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Conserved domains on  [gi|961964003|ref|XP_014916780|]
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PREDICTED: ATP-binding cassette sub-family B member 9-like isoform X1 [Poecilia latipinna]

Protein Classification

ABC transporter permease/ATP-binding protein( domain architecture ID 1000000)

ABC transporter family protein containing permease (a six-transmembrane helical domain) and ATP-binding components functions as an ATP-dependent transporter, similar to ABC transporter B (ABCB) family members

CATH:  3.40.50.300
EC:  7.5.2.-
Gene Ontology:  GO:0140359|GO:0005524|GO:0042626|GO:0016887
PubMed:  11421270|19234479|26517899
SCOP:  4003976
TCDB:  3.A.1

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
3a01208 super family cl36782
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
 8-513 0e+00

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


The actual alignment was detected with superfamily member TIGR00958:

Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 711.49  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003    8 TLFFLLSSMAIGVRGGVFTLTMARLNVRLRSRLFRTLMTQEIAFFDENHTGDILSRLSADTTQVSDLISQNVNVFLRSVI 87
Cdd:TIGR00958 208 CLLSIASSVSAGLRGGSFNYTMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLV 287

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   88 KGTGFIIFMFRMSWKLTLVTMMGFPFIALVSKLYGEYYKKLTKEVQTVLAEANKVAEETISGMRTVRSFANESREANSYY 167
Cdd:TIGR00958 288 MLLGLLGFMLWLSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFK 367

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  168 AKLLVMFQLNKKQALAYACYMWSSCISELALEVAVLYYGGHLVLTDQLSSGGLISFFIYMLELGECFESIASVYSGLMQG 247
Cdd:TIGR00958 368 EALEETLQLNKRKALAYAGYLWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQA 447

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  248 VGAAEKVFEYLDRKPKHPADGTEAPNSCTGLVEFKDVTFAYPTRPETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLL 327
Cdd:TIGR00958 448 VGASEKVFEYLDRKPNIPLTGTLAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALL 527

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  328 ENFYLPQGGQVLLDGKPVNEFQHDYLHSKIALVGQEPVLFARTIKENISYGLSDVSMEMVVQAATKANAHDFITTLPKGY 407
Cdd:TIGR00958 528 QNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGY 607

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  408 DTSVGEKGLQLSGGQKQRVAIARALIRQPRVLILDEATSALDAESEHIVQQALNSimQEHTVLVIAHRLSTVEKADNIIV 487
Cdd:TIGR00958 608 DTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSR--ASRTVLLIAHRLSTVERADQILV 685

                         490       500
                  ....*....|....*....|....*.
gi 961964003  488 IDRGQVAERGTHSQLMATGGLYCKLV 513
Cdd:TIGR00958 686 LKKGSVVEMGTHKQLMEDQGCYKHLV 711
 
Name Accession Description Interval E-value
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
 8-513 0e+00

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 711.49  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003    8 TLFFLLSSMAIGVRGGVFTLTMARLNVRLRSRLFRTLMTQEIAFFDENHTGDILSRLSADTTQVSDLISQNVNVFLRSVI 87
Cdd:TIGR00958 208 CLLSIASSVSAGLRGGSFNYTMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLV 287

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   88 KGTGFIIFMFRMSWKLTLVTMMGFPFIALVSKLYGEYYKKLTKEVQTVLAEANKVAEETISGMRTVRSFANESREANSYY 167
Cdd:TIGR00958 288 MLLGLLGFMLWLSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFK 367

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  168 AKLLVMFQLNKKQALAYACYMWSSCISELALEVAVLYYGGHLVLTDQLSSGGLISFFIYMLELGECFESIASVYSGLMQG 247
Cdd:TIGR00958 368 EALEETLQLNKRKALAYAGYLWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQA 447

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  248 VGAAEKVFEYLDRKPKHPADGTEAPNSCTGLVEFKDVTFAYPTRPETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLL 327
Cdd:TIGR00958 448 VGASEKVFEYLDRKPNIPLTGTLAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALL 527

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  328 ENFYLPQGGQVLLDGKPVNEFQHDYLHSKIALVGQEPVLFARTIKENISYGLSDVSMEMVVQAATKANAHDFITTLPKGY 407
Cdd:TIGR00958 528 QNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGY 607

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  408 DTSVGEKGLQLSGGQKQRVAIARALIRQPRVLILDEATSALDAESEHIVQQALNSimQEHTVLVIAHRLSTVEKADNIIV 487
Cdd:TIGR00958 608 DTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSR--ASRTVLLIAHRLSTVERADQILV 685

                         490       500
                  ....*....|....*....|....*.
gi 961964003  488 IDRGQVAERGTHSQLMATGGLYCKLV 513
Cdd:TIGR00958 686 LKKGSVVEMGTHKQLMEDQGCYKHLV 711
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
9-519 0e+00

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 571.34  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   9 LFFLLSSMAIGVRGGVFTLTMARLNVRLRSRLFRTLMTQEIAFFDENHTGDILSRLSADTTQVSDLISQNVNVFLRSVIK 88
Cdd:COG1132   69 GLALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVT 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  89 GTGFIIFMFRMSWKLTLVTMMGFPFIALVSKLYGEYYKKLTKEVQTVLAEANKVAEETISGMRTVRSFANESREANSYYA 168
Cdd:COG1132  149 LIGALVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFRE 228

