEIIERGTHSSLLAEK 561
Cdd:COG4138  155 LLLDEPMNSLDVAQQAALDRLLRELCQQGITVVMsSHDLNhTLRHADRVWLLKQGKLVASGETAEVMTPE 224
ABC_6TM_PrtD_LapB_HlyB_like cd18783
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ...
15-300 2.30e-12

uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.


Pssm-ID: 350056 [Multi-domain]  Cd Length: 294  Bit Score: 67.93  E-value: 2.30e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  15 RLLMIGVFILIFIASGISIIYPLLGGKVIDDVVYQNKTNLLIPLLLIMIISTIIRTICRYTYQIMCERIGQNSLFRIRED 94
Cdd:cd18783    1 KRLFRDVAIASLILHVLALAPPIFFQIVIDKVLVHQSYSTLYVLTIGVVIALLFEGILGYLRRYLLLVATTRIDARLALR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  95 LYKKLQSLDFDFFNNTRVGDIMARMtGDTDAIRHFVSwvsyNILENVFLFSFAII----IMAAIDWKLT---LALVIVTP 167
Cdd:cd18783   81 TFDRLLSLPIDFFERTPAGVLTKHM-QQIERIRQFLT----GQLFGTLLDATSLLvflpVLFFYSPTLAlvvLAFSALIA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 168 LIAILTMKMSSKAQPVFYeiRESFSRlNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSRTYLPVLD 247
Cdd:cd18783  156 LIILAFLPPFRRRLQALY--RAEGER-QAFLVETVHGIRTVKSLALEPRQRREWDERVARAIRARFAVGRLSNWPQTLTG 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 404223395 248 SLAGMLVVITLIFGGYLVIKGQMTLGDLVAFNgflwMLNGpmRMSGWLINDVQ 300
Cdd:cd18783  233 PLEKLMTVGVIWVGAYLVFAGSLTVGALIAFN----MLAG--RVAGPLVQLAG 279
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
351-561 3.74e-12

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 66.46  E-value: 3.74e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 351 VLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDAR--KWHVRELRNhIATVMQDIFLFSD-TIE 427
Cdd:PRK10895  18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllPLHARARRG-IGYLPQEASIFRRlSVY 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 428 GNIAfgAPDATMEDVRRMARIADADHFIETMPESYdtIVGERGVGLSGGQKQRISLARALLKNPSILILDDTTSAVDMET 507
Cdd:PRK10895  97 DNLM--AVLQIRDDLSAEQREDRANELMEEFHIEH--LRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPIS 172
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 508 EVKIqgelKKITENTT-----TFIIAHRI-SSVKEADEILILNHGEIIERGTHSSLLAEK 561
Cdd:PRK10895 173 VIDI----KRIIEHLRdsglgVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQDE 228
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
351-550 4.17e-12

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 65.96  E-value: 4.17e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 351 VLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVR---ELR-NHIATVMQDiFLFSDTI 426
Cdd:PRK10584  25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEaraKLRaKHVGFVFQS-FMLIPTL 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 427 EgniafgapdaTMEDVRRMARIADadhfiETMPESYD---TIVGERGVG---------LSGGQKQRISLARALLKNPSIL 494
Cdd:PRK10584 104 N----------ALENVELPALLRG-----ESSRQSRNgakALLEQLGLGkrldhlpaqLSGGEQQRVALARAFNGRPDVL 168
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 404223395 495 ILDDTTSAVDMETEVKIQGELKKITEN--TTTFIIAHRISSVKEADEILILNHGEIIE 550
Cdd:PRK10584 169 FADEPTGNLDRQTGDKIADLLFSLNREhgTTLILVTHDLQLAARCDRRLRLVNGQLQE 226
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
347-549 5.95e-12

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 68.11  E-value: 5.95e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 347 PNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNH-IATVMQDIFLFSD- 424
Cdd:PRK10762  15 PGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAgIGIIHQELNLIPQl 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 425 TIEGNIAFGapdatMEDVRRMARI------ADADHFIETM--PESYDTIVGErgvgLSGGQKQRISLARALLKNPSILIL 496
Cdd:PRK10762  95 TIAENIFLG-----REFVNRFGRIdwkkmyAEADKLLARLnlRFSSDKLVGE----LSIGEQQMVEIAKVLSFESKVIIM 165
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 404223395 497 DDTTSAV-DMETE--VKIQGELKkiTENTTTFIIAHRISSVKE-ADEILILNHGEII 549
Cdd:PRK10762 166 DEPTDALtDTETEslFRVIRELK--SQGRGIVYISHRLKEIFEiCDDVTVFRDGQFI 220
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
348-552 6.92e-12

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 66.02  E-value: 6.92e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 348 NTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYD-----PTSGEILIDGVDARKWHVR--ELRNHIATVMQDIF 420
Cdd:PRK14267  16 SNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSPDVDpiEVRREVGMVFQYPN 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 421 LFSD-TIEGNIAFGAPDATMEDVRRmariaDADHFIE------TMPESYDTIVGERGVGLSGGQKQRISLARALLKNPSI 493
Cdd:PRK14267  96 PFPHlTIYDNVAIGVKLNGLVKSKK-----ELDERVEwalkkaALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKI 170
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 494 LILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHR-ISSVKEADEILILNHGEIIERG 552
Cdd:PRK14267 171 LLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVG 230
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
312-495 1.49e-11

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 66.97  E-value: 1.49e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 312 MMATDAKIPIHAEKPAPslqGHV--EFKNVSFHfeDDPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPT 389
Cdd:COG3845  237 MVGREVLLRVEKAPAEP---GEVvlEVENLSVR--DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPA 311
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 390 SGEILIDGVDARKWHVRELRNH-IATVMQD---IFLFSD-TIEGNIAFGAPDAT------MEDVRRMAriADADHFIETM 458
Cdd:COG3845  312 SGSIRLDGEDITGLSPRERRRLgVAYIPEDrlgRGLVPDmSVAENLILGRYRRPpfsrggFLDRKAIR--AFAEELIEEF 389
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 404223395 459 ---PESYDTIVGergvGLSGGQKQRISLARALLKNPSILI 495
Cdd:COG3845  390 dvrTPGPDTPAR----SLSGGNQQKVILARELSRDPKLLI 425
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
341-552 1.80e-11

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


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 67.44  E-value: 1.80e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395   341 FHFEDDPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLIC----RFYDPTSGEILIDGVDAR--KWHVR-------E 407
Cdd:TIGR00956   66 KKFRDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEeiKKHYRgdvvynaE 145
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395   408 LRNHIA--TVmqdiflfSDTIEGNIAFGAPDATMEDVRRMARIADADHFIET---MPESYDTIVGERGV-GLSGGQKQRI 481
Cdd:TIGR00956  146 TDVHFPhlTV-------GETLDFAARCKTPQNRPDGVSREEYAKHIADVYMAtygLSHTRNTKVGNDFVrGVSGGERKRV 218
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 404223395   482 SLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITE--NTTTFIIAHRISsvKEA----DEILILNHGEIIERG 552
Cdd:TIGR00956  219 SIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANilDTTPLVAIYQCS--QDAyelfDKVIVLYEGYQIYFG 293
ABC_6TM_CvaB_RaxB_like cd18567
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ...
21-278 2.86e-11

Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium.


Pssm-ID: 350011 [Multi-domain]  Cd Length: 294  Bit Score: 64.40  E-value: 2.86e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  21 VFILIFIASGISIIYPLLGGKVIDDVVYQNKTNLLIPLLLIMIISTIIRTICRYTYQIMCERIGQNSLFRIREDLYKKLQ 100
Cdd:cd18567    7 ILLLSLALELFALASPLYLQLVIDEVIVSGDRDLLTVLAIGFGLLLLLQALLSALRSWLVLYLSTSLNLQWTSNLFRHLL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 101 SLDFDFFNNTRVGDIMARMtGDTDAIRHFVSWVSYNILENVFLFSFAIIIMAAIDWKLTLALVIVTPLIAIL------TM 174
Cdd:cd18567   87 RLPLSYFEKRHLGDIVSRF-GSLDEIQQTLTTGFVEALLDGLMAILTLVMMFLYSPKLALIVLAAVALYALLrlalypPL 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 175 KMSSKAQpvfyeIRESfSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSRTYLPVLDSLAGMLV 254
Cdd:cd18567  166 RRATEEQ-----IVAS-AKEQSHFLETIRGIQTIKLFGREAEREARWLNLLVDAINADIRLQRLQILFSAANGLLFGLEN 239
                        250       260
                 ....*....|....*....|....
gi 404223395 255 VITLIFGGYLVIKGQMTLGDLVAF 278
Cdd:cd18567  240 ILVIYLGALLVLDGEFTVGMLFAF 263
ABCG_PDR_domain2 cd03232
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...
336-546 2.94e-11

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


Pssm-ID: 213199 [Multi-domain]  Cd Length: 192  Bit Score: 62.65  E-value: 2.94e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 336 FKNVSFHFeDDPNTD--VLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDP--TSGEILIDGVDARKwhvrELRNH 411
Cdd:cd03232    6 WKNLNYTV-PVKGGKrqLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAgvITGEILINGRPLDK----NFQRS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 412 IATVMQ-DIFLFSDTIEGNIAFGApdatmeDVRrmariadadhfietmpesydtivgergvGLSGGQKQRISLARALLKN 490
Cdd:cd03232   81 TGYVEQqDVHSPNLTVREALRFSA------LLR----------------------------GLSVEQRKRLTIGVELAAK 126
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 404223395 491 PSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIA-HRISSV--KEADEILILNHG 546
Cdd:cd03232  127 PSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTiHQPSASifEKFDRLLLLKRG 185
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
344-550 4.88e-11

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


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 62.67  E-value: 4.88e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 344 EDDPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIAtvmqdiflfs 423
Cdd:COG2401   38 LRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQFGREASLIDAIG---------- 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 424 dtiegniAFGAPDATMEdVRRMARIADADHFIETMPEsydtivgergvgLSGGQKQRISLARALLKNPSILILDDTTSAV 503
Cdd:COG2401  108 -------RKGDFKDAVE-LLNAVGLSDAVLWLRRFKE------------LSTGQKFRFRLALLLAERPKLLVIDEFCSHL 167
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 404223395 504 DMETEVKIQGELKKIT-ENTTTFIIAHRISSVKEA---DEILILNHGEIIE 550
Cdd:COG2401  168 DRQTAKRVARNLQKLArRAGITLVVATHHYDVIDDlqpDLLIFVGYGGVPE 218
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
351-515 7.99e-11

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


Pssm-ID: 213198 [Multi-domain]  Cd Length: 201  Bit Score: 61.74  E-value: 7.99e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 351 VLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGvdarkwhvrelrnhiatvmQDIFLFSDTIEGNI 430
Cdd:cd03231   15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNG-------------------GPLDFQRDSIARGL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 431 AFGAPDATME---DVRRMARIADADHFIETMPESYDTiVGERGVG------LSGGQKQRISLARALLKNPSILILDDTTS 501
Cdd:cd03231   76 LYLGHAPGIKttlSVLENLRFWHADHSDEQVEEALAR-VGLNGFEdrpvaqLSAGQQRRVALARLLLSGRPLWILDEPTT 154
                        170
                 ....*....|....
gi 404223395 502 AVDMETEVKIQGEL 515
Cdd:cd03231  155 ALDKAGVARFAEAM 168
sufC PRK09580
cysteine desulfurase ATPase component; Reviewed
334-563 9.46e-11

cysteine desulfurase ATPase component; Reviewed


Pssm-ID: 181965 [Multi-domain]  Cd Length: 248  Bit Score: 62.50  E-value: 9.46e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFEDDPntdVLKNISLKASPGQTIAILGETGAGKSTLVNLIC--RFYDPTSGEILIDGVDARKWHVRELRNh 411
Cdd:PRK09580   2 LSIKDLHVSVEDKA---ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDLLELSPEDRAG- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 412 iatvmQDIFL-FSDTIE----GNIAFgaPDATMEDVRRMARIADADHF-----IE------TMPEsyDTIVGERGVGLSG 475
Cdd:PRK09580  78 -----EGIFMaFQYPVEipgvSNQFF--LQTALNAVRSYRGQEPLDRFdfqdlMEekiallKMPE--DLLTRSVNVGFSG 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 476 GQKQRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIA---HRISSVKEADEILILNHGEIIERG 552
Cdd:PRK09580 149 GEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVthyQRILDYIKPDYVHVLYQGRIVKSG 228
                        250
                 ....*....|...
gi 404223395 553 THSSL--LAEKGY 563
Cdd:PRK09580 229 DFTLVkqLEEQGY 241
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
351-568 1.01e-10

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


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 64.74  E-value: 1.01e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395   351 VLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDP---TSGEILIDGVDARKWHVRElrnhIATVMQ-DIFLFSDTI 426
Cdd:TIGR00956  778 ILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGRPLDSSFQRS----IGYVQQqDLHLPTSTV 853
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395   427 EGNIAFGAPdatmedVRRMARIADA------DHFIETMP-ESY-DTIVGERGVGLSGGQKQRISLARALLKNPSILI-LD 497
Cdd:TIGR00956  854 RESLRFSAY------LRQPKSVSKSekmeyvEEVIKLLEmESYaDAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLD 927
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 404223395   498 DTTSAVDMETEVKIQGELKKITENTTTFIIA-HRISSV--KEADEILILNHG-EII---ERGTHSSLLAEkgyYFDIY 568
Cdd:TIGR00956  928 EPTSGLDSQTAWSICKLMRKLADHGQAILCTiHQPSAIlfEEFDRLLLLQKGgQTVyfgDLGENSHTIIN---YFEKH 1002
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
352-553 1.05e-10

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 62.34  E-value: 1.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 352 LKNISLKASPGQTIAILGETGAGKSTLVNLICRFY--DPTSG---EILIDGVD-----ARKwhVRELRNHIATVMQDIFL 421
Cdd:PRK09984  20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgDKSAGshiELLGRTVQregrlARD--IRKSRANTGYIFQQFNL 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 422 FSD-TIEGNIAFGA---------------PDATMEDVRRMARIADAdHFIEtmpesydtivgERGVGLSGGQKQRISLAR 485
Cdd:PRK09984  98 VNRlSVLENVLIGAlgstpfwrtcfswftREQKQRALQALTRVGMV-HFAH-----------QRVSTLSGGQQQRVAIAR 165
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 404223395 486 ALLKNPSILILDDTTSAVDMETEVKIQGELKKITEN--TTTFIIAHRIS-SVKEADEILILNHGEIIERGT 553
Cdd:PRK09984 166 ALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdgITVVVTLHQVDyALRYCERIVALRQGHVFYDGS 236
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
351-504 1.24e-10

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


Pssm-ID: 273491 [Multi-domain]  Cd Length: 198  Bit Score: 61.22  E-value: 1.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  351 VLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRN-----HIATVMQDIflfsdT 425
Cdd:TIGR01189  15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENilylgHLPGLKPEL-----S 89
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 404223395  426 IEGNIAFGAPDATMEDVRRMARIADADhfietMPESYDTIVGErgvgLSGGQKQRISLARALLKNPSILILDDTTSAVD 504
Cdd:TIGR01189  90 ALENLHFWAAIHGGAQRTIEDALAAVG-----LTGFEDLPAAQ----LSAGQQRRLALARLWLSRRPLWILDEPTTALD 159
hmuV PRK13547
heme ABC transporter ATP-binding protein;
351-558 1.40e-10

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 62.15  E-value: 1.40e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 351 VLKNISLKASPGQTIAILGETGAGKSTLVNL----ICRFYDP----TSGEILIDG-----VDARKwhVRELRNHIATVMQ 417
Cdd:PRK13547  16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKAlagdLTGGGAPrgarVTGDVTLNGeplaaIDAPR--LARLRAVLPQAAQ 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 418 DIFLFS-DTIEGNIAFGAPDATMEDVRRMARIADAdhfiETMPESYDTIVGERGVGLSGGQKQRISLARALLK------- 489
Cdd:PRK13547  94 PAFAFSaREIVLLGRYPHARRAGALTHRDGEIAWQ----ALALAGATALVGRDVTTLSGGELARVQFARVLAQlwpphda 169
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 404223395 490 --NPSILILDDTTSAVDMETEVKIQGELKKITE--NTTTFIIAHRIS-SVKEADEILILNHGEIIERGTHSSLL 558
Cdd:PRK13547 170 aqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARdwNLGVLAIVHDPNlAARHADRIAMLADGAIVAHGAPADVL 243
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
361-553 1.45e-10

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 59.69  E-value: 1.45e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395   361 PGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIdgvdarkwhvrelrnhiatvmqdiflfsdtiegniafgapdatme 440
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY--------------------------------------------- 35
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395   441 dvrrmarIADADHFIETMPESYDTIVGERGVGLSGGQKQRISLARALLKNPSILILDDTTSAVDMETEVKIQ-------G 513
Cdd:smart00382  36 -------IDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleelrlL 108
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 404223395   514 ELKKITENTTTFIIAHRISSVKEADEILILNHGEIIERGT 553
Cdd:smart00382 109 LLLKSEKNLTVILTTNDEKDLGPALLRRRFDRRIVLLLIL 148
ABC_6TM_HMT1 cd18583
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents ...
77-300 1.73e-10

Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents the HMT1 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster. HMT1 is closely related to Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria.


Pssm-ID: 350027 [Multi-domain]  Cd Length: 290  Bit Score: 62.16  E-value: 1.73e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  77 QIMCERIGQNSLFRIREDLYKKLQSLDFDFFNNTRVGDIMARMTGDTdAIRHFVSWVSYNILENVFLFSFAIIIMA-AID 155
Cdd:cd18583   58 SWLWIPVEQYSYRALSTAAFNHVMNLSMDFHDSKKSGEVLKAIEQGS-SINDLLEQILFQIVPMIIDLVIAIVYLYyLFD 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 156 WKLTLALVIVTPLIAILTMKMSSKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDS 235
Cdd:cd18583  137 PYMGLIVAVVMVLYVWSTIKLTSWRTKLRRDMIDADREERSILTESLLNWETVKYFNREPYEKERYREAVKNYQKAERKY 216
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 404223395 236 advsRTYLPVLDSLAGMLVVITLIFG----GYLVIKGQMTLGDLVAFNGFLWMLNGPMRMSGWLINDVQ 300
Cdd:cd18583  217 ----LFSLNLLNAVQSLILTLGLLAGcflaAYQVSQGQATVGDFVTLLTYWAQLSGPLNFFATLYRSIQ 281
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
346-507 1.96e-10

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 63.60  E-value: 1.96e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 346 DPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGE-ILIDGV-----------DARKwHVRElrnHIA 413
Cdd:PRK11819  17 PPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEaRPAPGIkvgylpqepqlDPEK-TVRE---NVE 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 414 TVMQDIF-LFSDTIEGNIAFGAPDATMEDV-RRMARI------ADA---DHFIE-TM-----PESyDTIVGErgvgLSGG 476
Cdd:PRK11819  93 EGVAEVKaALDRFNEIYAAYAEPDADFDALaAEQGELqeiidaADAwdlDSQLEiAMdalrcPPW-DAKVTK----LSGG 167
                        170       180       190
                 ....*....|....*....|....*....|.
gi 404223395 477 QKQRISLARALLKNPSILILDDTTSAVDMET 507
Cdd:PRK11819 168 ERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
337-549 2.87e-10

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 62.82  E-value: 2.87e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 337 KNVSFHFeddPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRE-LRNHIATV 415
Cdd:PRK10982   2 SNISKSF---PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEaLENGISMV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 416 MQDIFLFSD-TIEGNIAFGA-PDATM-EDVRRMARIADA---DHFIETMPEsydtivgERGVGLSGGQKQRISLARALLK 489
Cdd:PRK10982  79 HQELNLVLQrSVMDNMWLGRyPTKGMfVDQDKMYRDTKAifdELDIDIDPR-------AKVATLSVSQMQMIEIAKAFSY 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 404223395 490 NPSILILDDTTSAVDmETEV----KIQGELKKitENTTTFIIAHRISSVKE-ADEILILNHGEII 549
Cdd:PRK10982 152 NAKIVIMDEPTSSLT-EKEVnhlfTIIRKLKE--RGCGIVYISHKMEEIFQlCDEITILRDGQWI 213
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
324-553 2.91e-10

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


Pssm-ID: 130324 [Multi-domain]  Cd Length: 2272  Bit Score: 63.49  E-value: 2.91e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395   324 EKPAPSLQGHVEFKNVSFHFE--DDPNTDVLkNISLKASpgQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDAR 401
Cdd:TIGR01257  919 ERELPGLVPGVCVKNLVKIFEpsGRPAVDRL-NITFYEN--QITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIE 995
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395   402 KwHVRELRNHIATVMQDIFLFSD-TIEGNIAFGAPdatmedvRRMARIADADHFIETMPEsyDTIV----GERGVGLSGG 476
Cdd:TIGR01257  996 T-NLDAVRQSLGMCPQHNILFHHlTVAEHILFYAQ-------LKGRSWEEAQLEMEAMLE--DTGLhhkrNEEAQDLSGG 1065
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 404223395   477 QKQRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHRISSVK-EADEILILNHGEIIERGT 553
Cdd:TIGR01257 1066 MQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADlLGDRIAIISQGRLYCSGT 1143
GguA NF040905
sugar ABC transporter ATP-binding protein;
352-550 3.44e-10

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 62.50  E-value: 3.44e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 352 LKNISLKASPGQTIAILGETGAGKSTLVNLICRFYdPT---SGEILIDGVDARKWHVRELRNH-IATVMQDIFLFSD-TI 426
Cdd:NF040905  17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGEVCRFKDIRDSEALgIVIIHQELALIPYlSI 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 427 EGNIAFGAPDATMEDVRRMARIADADHFIET--MPESYDTIVGERGVGlsggQKQRISLARALLKNPSILILDDTTSAV- 503
Cdd:NF040905  96 AENIFLGNERAKRGVIDWNETNRRARELLAKvgLDESPDTLVTDIGVG----KQQLVEIAKALSKDVKLLILDEPTAALn 171
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 404223395 504 --DMETEVKIQGELKKitENTTTFIIAHRISSVKE-ADEILILNHGEIIE 550
Cdd:NF040905 172 eeDSAALLDLLLELKA--QGITSIIISHKLNEIRRvADSITVLRDGRTIE 219
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
356-531 4.03e-10

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


Pssm-ID: 213204 [Multi-domain]  Cd Length: 246  Bit Score: 60.50  E-value: 4.03e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 356 SLKASPG-----QTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDarkwhvrelrnhIATVMQDIflfsdtiegni 430
Cdd:cd03237   14 TLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDT------------VSYKPQYI----------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 431 afgAPDATMEdVRRMARIADADHFI------ETM-PESYDTIVGERGVGLSGGQKQRISLARALLKNPSILILDDTTSAV 503
Cdd:cd03237   71 ---KADYEGT-VRDLLSSITKDFYThpyfktEIAkPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYL 146
                        170       180       190
                 ....*....|....*....|....*....|
gi 404223395 504 DMETEVKIQGELKKITENT--TTFIIAHRI 531
Cdd:cd03237  147 DVEQRLMASKVIRRFAENNekTAFVVEHDI 176
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
353-552 6.74e-10

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 60.10  E-value: 6.74e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 353 KNISLKASPGQTIAILGETGAGKS----TLVNLICRFYDPTSGEILIDGVDArkwHVRELRN-HIATVMQDiflfsdtie 427
Cdd:PRK10418  20 HGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPV---APCALRGrKIATIMQN--------- 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 428 gniafgaPDATMEDVRRMAriadaDHFIETM-----PESYDTIVGE-RGVGL--------------SGGQKQRISLARAL 487
Cdd:PRK10418  88 -------PRSAFNPLHTMH-----THARETClalgkPADDATLTAAlEAVGLenaarvlklypfemSGGMLQRMMIALAL 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 404223395 488 LKNPSILILDDTTSAVDMETEVKIQGELKKI--TENTTTFIIAHRISSV-KEADEILILNHGEIIERG 552
Cdd:PRK10418 156 LCEAPFIIADEPTTDLDVVAQARILDLLESIvqKRALGMLLVTHDMGVVaRLADDVAVMSHGRIVEQG 223
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
354-504 8.92e-10

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 58.66  E-value: 8.92e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 354 NISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKwhVRE--LRN-----HIATVMQDIflfsdTI 426
Cdd:PRK13538  19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRR--QRDeyHQDllylgHQPGIKTEL-----TA 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 427 EGNIAFGAPDATMEDVRRMARIADAdhfietmpesydtiVGERGV------GLSGGQKQRISLARALLKNPSILILDDTT 500
Cdd:PRK13538  92 LENLRFYQRLHGPGDDEALWEALAQ--------------VGLAGFedvpvrQLSAGQQRRVALARLWLTRAPLWILDEPF 157

                 ....
gi 404223395 501 SAVD 504
Cdd:PRK13538 158 TAID 161
tagH PRK13545
teichoic acids export protein ATP-binding subunit; Provisional
352-570 1.36e-09

teichoic acids export protein ATP-binding subunit; Provisional


Pssm-ID: 184130 [Multi-domain]  Cd Length: 549  Bit Score: 60.67  E-value: 1.36e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 352 LKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRELRNHIaTVMQDIFLfsdtiEGNIA 431
Cdd:PRK13545  40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNGQL-TGIENIEL-----KGLMM 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 432 FGAPDATMEDVRRMARIADADHFIETMPESYdtivgergvglSGGQKQRISLARALLKNPSILILDDTTSAVDMETEVKI 511
Cdd:PRK13545 114 GLTKEKIKEIIPEIIEFADIGKFIYQPVKTY-----------SSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKC 182
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 404223395 512 QGELKKITEN-TTTFIIAHRISSVKE-ADEILILNHGEIIERGTHSSLLAEKGYYFDIYNK 570
Cdd:PRK13545 183 LDKMNEFKEQgKTIFFISHSLSQVKSfCTKALWLHYGQVKEYGDIKEVVDHYDEFLKKYNQ 243
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
337-553 1.42e-09

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 59.76  E-value: 1.42e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 337 KNVSFHFEDD--PNTDVlKNISLKASPGQTIAILGETGAGKS----TLVNLIcRFYDPTSGEIL-IDGVDARKWHVRELR 409
Cdd:PRK11022   7 DKLSVHFGDEsaPFRAV-DRISYSVKQGEVVGIVGESGSGKSvsslAIMGLI-DYPGRVMAEKLeFNGQDLQRISEKERR 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 410 NHIATVMQDIFlfSDTIEG-NIAFGAPDATMEDVR------RMARIADADHFIETM----PESYDTIVGERgvgLSGGQK 478
Cdd:PRK11022  85 NLVGAEVAMIF--QDPMTSlNPCYTVGFQIMEAIKvhqggnKKTRRQRAIDLLNQVgipdPASRLDVYPHQ---LSGGMS 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 479 QRISLARALLKNPSILILDDTTSAVDmeteVKIQG-------ELKKiTENTTTFIIAHRISSVKE-ADEILILNHGEIIE 550
Cdd:PRK11022 160 QRVMIAMAIACRPKLLIADEPTTALD----VTIQAqiielllELQQ-KENMALVLITHDLALVAEaAHKIIVMYAGQVVE 234

                 ...
gi 404223395 551 RGT 553
Cdd:PRK11022 235 TGK 237
ABC_6TM_NHLM_bacteriocin cd18569
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; ...
102-312 2.55e-09

Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; This group includes the six-transmembrane helical domain (6-TMD) of the ABC subunit of NHLM (Nitrile Hydratase Leader Microcin) bacteriocin system, which contains ABC transporter (permease/ATP-binding fused protein) with a peptidase domain. ABC-transporter proteins in this group are predicted to be a subunit of a bacteriocin processing and export system, and they carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.


Pssm-ID: 350013 [Multi-domain]  Cd Length: 294  Bit Score: 58.64  E-value: 2.55e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 102 LDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVSYNILeNVFLFSFAIIIMAAIDWKLTLALVIVTpLIAILTMKMSSKAQ 181
Cdd:cd18569   88 LPVEFFSQRYAGDIASRVQSNDRVANLLSGQLATTVL-NLVMAVFYALLMLQYDVPLTLIGIAIA-LLNLLVLRLVSRKR 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 182 pvfyeiRESFSRLnsMVEEN------ISGNRV---VKAFAREDFemkkFHEHNEDFKKRNLDS---ADVSRTYL----PV 245
Cdd:cd18569  166 ------VDLNRRL--LQDSGkltgttMSGLQMietLKASGAESD----FFSRWAGYQAKVLNAqqeLGRTNQLLgalpTL 233
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 404223395 246 LDSLAGMLVvitLIFGGYLVIKGQMTLGDLVAFNGFLWMLNGPmrmsgwlindVQRFIASSFKIQDM 312
Cdd:cd18569  234 LSALTNAAI---LGLGGLLVMDGALTIGMLVAFQSLMASFLAP----------VNSLVGLGGTLQEM 287
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
338-553 2.84e-09

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 58.97  E-value: 2.84e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 338 NVSFHFEDDPNTDVLK-NISLKAspGQTIAILGETGAGKS----TLVNLICRfYDPTSGEILIDG---VDARKWHVRELR 409
Cdd:PRK09473  19 RVTFSTPDGDVTAVNDlNFSLRA--GETLGIVGESGSGKSqtafALMGLLAA-NGRIGGSATFNGreiLNLPEKELNKLR 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 410 -NHIATVMQDiflfsDTIEGNIAFGAPDATMEDVRRMARIADADHFIET--------MPESYDTIvGERGVGLSGGQKQR 480
Cdd:PRK09473  96 aEQISMIFQD-----PMTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESvrmldavkMPEARKRM-KMYPHEFSGGMRQR 169
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 404223395 481 ISLARALLKNPSILILDDTTSAVDMETEVKIQ---GELKKiTENTTTFIIAHRISSVKE-ADEILILNHGEIIERGT 553
Cdd:PRK09473 170 VMIAMALLCRPKLLIADEPTTALDVTVQAQIMtllNELKR-EFNTAIIMITHDLGVVAGiCDKVLVMYAGRTMEYGN 245
ABC_6TM_Pgp_ABCB1 cd18558
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ...
90-276 2.88e-09

Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1(ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.


Pssm-ID: 350002 [Multi-domain]  Cd Length: 312  Bit Score: 58.83  E-value: 2.88e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  90 RIREDLYKKLQSLDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENVFLFSFAIIIMAAIDWKLTLALVIVTPLI 169
Cdd:cd18558   93 KIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRGWKLTLVILAISPVL 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 170 AI---LTMKMSSKAQPvfyEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSRTYLPVL 246
Cdd:cd18558  173 GLsavVWAKILSGFTD---KEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKKAITFNISMGAA 249
                        170       180       190
                 ....*....|....*....|....*....|
gi 404223395 247 DSLAGMLVVITLIFGGYLVIKGQMTLGDLV 276
Cdd:cd18558  250 FLLIYASYALAFWYGTYLVTQQEYSIGEVL 279
ABC_6TM_CydC cd18585
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ...
67-271 3.04e-09

Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH transporter; The CydC protein, together with the CydD protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).


Pssm-ID: 350029 [Multi-domain]  Cd Length: 290  Bit Score: 58.26  E-value: 3.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  67 IIRTICRYTyqimcER-IGQNSLFRIREDL----YKKLQSLDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENV 141
Cdd:cd18585   46 ITRTAGRYG-----ERlVSHDATFRLLSNLrvwfYRKLEPLAPARLQKYRSGDLLNRIVADIDTLDNLYLRVLSPPVVAL 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 142 FLFSFAIIIMAAIDWKLTLALV-------IVTPLIAILTMKMSSKaqpvfyEIRESFSRLNSMVEENISGNRVVKAFARE 214
Cdd:cd18585  121 LVILATILFLAFFSPALALILLaglllagVVIPLLFYRLGKKIGQ------QLVQLRAELRTELVDGLQGMAELLIFGAL 194
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 404223395 215 DFEMKKFHEHNEDFKKRNLDSADVSRTYLPVLDSLAGMLVVITLIFGGYLVIKGQMT 271
Cdd:cd18585  195 ERQRQQLEQLSDALIKEQRRLARLSGLSQALMILLSGLTVWLVLWLGAPLVQNGALD 251
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
334-563 3.43e-09

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 59.52  E-value: 3.43e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFEDDPntdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEIlidgvdarKWhvRELRN--- 410
Cdd:PRK15064 320 LEVENLTKGFDNGP---LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV--------KW--SENANigy 386
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 411 ----HIATVMQDIFLF---------SD------TIEGNIAFGApdatmEDVRRMARIadadhfietmpesydtivgergv 471
Cdd:PRK15064 387 yaqdHAYDFENDLTLFdwmsqwrqeGDdeqavrGTLGRLLFSQ-----DDIKKSVKV----------------------- 438
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 472 gLSGGQKQRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKItENTTTFIIAHR--ISSVkeADEILILNHGEII 549
Cdd:PRK15064 439 -LSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKY-EGTLIFVSHDRefVSSL--ATRIIEITPDGVV 514
                        250
                 ....*....|....*
gi 404223395 550 E-RGTHSSLLAEKGY 563
Cdd:PRK15064 515 DfSGTYEEYLRSQGI 529
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
335-507 3.88e-09

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 59.58  E-value: 3.88e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 335 EFKNVSFHFEDDpntDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEI--------------------- 393
Cdd:PRK11147 321 EMENVNYQIDGK---QLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIhcgtklevayfdqhraeldpe 397
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 394 ------LIDG-----VDARKwhvrelrNHIATVMQDiFLFSdtiegniafgaPDATMEDVRrmariadadhfietmpesy 462
Cdd:PRK11147 398 ktvmdnLAEGkqevmVNGRP-------RHVLGYLQD-FLFH-----------PKRAMTPVK------------------- 439
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 404223395 463 dtivgergvGLSGGQKQRISLARALLKNPSILILDDTTSAVDMET 507
Cdd:PRK11147 440 ---------ALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVET 475
3a01203 TIGR00954
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...
347-535 1.54e-08

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


Pssm-ID: 273360 [Multi-domain]  Cd Length: 659  Bit Score: 57.45  E-value: 1.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  347 PNTDVLKN-ISLKASPGQTIAILGETGAGKSTLVNLICRFYdPTSGEILIDGVDARKWHV--------RELRNHIatvmq 417
Cdd:TIGR00954 462 PNGDVLIEsLSFEVPSGNNLLICGPNGCGKSSLFRILGELW-PVYGGRLTKPAKGKLFYVpqrpymtlGTLRDQI----- 535
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  418 difLFSDTIEGNIAFGAPDAtmeDVRRMARIADADHFIEtmpesydtivgeRGVG----------LSGGQKQRISLARAL 487
Cdd:TIGR00954 536 ---IYPDSSEDMKRRGLSDK---DLEQILDNVQLTHILE------------REGGwsavqdwmdvLSGGEKQRIAMARLF 597
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 404223395  488 LKNPSILILDDTTSAVDMETEVKIQGELKKIteNTTTFIIAHRISSVK 535
Cdd:TIGR00954 598 YHKPQFAILDECTSAVSVDVEGYMYRLCREF--GITLFSVSHRKSLWK 643
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
353-548 1.88e-08

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 56.98  E-value: 1.88e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 353 KNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRE-LRNHIATVMQD-----IFL----- 421
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrLARGLVYLPEDrqssgLYLdapla 359
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 422 --FSDTIEGNIAF----GAPDATMEDVRRMARI--ADADHFIETmpesydtivgergvgLSGGQKQRISLARALLKNPSI 493
Cdd:PRK15439 360 wnVCALTHNRRGFwikpARENAVLERYRRALNIkfNHAEQAART---------------LSGGNQQKVLIAKCLEASPQL 424
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 494 LILDDTTSAVDMETEVKIQGELKKITENTTTFIIahrISS-----VKEADEILILNHGEI 548
Cdd:PRK15439 425 LIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLF---ISSdleeiEQMADRVLVMHQGEI 481
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
335-504 3.49e-08

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 56.09  E-value: 3.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 335 EFKNVSFHFEDDPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYD-PTSGEILIDGVDARKWHVRE-LRNHI 412
Cdd:PRK13549 261 EVRNLTAWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIRNPQQaIAQGI 340
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 413 ATVMQD-----IFLFSDTIEgNIAFgapdATMEDVRRMARIADA------DHFIETMpeSYDTIVGERGVG-LSGGQKQR 480
Cdd:PRK13549 341 AMVPEDrkrdgIVPVMGVGK-NITL----AALDRFTGGSRIDDAaelktiLESIQRL--KVKTASPELAIArLSGGNQQK 413
                        170       180
                 ....*....|....*....|....
gi 404223395 481 ISLARALLKNPSILILDDTTSAVD 504
Cdd:PRK13549 414 AVLAKCLLLNPKILILDEPTRGID 437
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
354-552 6.24e-08

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 54.16  E-value: 6.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 354 NISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVREL----RNHIAT-----VMQ---DIFL 421
Cdd:PRK11701  24 DVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseaeRRRLLRtewgfVHQhprDGLR 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 422 FSDTIEGNIA----------FGAPDATMED-VRRM----ARIADAdhfietmPESYdtivgergvglSGGQKQRISLARA 486
Cdd:PRK11701 104 MQVSAGGNIGerlmavgarhYGDIRATAGDwLERVeidaARIDDL-------PTTF-----------SGGMQQRLQIARN 165
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 404223395 487 LLKNPSILILDDTTSAVDmeteVKIQGELKKITENTTT------FIIAHRISSVK-EADEILILNHGEIIERG 552
Cdd:PRK11701 166 LVTHPRLVFMDEPTGGLD----VSVQARLLDLLRGLVRelglavVIVTHDLAVARlLAHRLLVMKQGRVVESG 234
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
326-507 6.90e-08

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


Pssm-ID: 274744 [Multi-domain]  Cd Length: 552  Bit Score: 55.33  E-value: 6.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  326 PAPSLQGHV-EFKNVSFHFEDDPntdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILI-DGVdarkw 403
Cdd:TIGR03719 314 PGPRLGDKViEAENLTKAFGDKL---LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgETV----- 385
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  404 hvrelrnHIATVMQdiflFSDTIEGN------IAFGAPDATMEDVRRMARiadadhfietmpeSYDTIVGERG------V 471
Cdd:TIGR03719 386 -------KLAYVDQ----SRDALDPNktvweeISGGLDIIKLGKREIPSR-------------AYVGRFNFKGsdqqkkV 441
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 404223395  472 G-LSGGQKQRISLARALLKNPSILILDDTTSAVDMET 507
Cdd:TIGR03719 442 GqLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVET 478
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
338-538 9.30e-08

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127 [Multi-domain]  Cd Length: 200  Bit Score: 52.64  E-value: 9.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 338 NVSFHFEDDPntdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKwhvrelrnHIATVMQ 417
Cdd:PRK13540   6 ELDFDYHDQP---LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK--------DLCTYQK 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 418 DIFLFSD--------TIEGNIAFGA-PDATMEDVRRMARIADADHFIetmpesyDTIVGErgvgLSGGQKQRISLARALL 488
Cdd:PRK13540  75 QLCFVGHrsginpylTLRENCLYDIhFSPGAVGITELCRLFSLEHLI-------DYPCGL----LSSGQKRQVALLRLWM 143
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 404223395 489 KNPSILILDDTTSAVDmetEVKIQGELKKITENT----TTFIIAHRISSVKEAD 538
Cdd:PRK13540 144 SKAKLWLLDEPLVALD---ELSLLTIITKIQEHRakggAVLLTSHQDLPLNKAD 194
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
368-504 1.50e-07

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 54.36  E-value: 1.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 368 LGETGAGKST----LVNLIcrfyDPTSGEILIDG--VDARKWHVR--------------ELrnhiaTVMQDIFLFsdtie 427
Cdd:NF033858 298 LGSNGCGKSTtmkmLTGLL----PASEGEAWLFGqpVDAGDIATRrrvgymsqafslygEL-----TVRQNLELH----- 363
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 428 gniA--FGAPDATMED-VRRMARIADADHFIETMPESydtivgergvgLSGGQKQRISLARALLKNPSILILDDTTSAVD 504
Cdd:NF033858 364 ---ArlFHLPAAEIAArVAEMLERFDLADVADALPDS-----------LPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
352-504 1.52e-07

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 54.24  E-value: 1.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 352 LKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVDARKWHVRE-LRNHIATVMQDI----FLFSDTI 426
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDgLANGIVYISEDRkrdgLVLGMSV 347
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 427 EGNIAFGAPDA---TMEDVRRMARIADADHFIETM----PeSYDTIVGErgvgLSGGQKQRISLARALLKNPSILILDDT 499
Cdd:PRK10762 348 KENMSLTALRYfsrAGGSLKHADEQQAVSDFIRLFniktP-SMEQAIGL----LSGGNQQKVAIARGLMTRPKVLILDEP 422

                 ....*
gi 404223395 500 TSAVD 504
Cdd:PRK10762 423 TRGVD 427
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
355-560 1.58e-07

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 52.63  E-value: 1.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 355 ISLKASPGQTIAILGETGAGKSTLVNLICRFYdPTSGEILIDGVDARKWHVRELRNHIATVMQ--------DIFLFSDTI 426
Cdd:PRK03695  15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRAYLSQqqtppfamPVFQYLTLH 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 427 EG-NIAFGAPDATMEDVRRMARIADADHfietmpesydtivgeRGVG-LSGGQKQRISLARALLK-----NPS--ILILD 497
Cdd:PRK03695  94 QPdKTRTEAVASALNEVAEALGLDDKLG---------------RSVNqLSGGEWQRVRLAAVVLQvwpdiNPAgqLLLLD 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 404223395 498 DTTSAVDMETEVKIQGELKKITENTTTFIIA-HRIS-SVKEADEILILNHGEIIERGTHSSLLAE 560
Cdd:PRK03695 159 EPMNSLDVAQQAALDRLLSELCQQGIAVVMSsHDLNhTLRHADRVWLLKQGKLLASGRRDEVLTP 223
PRK13543 PRK13543
heme ABC exporter ATP-binding protein CcmA;
320-506 1.67e-07

heme ABC exporter ATP-binding protein CcmA;


Pssm-ID: 184129 [Multi-domain]  Cd Length: 214  Bit Score: 52.16  E-value: 1.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 320 PIHAEKPApsLQGHvefkNVSFHFEDDPntdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVD 399
Cdd:PRK13543   4 PLHTAPPL--LAAH----ALAFSRNEEP---VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKT 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 400 A----RKWHVRELrNHIATVMQDIflfsdtiegniafgapdATMEDVrrmariadadHFI--------ETMPESYDTIVG 467
Cdd:PRK13543  75 AtrgdRSRFMAYL-GHLPGLKADL-----------------STLENL----------HFLcglhgrraKQMPGSALAIVG 126
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 404223395 468 ERGVG------LSGGQKQRISLARALLKNPSILILDDTTSAVDME 506
Cdd:PRK13543 127 LAGYEdtlvrqLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLE 171
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
335-548 1.68e-07

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


Pssm-ID: 131681 [Multi-domain]  Cd Length: 500  Bit Score: 54.06  E-value: 1.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  335 EFKNVSFHFEDDPNTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPT-SGEILIDG--VDARKwHVRELRNH 411
Cdd:TIGR02633 259 EARNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGkpVDIRN-PAQAIRAG 337
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  412 IATVMQDIF---LFSDTIEG-NIAFGAPDA-----TMEDVRRMARIADADHFIETMPESYDTIVGergvGLSGGQKQRIS 482
Cdd:TIGR02633 338 IAMVPEDRKrhgIVPILGVGkNITLSVLKSfcfkmRIDAAAELQIIGSAIQRLKVKTASPFLPIG----RLSGGNQQKAV 413
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 404223395  483 LARALLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIahrISS-----VKEADEILILNHGEI 548
Cdd:TIGR02633 414 LAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIV---VSSelaevLGLSDRVLVIGEGKL 481
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
334-504 2.76e-07

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 53.59  E-value: 2.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 334 VEFKNVSFHFEDdpnTDVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGVD-ARKWHVRELRNHI 412
Cdd:NF033858   2 ARLEGVSHRYGK---TVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDmADARHRRAVCPRI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 413 ATVMQDI--FLFSD-TIEGNIAF-----GAPDAtmEDVRRMARIADA---DHFietmpesydtivGERGVG-LSGGQKQR 480
Cdd:NF033858  79 AYMPQGLgkNLYPTlSVFENLDFfgrlfGQDAA--ERRRRIDELLRAtglAPF------------ADRPAGkLSGGMKQK 144
                        170       180
                 ....*....|....*....|....
gi 404223395 481 ISLARALLKNPSILILDDTTSAVD 504
Cdd:NF033858 145 LGLCCALIHDPDLLILDEPTTGVD 168
ABC_6TM_NdvA_beta-glucan_exporter_like cd18562
Six-transmembrane helical domain of the cyclic beta-glucan ABC transporter NdvA, and similar ...
143-285 3.77e-07

Six-transmembrane helical domain of the cyclic beta-glucan ABC transporter NdvA, and similar proteins; This group represents the six-transmembrane domain of NdvA, an ATP-dependent exporter of cyclic beta glucans, and similar proteins. NdvA is required for nodulation of legume roots and is involved in beta-(1,2)-glucan export to the periplasm. NdvA mutants in Brucella abortus and Sinorhizobium meliloti have been shown to exhibit decreased virulence in mice and inhibit intracellular multiplication in HeLa cells. These results suggest that cyclic beta-(1,2)-glucan is required to transport into the periplasmatic space to function as a virulence factor. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.


Pssm-ID: 350006 [Multi-domain]  Cd Length: 289  Bit Score: 51.86  E-value: 3.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 143 LFSFAIIIMAA--IDWKLTL---ALVIVTPLIAILTMKMSSKAQPvfyEIRESFSRLNSMVEENISGNRVVKAFAREDFE 217
Cdd:cd18562  121 LVSLIVLLPVAlwMNWRLALllvVLAAVYAALNRLVMRRTKAGQA---AVEEHHSALSGRVGDVIGNVTVVQSYTRLAAE 197
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 404223395 218 MKKFHehneDFKKRNLDSAdvsrtyLPVLDSLAGMLVV--------ITLIF--GGYLVIKGQMTLGDLVAFNGFLWML 285
Cdd:cd18562  198 TSALR----GITRRLLAAQ------YPVLNWWALASVLtraastltMVAIFalGAWLVQRGELTVGEIVSFVGFATLL 265
ABC_6TM_ABCC cd18559
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ...
16-299 4.82e-07

Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents the 6-transmembrane (6TM) domain of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides.


Pssm-ID: 350003 [Multi-domain]  Cd Length: 290  Bit Score: 51.83  E-value: 4.82e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  16 LLMIGVFILIFIASGISIIYPLLGgkVIDDVvyQNKTNLLIPLLLIMIISTIIRTICRYTYQIMCERIGQNSLFRIREDL 95
Cdd:cd18559    2 FLLIKLVLCNHVFSGPSNLWLLLW--FDDPV--NGPQEHGQVYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  96 YKKLQSLDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVSynileNVFLFSFAIIIMAAIDW-KLTLALVIVTPLIAIL-- 172
Cdd:cd18559   78 YHKALRSPISFFERTPSGELVNLFSKDLDRVDSMAPQVI-----KMWMGPLQNVIGLYLLIlLAGPMAAVGIPLGLLYvp 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 173 ---TMKMSSKAqpvfYEIRESFSRLN--SMVEENISGNRVVKAFAREdfemkkfhehnEDFKKRNLDSADVSRTYLPVLD 247
Cdd:cd18559  153 vnrVYAASSRQ----LKRLESVSKDPryKLFNETLLGISVIKAFEWE-----------EAFIRQVDAKRDNELAYLPSIV 217
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 404223395 248 SL---------AGMLVVITLIFGGYLVIKGQMTLGDLVAFNGF--LWMLNGPMRMSGWLINDV 299
Cdd:cd18559  218 YLralavrlwcVGPCIVLFASFFAYVSRHSLAGLVALKVFYSLalTTYLNWPLNMSPEVITNI 280
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
354-529 5.80e-07

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 52.20  E-value: 5.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 354 NISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGvdarkwHVRelrnhIATVMQDIFLFS-----DTI-- 426
Cdd:PRK15064  19 NISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDP------NER-----LGKLRQDQFAFEeftvlDTVim 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 427 ----------EGNIAFGAPDATMEDVRRMA----RIADADHFietMPESYdtiVGE--RGVGL------------SGGQK 478
Cdd:PRK15064  88 ghtelwevkqERDRIYALPEMSEEDGMKVAdlevKFAEMDGY---TAEAR---AGEllLGVGIpeeqhyglmsevAPGWK 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 404223395 479 QRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKitENTTTFIIAH 529
Cdd:PRK15064 162 LRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNE--RNSTMIIISH 210
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
351-506 6.78e-07

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 52.09  E-value: 6.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 351 VLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEI-LIDGVDARKWHVRELRnhiatvmqdiFLFSDTiegn 429
Cdd:PRK10636 327 ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGYFAQHQLE----------FLRADE---- 392
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 430 iafgAPdatmedVRRMARIADAdhfiETMPESYDTI---------VGERGVGLSGGQKQRISLARALLKNPSILILDDTT 500
Cdd:PRK10636 393 ----SP------LQHLARLAPQ----ELEQKLRDYLggfgfqgdkVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPT 458

                 ....*.
gi 404223395 501 SAVDME 506
Cdd:PRK10636 459 NHLDLD 464
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
352-553 7.30e-07

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


Pssm-ID: 213238 [Multi-domain]  Cd Length: 261  Bit Score: 50.69  E-value: 7.30e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 352 LKNISLKASPGQTIAILGETGAGKSTLVN------LICRFY----DPTSGEIlIDGVDARKWHV--------RELRNHIA 413
Cdd:cd03271   11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINdtlypaLARRLHlkkeQPGNHDR-IEGLEHIDKVIvidqspigRTPRSNPA 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 414 T---VMQDIF-LFSDTIEG---------------NIAfgapdatmeDVRRMArIADADHFIETMPESYDTI--------- 465
Cdd:cd03271   90 TytgVFDEIReLFCEVCKGkrynretlevrykgkSIA---------DVLDMT-VEEALEFFENIPKIARKLqtlcdvglg 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 466 ---VGERGVGLSGGQKQRISLARALLK---NPSILILDDTTSAVDMETEVKIQGELKKITEN-TTTFIIAHRISSVKEAD 538
Cdd:cd03271  160 yikLGQPATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKgNTVVVIEHNLDVIKCAD 239
                        250       260
                 ....*....|....*....|.
gi 404223395 539 EILIL------NHGEIIERGT 553
Cdd:cd03271  240 WIIDLgpeggdGGGQVVASGT 260
PRK15093 PRK15093
peptide ABC transporter ATP-binding protein SapD;
355-559 8.78e-07

peptide ABC transporter ATP-binding protein SapD;


Pssm-ID: 185049 [Multi-domain]  Cd Length: 330  Bit Score: 50.96  E-value: 8.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 355 ISLKASPGQTIAILGETGAGKSTLVNLICRF----YDPTSGEILIDGVDARKWHVRELRNHIATVMQDIFLF-------S 423
Cdd:PRK15093  26 VSMTLTEGEIRGLVGESGSGKSLIAKAICGVtkdnWRVTADRMRFDDIDLLRLSPRERRKLVGHNVSMIFQEpqscldpS 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 424 DTIEGNIAFGAPDATMED---------VRR----MARIADADHfietmpesyDTIVGERGVGLSGGQKQRISLARALLKN 490
Cdd:PRK15093 106 ERVGRQLMQNIPGWTYKGrwwqrfgwrKRRaielLHRVGIKDH---------KDAMRSFPYELTEGECQKVMIAIALANQ 176
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 404223395 491 PSILILDDTTSAVDMETEVKIQGELKKITEN--TTTFIIAHRISSV-KEADEILILNHGEIIERGTHSSLLA 559
Cdd:PRK15093 177 PRLLIADEPTNAMEPTTQAQIFRLLTRLNQNnnTTILLISHDLQMLsQWADKINVLYCGQTVETAPSKELVT 248
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
314-498 1.03e-06

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 51.55  E-value: 1.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 314 ATDAKIPIHAEKPA----PSLQGHVEFKNVSFHFEDDPntdVLKNISLKASPGQTIAILGETGAGKSTLVNLIC----RF 385
Cdd:PRK10938 237 LEGVQLPEPDEPSArhalPANEPRIVLNNGVVSYNDRP---ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITgdhpQG 313
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 386 Y--DPT-------SGEILidgvdarkWhvrELRNHIATVMQDIFL---------------FSDTIegNIAFGAPDA---- 437
Cdd:PRK10938 314 YsnDLTlfgrrrgSGETI--------W---DIKKHIGYVSSSLHLdyrvstsvrnvilsgFFDSI--GIYQAVSDRqqkl 380
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 404223395 438 TMEDVRRM---ARIADAD-HfietmpesydtivgergvGLSGGQkQRISL-ARALLKNPSILILDD 498
Cdd:PRK10938 381 AQQWLDILgidKRTADAPfH------------------SLSWGQ-QRLALiVRALVKHPTLLILDE 427
GguA NF040905
sugar ABC transporter ATP-binding protein;
335-504 1.24e-06

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 51.33  E-value: 1.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 335 EFKNVSFHFEDDPNTDVLKNISLKASPGQTIAILGETGAGKSTL-VNLICRFYDP-TSGEILIDGVDARKWHVRE-LRNH 411
Cdd:NF040905 259 EVKNWTVYHPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELaMSVFGRSYGRnISGTVFKDGKEVDVSTVSDaIDAG 338
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 412 IATVMQDI----FLFSDTIEGNIafgapdaTMEDVRRMARIADADHFIET-MPESYDT---I----VGERGVGLSGGQKQ 479
Cdd:NF040905 339 LAYVTEDRkgygLNLIDDIKRNI-------TLANLGKVSRRGVIDENEEIkVAEEYRKkmnIktpsVFQKVGNLSGGNQQ 411
                        170       180
                 ....*....|....*....|....*
gi 404223395 480 RISLARALLKNPSILILDDTTSAVD 504
Cdd:NF040905 412 KVVLSKWLFTDPDVLILDEPTRGID 436
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
352-531 1.55e-06

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 50.96  E-value: 1.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 352 LKNISLKASPGQ-----TIAILGETGAGKSTLVNLICRFYDPTSGEILIDgvdarkwhVRelrnhIATVMQDIFlfsdti 426
Cdd:PRK13409 350 LGDFSLEVEGGEiyegeVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE--------LK-----ISYKPQYIK------ 410
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 427 egniafGAPDATMEDVRRMARIADADHFIET-------MPESYDTIVGErgvgLSGGQKQRISLARALLKNPSILILDDT 499
Cdd:PRK13409 411 ------PDYDGTVEDLLRSITDDLGSSYYKSeiikplqLERLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEP 480
                        170       180       190
                 ....*....|....*....|....*....|....
gi 404223395 500 TSAVDMETEVKIQGELKKITENT--TTFIIAHRI 531
Cdd:PRK13409 481 SAHLDVEQRLAVAKAIRRIAEEReaTALVVDHDI 514
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
473-546 1.73e-06

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


Pssm-ID: 213205 [Multi-domain]  Cd Length: 176  Bit Score: 48.47  E-value: 1.73e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 404223395 473 LSGGQKQRISLARALLKNP--SILILDDTTSAVDMETEVKIQGELKK-ITENTTTFIIAHRISSVKEADEILILNHG 546
Cdd:cd03238   88 LSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQDINQLLEVIKGlIDLGNTVILIEHNLDVLSSADWIIDFGPG 164
ABC_6TM_AarD_CydDC_like cd18561
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ...
67-276 1.75e-06

Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and similar proteins; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).


Pssm-ID: 350005 [Multi-domain]  Cd Length: 289  Bit Score: 49.97  E-value: 1.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  67 IIRTICRYTYQIMCERIGQNSLFRIREDLYKKLQSLDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVsyniLENVFL-FS 145
Cdd:cd18561   47 VLRAALLWLRERVAHRAAQRVKQHLRRRLFAKLLKLGPGYLEGERTGELQTTVVDGVEALEAYYGRY----LPQLLVaLL 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 146 FAIII---MAAIDWKLTLALVIVTPLIAILTMKMSSKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFH 222
Cdd:cd18561  123 GPLLIliyLFFLDPLVALILLVFALLIPLSPALWDRLAKDTGRRHWAAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELA 202
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 404223395 223 EHNEDFKKRNLDSADVSRTYLPVLDSLAGMLVVITLIFGGYLVIKGQMTLGDLV 276
Cdd:cd18561  203 ARAEDLRQATMKVLAVSLLSSGIMGLATALGTALALGVGALRVLGGQLTLSSLL 256
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
441-562 1.77e-06

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 50.50  E-value: 1.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 441 DVRRMARIADADHFIETMpeSYDTIVGERGVGLSGGQKQRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITE 520
Cdd:NF000106 115 DLSRKDARARADELLERF--SLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVR 192
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 404223395 521 NTTTFIIAHRISSVKE--ADEILILNHGEIIERGTHSSLLAEKG 562
Cdd:NF000106 193 DGATVLLTTQYMEEAEqlAHELTVIDRGRVIADGKVDELKTKVG 236
ABC_6TM_ABCB6 cd18581
Six-transmembrane helical domain of the ATP-binding cassette subfamily B member 6, ...
82-293 2.14e-06

Six-transmembrane helical domain of the ATP-binding cassette subfamily B member 6, mitochondrial; This group represents the ABCB6 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. ABCB6 is originally identified as a porphyrin transporter present in the outer membrane of mitochondria. It is highly expressed in cells resistance to arsenic and protects against arsenic cytotoxicity. Moreover, ABCB6 (ABC transporter subfamily B, member 6) is closely related to yeast ATM1 and human ABCB7, which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia.


Pssm-ID: 350025 [Multi-domain]  Cd Length: 300  Bit Score: 49.55  E-value: 2.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  82 RIGQNSLFRIREDLYKKLQSLDFDFFNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENVFLFSFAIIIMAAidwkltlA 161
Cdd:cd18581   72 PVQQFTTREISVKLFAHLHSLSLRWHLSRKTGEVLRVMDRGTSSINSLLSYVLFNIGPTIADIIIAIIYFAI-------A 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 162 LVIVTPLIAILTMKMSSKAQPVFYEIRESFSRLNSMVEENISGNRV--------VKAFAREDFEMKKFHEHNEDFKKrnl 233
Cdd:cd18581  145 FNPWFGLIVFVTMALYLILTIIITEWRTKFRREMNKLDNEKRAKAVdsllnfetVKYYNAERFEVERYRRAIDDYQV--- 221
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 404223395 234 dsAD-VSRTYLPVLDSLAGMLVVITLIFG----GYLVIKGQMTLGDLVAFNGFLWMLNGPMRMSG 293
Cdd:cd18581  222 --AEwKSNASLNLLNTAQNLIITIGLLAGsllcAYFVVEGKLTVGDFVLFLTYIIQLYAPLNFFG 284
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
319-507 2.24e-06

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 50.50  E-value: 2.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 319 IPihaekPAPSLQGHV-EFKNVSFHFEDDpntdVL-KNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILI- 395
Cdd:PRK11819 314 IP-----PGPRLGDKViEAENLSKSFGDR----LLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIg 384
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 396 DGVdarkwhvrelrnHIATVMQdiflFSDTIEgniafgaPDATMEDVrrmarIADADHFIE----TMP-ESYDTIVGERG 470
Cdd:PRK11819 385 ETV------------KLAYVDQ----SRDALD-------PNKTVWEE-----ISGGLDIIKvgnrEIPsRAYVGRFNFKG 436
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 404223395 471 ------VG-LSGGQKQRISLARALLKNPSILILDDTTSAVDMET 507
Cdd:PRK11819 437 gdqqkkVGvLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVET 480
PLN03073 PLN03073
ABC transporter F family; Provisional
320-513 2.57e-06

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 50.63  E-value: 2.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 320 PIHAEKPAPSLqghVEFKNVSFHFEDDPNtdVLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILidgvd 399
Cdd:PLN03073 498 PTPDDRPGPPI---ISFSDASFGYPGGPL--LFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF----- 567
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 400 aRKWHVRelrnhiatvmqdIFLFSDT-IEGniafgaPDATMEDVRRMARIadadhFIETMPESYDTIVGERGVG------ 472
Cdd:PLN03073 568 -RSAKVR------------MAVFSQHhVDG------LDLSSNPLLYMMRC-----FPGVPEQKLRAHLGSFGVTgnlalq 623
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 404223395 473 ----LSGGQKQRISLARALLKNPSILILDDTTSAVDME-TEVKIQG 513
Cdd:PLN03073 624 pmytLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDaVEALIQG 669
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
338-507 7.81e-06

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 48.79  E-value: 7.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 338 NVSFHFEDDPntdVLKNISLKASPGQTIAILGETGAGKSTLVNLIcrfydptSGEILIDgvDARKWHVRELRnhIATVMQ 417
Cdd:PRK11147   8 GAWLSFSDAP---LLDNAELHIEDNERVCLVGRNGAGKSTLMKIL-------NGEVLLD--DGRIIYEQDLI--VARLQQ 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 418 DIflfSDTIEGN----IAFG------------------APDATMEDVRRMARI-ADADH------------FIETMPESY 462
Cdd:PRK11147  74 DP---PRNVEGTvydfVAEGieeqaeylkryhdishlvETDPSEKNLNELAKLqEQLDHhnlwqlenrineVLAQLGLDP 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 404223395 463 DTIVGErgvgLSGGQKQRISLARALLKNPSILILDDTTSAVDMET 507
Cdd:PRK11147 151 DAALSS----LSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIET 191
ABC_6TM_ABCC_D2 cd18580
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ...
106-301 9.06e-06

Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.


Pssm-ID: 350024 [Multi-domain]  Cd Length: 294  Bit Score: 47.88  E-value: 9.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 106 FFNNTRVGDIMARMTGDTDAIRHFVSWVSYNILENVFLFSFAIIIMAAIDWKLTLALVIVTPLIAILTMkmsskaqpvFY 185
Cdd:cd18580   89 FFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVYYLLQR---------YY 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 186 -----EIR----ESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHnedfkkrnLDSAdvSRTYLP----------VL 246
Cdd:cd18580  160 lrtsrQLRrlesESRSPLYSHFSETLSGLSTIRAFGWQERFIEENLRL--------LDAS--QRAFYLllavqrwlglRL 229
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 404223395 247 DSLAGMLVVITLIFGgyLVIKGQMTLGDL-VAFN---GFLWMLNGPMRMSGWLIND---VQR 301
Cdd:cd18580  230 DLLGALLALVVALLA--VLLRSSISAGLVgLALTyalSLTGSLQWLVRQWTELETSmvsVER 289
PLN03140 PLN03140
ABC transporter G family member; Provisional
351-504 9.24e-06

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 48.69  E-value: 9.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  351 VLKNISLKASPGQTIAILGETGAGKSTLVNLIC--RFYDPTSGEILIDGVDARKWHVRELRNHIAtvMQDIFLFSDTIEG 428
Cdd:PLN03140  895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAgrKTGGYIEGDIRISGFPKKQETFARISGYCE--QNDIHSPQVTVRE 972
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 404223395  429 NIAFGAPDATMEDVRRMARIADADHFIE--TMPESYDTIVGERGV-GLSGGQKQRISLARALLKNPSILILDDTTSAVD 504
Cdd:PLN03140  973 SLIYSAFLRLPKEVSKEEKMMFVDEVMElvELDNLKDAIVGLPGVtGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 1051
ABC_6TM_PrtD_like cd18586
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS ...
90-294 1.30e-05

Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS metalloprotease secretion system, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) such as PrtD, which is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. The Aquifex aeolicus PrtDEF of T1SS is composed of an inner-membrane ABC transporter (PrtD), a periplasmic membrane-fusion protein (PrtE), and an outer-membrane porin (PrtF). These three components assemble into complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides


Pssm-ID: 350030 [Multi-domain]  Cd Length: 291  Bit Score: 47.21  E-value: 1.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  90 RIREDLYKKLQSLDFdffnNTRVGDIMARMTGDTDAIRHFVSWVSyniLENVFLFSFAIIIMAAI----DWKLTLALVIV 165
Cdd:cd18586   76 ELGRRVFRAVLELPL----ESRPSGYWQQLLRDLDTLRNFLTGPS---LFAFFDLPWAPLFLAVIflihPPLGWVALVGA 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 166 TPLIAILTMKMSSKAQPVFYEIRESFSRlNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKKRNLDSADVSRTYLPV 245
Cdd:cd18586  149 PVLVGLAWLNHRATRKPLGEANEAQAAR-DALAAETLRNAETIKALGMLGNLRRRWEARHAETLELQIRASDLAGAISAI 227
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 404223395 246 LDSLAGMLVVITLIFGGYLVIKGQMTLGDLVAFNgflwMLNG----PMR--MSGW 294
Cdd:cd18586  228 GKTLRMALQSLILGVGAYLVIDGELTIGALIAAS----ILSGralaPIDqlVGAW 278
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
471-547 2.17e-05

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


Pssm-ID: 213189 [Multi-domain]  Cd Length: 177  Bit Score: 45.26  E-value: 2.17e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 404223395 471 VGLSGGQKQRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITENT--TTFIIAHRISSVKEADEILILNHGE 547
Cdd:cd03222   70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGkkTALVVEHDLAVLDYLSDRIHVFEGE 148
PLN03140 PLN03140
ABC transporter G family member; Provisional
351-559 2.25e-05

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 47.53  E-value: 2.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  351 VLKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPT---SGEILIDGVDARKWHVRELRNHIAtvMQDIFLFSDTIE 427
Cdd:PLN03140  180 ILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSlkvSGEITYNGYRLNEFVPRKTSAYIS--QNDVHVGVMTVK 257
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  428 GNIAFGAP--------DATMEDVRRM--ARI---ADADHFIE---------TMPESY-----------DTIVGERGV-GL 473
Cdd:PLN03140  258 ETLDFSARcqgvgtryDLLSELARREkdAGIfpeAEVDLFMKatamegvksSLITDYtlkilgldickDTIVGDEMIrGI 337
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  474 SGGQKQRISLARALLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIAHRISSVKEA----DEILILNHGEII 549
Cdd:PLN03140  338 SGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLMSLLQPAPETfdlfDDIILLSEGQIV 417
                         250
                  ....*....|
gi 404223395  550 ERGTHSSLLA 559
Cdd:PLN03140  418 YQGPRDHILE 427
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
352-531 2.44e-05

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


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 47.09  E-value: 2.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 352 LKNISLKASPGQ-----TIAILGETGAGKSTLVNLICRFYDPTSGEI------------LIDGVDARkwhVRE-LRNHIA 413
Cdd:COG1245  351 YGGFSLEVEGGEiregeVLGIVGPNGIGKTTFAKILAGVLKPDEGEVdedlkisykpqyISPDYDGT---VEEfLRSANT 427
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 414 TVMQDIFLFSdtiegniafgapdatmEDVRRMAriadadhfIETMpesYDTIVGErgvgLSGGQKQRISLARALLKNPSI 493
Cdd:COG1245  428 DDFGSSYYKT----------------EIIKPLG--------LEKL---LDKNVKD----LSGGELQRVAIAACLSRDADL 476
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 404223395 494 LILDDTTSAVDMETEVKIQGELKKITENT--TTFIIAHRI 531
Cdd:COG1245  477 YLLDEPSAHLDVEQRLAVAKAIRRFAENRgkTAMVVDHDI 516
PRK13546 PRK13546
teichoic acids export ABC transporter ATP-binding subunit TagH;
352-536 4.71e-05

teichoic acids export ABC transporter ATP-binding subunit TagH;


Pssm-ID: 184131 [Multi-domain]  Cd Length: 264  Bit Score: 45.19  E-value: 4.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 352 LKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEILIDGvDARKWHVRELRNHIATVMQdiflfsdtiegNIA 431
Cdd:PRK13546  40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-EVSVIAISAGLSGQLTGIE-----------NIE 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 432 FG------APDATMEDVRRMARIADADHFIETMPESYdtivgergvglSGGQKQRISLARALLKNPSILILDDTTSAVDm 505
Cdd:PRK13546 108 FKmlcmgfKRKEIKAMTPKIIEFSELGEFIYQPVKKY-----------SSGMRAKLGFSINITVNPDILVIDEALSVGD- 175
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 404223395 506 etEVKIQGELKKITE----NTTTFIIAHRISSVKE 536
Cdd:PRK13546 176 --QTFAQKCLDKIYEfkeqNKTIFFVSHNLGQVRQ 208
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
361-529 5.67e-05

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 45.96  E-value: 5.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 361 PGQTIAILGETGAGKSTLVNLI--------CRFYDPTSGEILIDgvdarkwHVRelrnhiATVMQDifLFSDTIEGNIaf 432
Cdd:PRK13409  98 EGKVTGILGPNGIGKTTAVKILsgelipnlGDYEEEPSWDEVLK-------RFR------GTELQN--YFKKLYNGEI-- 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 433 gapdatmedvrrmaRIADADHFIETMPESYDTIVG-------ERGV-------------------GLSGGQKQRISLARA 486
Cdd:PRK13409 161 --------------KVVHKPQYVDLIPKVFKGKVRellkkvdERGKldevverlglenildrdisELSGGELQRVAIAAA 226
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 404223395 487 LLKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIAH 529
Cdd:PRK13409 227 LLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEH 269
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
473-553 6.89e-05

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


Pssm-ID: 273184 [Multi-domain]  Cd Length: 925  Bit Score: 45.77  E-value: 6.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  473 LSGGQKQRISLARALLK---NPSILILDDTTSAVDMETEVKIQGELKKITEN-TTTFIIAHRISSVKEADEILIL----- 543
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKrstGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKgNTVVVIEHNLDVIKTADYIIDLgpegg 909
                          90
                  ....*....|.
gi 404223395  544 -NHGEIIERGT 553
Cdd:TIGR00630 910 dGGGTVVASGT 920
PRK01889 PRK01889
GTPase RsgA; Reviewed
360-380 1.61e-04

GTPase RsgA; Reviewed


Pssm-ID: 234988 [Multi-domain]  Cd Length: 356  Bit Score: 44.15  E-value: 1.61e-04
                         10        20
                 ....*....|....*....|.
gi 404223395 360 SPGQTIAILGETGAGKSTLVN 380
Cdd:PRK01889 193 SGGKTVALLGSSGVGKSTLVN 213
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
352-548 7.63e-04

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 42.41  E-value: 7.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 352 LKNISLKASPGQTIAILGETGAGKSTLVNLICRFYDPTSGEIlidgvdarKWHVRELRNHIA-TVMQDIFLF------SD 424
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTI--------TLHGKKINNHNAnEAINHGFALvteerrST 335
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 425 TIEGN--IAFGAPDATME---------DVRRMAriADADHFIETM---PESYDTIVGErgvgLSGGQKQRISLARALLKN 490
Cdd:PRK10982 336 GIYAYldIGFNSLISNIRnyknkvgllDNSRMK--SDTQWVIDSMrvkTPGHRTQIGS----LSGGNQQKVIIGRWLLTQ 409
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 404223395 491 PSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIahrISS-----VKEADEILILNHGEI 548
Cdd:PRK10982 410 PEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIII---ISSempelLGITDRILVMSNGLV 469
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
471-543 2.83e-03

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


Pssm-ID: 213194 [Multi-domain]  Cd Length: 162  Bit Score: 38.88  E-value: 2.83e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 404223395 471 VGLSGGQKQRISLARAL----LKNPSILILDDTTSAVDMETEVKIQGELKKITENTTTFIIA-HRISSVKEADEILIL 543
Cdd:cd03227   76 LQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVItHLPELAELADKLIHI 153
ABC_6TM_T1SS_like cd18779
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ...
99-281 3.26e-03

uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.


Pssm-ID: 350052 [Multi-domain]  Cd Length: 294  Bit Score: 39.84  E-value: 3.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  99 LQSLDFDFFNNTRVGDIMARMTGDTdAIR-----HFVSWVsyniLENVFLFSFAIIIMAAiDWKLTLaLVIVTPLIAILT 173
Cdd:cd18779   85 LLRLPYRFFQQRSTGDLLMRLSSNA-TIRelltsQTLSAL----LDGTLVLGYLALLFAQ-SPLLGL-VVLGLAALQVAL 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 174 MKMSSKAQPVFYEiRE--SFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEH-----NEDFKKRNLDSadvsrtylpVL 246
Cdd:cd18779  158 LLATRRRVRELMA-RElaAQAEAQSYLVEALSGIETLKASGAEDRALDRWSNLfvdqlNASLRRGRLDA---------LV 227
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 404223395 247 DSLAGMLVVIT----LIFGGYLVIKGQMTLGDLVAFNGF 281
Cdd:cd18779  228 DALLATLRLAAplvlLWVGAWQVLDGQLSLGTMLALNAL 266
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
344-383 3.68e-03

Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.


Pssm-ID: 206747 [Multi-domain]  Cd Length: 211  Bit Score: 38.92  E-value: 3.68e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 404223395 344 EDDPNTDVLKNIsLKaspGQTIAILGETGAGKSTLVNLIC 383
Cdd:cd01854   71 KTGEGLDELREL-LK---GKTSVLVGQSGVGKSTLLNALL 106
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
473-543 3.75e-03

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 40.58  E-value: 3.75e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 404223395  473 LSGGQKQRISLARALL---KNPSILILDDTTSAVDM-ETEVKIQGELKKITENTTTFIIAHRISSVKEADEILIL 543
Cdd:PRK00635  810 LSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLHThDIKALIYVLQSLTHQGHTVVIIEHNMHVVKVADYVLEL 884
ABC_6TM_LapB_like cd18587
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; ...
141-287 4.54e-03

Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), such as LapB. LapB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion, LapA is a RTX (repeats in toxin) protein found in Pseudomonas fluorescens and is required for biofilm formation in this organism. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. In this T1SS system, LapB is a cytoplasmic membrane-localized ATPase, LapC is a membrane fusion protein, and LapE is an outer membrane protein.


Pssm-ID: 350031  Cd Length: 293  Bit Score: 39.34  E-value: 4.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395 141 VFLFsfaIIIMAAIDWKLTLALVIVTPLIAILT------MKMSSKAQpvfyeIRESFSRlNSMVEENISGNRVVKAFARE 214
Cdd:cd18587  128 VLLF---LAVIALIGGPLALVPLVAIPLVLLYGlllqkpLRRLVEES-----MRESAQK-NALLVESLSGLETIKALGAE 198
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 404223395 215 DfemkKFHEHNEDFKKRNLDSADVSRTYLPVLDSLAGMLV----VITLIFGGYLVIKGQMTLGDLVAFNgflwMLNG 287
Cdd:cd18587  199 G----RMQRRWEEAVAALARSSLKSRLLSSSATNFAQFVQqlvtVAIVIVGVYLISDGELTMGGLIACV----ILSG 267
ABC_6TM_AarD_CydDC_like cd18781
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC cysteine ...
7-230 7.92e-03

uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and similar proteins; This subgroup belongs to the ABC_6TM_AarD_CydDC_like subgroup of the ABC_6TM exporter family. The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs). The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.


Pssm-ID: 350054 [Multi-domain]  Cd Length: 290  Bit Score: 38.67  E-value: 7.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395   7 IWQYVRkyrlLMIGVFILIFIASGISIIYPllggkviddvvYQNKTNLLIPLLLIMIISTIIRTICRYTYQIMCERIGQN 86
Cdd:cd18781    3 LLQWIS----LLANIAFVFSIANLLQKLLE-----------GKLTTASLLIVLGILAIAIIVRFICTRLASRASYRASAD 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 404223395  87 SLFRIREDLYKKLQSLDFDFFNNTRVGDIMARMTGDTDAI----RHFVSWVSYNILENVFLFsfaiIIMAAIDWKLTLAL 162
Cdd:cd18781   68 VKKTLREKIYDKLLRLGPSYQEKVSTAEVVQLSVEGVEQLeiyfGRYLPQFFYSMLAPLTLF----VVLAPINWKAALVL 143
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 404223395 163 VIVTPLIAILTMKMSSKAQPVFYEIRESFSRLNSMVEENISGNRVVKAFAREDFEMKKFHEHNEDFKK 230
Cdd:cd18781  144 LICVPLIPISIIAVQKIAKKLLSKYWGSYTDLGDSFLENLQGLTTLKIYQADERRHEEMNEEAEDFRK 211
PLN03073 PLN03073
ABC transporter F family; Provisional
474-505 8.10e-03

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 39.07  E-value: 8.10e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 404223395 474 SGGQKQRISLARALLKNPSILILDDTTSAVDM 505
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDL 377
YeeP COG3596
Predicted GTPase [General function prediction only];
364-384 8.55e-03

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 38.59  E-value: 8.55e-03
                         10        20
                 ....*....|....*....|.
gi 404223395 364 TIAILGETGAGKSTLVNLICR 384
Cdd:COG3596   41 VIALVGKTGAGKSSLINALFG 61
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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