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 169 KLLVMFQLNKKQALAYACYM-WSSCISELALeVAVLYYGGHLVLTDQLSSGGLISFFIYMLELGECFESIASVYSGLMQG 247
Cdd:COG1132  229 ANEELRRANLRAARLSALFFpLMELLGNLGL-ALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRA 307

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 248 VGAAEKVFEYLDRKPKHP-ADGTEAPNSCTGLVEFKDVTFAYPtrPETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSL 326
Cdd:COG1132  308 LASAERIFELLDEPPEIPdPPGAVPLPPVRGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNL 385

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 327 LENFYLPQGGQVLLDGKPVNEFQHDYLHSKIALVGQEPVLFARTIKENISYGLSDVSMEMVVQAATKANAHDFITTLPKG 406
Cdd:COG1132  386 LLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDG 465

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 407 YDTSVGEKGLQLSGGQKQRVAIARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQEHTVLVIAHRLSTVEKADNII 486
Cdd:COG1132  466 YDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRIL 545

                        490       500       510
                 ....*....|....*....|....*....|...
gi 961964003 487 VIDRGQVAERGTHSQLMATGGLYCKLVQRQVLG 519
Cdd:COG1132  546 VLDDGRIVEQGTHEELLARGGLYARLYRLQFGE 578
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
 279-516 3.24e-138

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: 399.99  E-value: 3.24e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 279 VEFKDVTFAYPTRPETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHDYLHSKIA 358
Cdd:cd03249    1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 359 LVGQEPVLFARTIKENISYGLSDVSMEMVVQAATKANAHDFITTLPKGYDTSVGEKGLQLSGGQKQRVAIARALIRQPRV 438
Cdd:cd03249   81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 961964003 439 LILDEATSALDAESEHIVQQALNSIMQEHTVLVIAHRLSTVEKADNIIVIDRGQVAERGTHSQLMATGGLYCKLVQRQ 516
Cdd:cd03249  161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
36-516 1.43e-120

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 367.42  E-value: 1.43e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  36 LRSRLFRTLMTQEIAFFDENHTGDILSRLSADTTQVSDLISQNVNVFLR---SVIkgtGFIIFMFRMSWKLTLVTMMGFP 112
Cdd:PRK11176 100 MRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVRegaSII---GLFIMMFYYSWQLSLILIVIAP 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 113 FIALVSKLYGEYYKKLTKEVQTVLAEANKVAEETISGMRTVRSFANESREANSYYAKLLVMFQLNKKQALAyacymwSS- 191
Cdd:PRK11176 177 IVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRQQGMKMVSA------SSi 250

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 192 ------CISELALeVAVLYYGGHLVLTDQLSSGGLISFFIYMLELGECFESIASVYSGLMQGVGAAEKVFEYLDRKPKHP 265
Cdd:PRK11176 251 sdpiiqLIASLAL-AFVLYAASFPSVMDTLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFAILDLEQEKD 329

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 266 aDGTEAPNSCTGLVEFKDVTFAYPTRpETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPV 345
Cdd:PRK11176 330 -EGKRVIERAKGDIEFRNVTFTYPGK-EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDL 407

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 346 NEFQHDYLHSKIALVGQEPVLFARTIKENISYGLSDV-SMEMVVQAATKANAHDFITTLPKGYDTSVGEKGLQLSGGQKQ 424
Cdd:PRK11176 408 RDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQ 487

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 425 RVAIARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQEHTVLVIAHRLSTVEKADNIIVIDRGQVAERGTHSQLMA 504
Cdd:PRK11176 488 RIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLA 567

                        490
                 ....*....|..
gi 961964003 505 TGGLYCKLVQRQ 516
Cdd:PRK11176 568 QNGVYAQLHKMQ 579
ABC_membrane pfam00664
ABC transporter transmembrane region; This family represents a unit of six transmembrane ...
 7-228 6.17e-49

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


Pssm-ID: 459896 [Multi-domain]  Cd Length: 274  Bit Score: 170.52  E-value: 6.17e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003    7 FTLFFLLSSMAIGVRGGVFTLTMARLNVRLRSRLFRTLMTQEIAFFDENHTGDILSRLSADTTQVSDLISQNVNVFLRSV 86
Cdd:pfam00664  47 LLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSL 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   87 IKGTGFIIFMFRMSWKLTLVTMMGFPFIALVSKLYGEYYKKLTKEVQTVLAEANKVAEETISGMRTVRSFANESREANSY 166
Cdd:pfam00664 127 ATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKY 206

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 961964003  167 YAKLLVMFQLNKKQALAYA-CYMWSSCISELALeVAVLYYGGHLVLTDQLSSGGLISFFIYML 228
Cdd:pfam00664 207 DKALEEALKAGIKKAVANGlSFGITQFIGYLSY-ALALWFGAYLVISGELSVGDLVAFLSLFA 268
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
287-488 4.90e-22

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 93.84  E-value: 4.90e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 287 AYPTRPetdVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGkpvnefqhdylHSKIALVGQ---E 363
Cdd:NF040873   1 GYGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQrseV 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 364 PVLFARTIKENISYGL---------SDVSMEMVVQAATKANAhdfITTLPKgydTSVGEkglqLSGGQKQRVAIARALIR 434
Cdd:NF040873  67 PDSLPLTVRDLVAMGRwarrglwrrLTRDDRAAVDDALERVG---LADLAG---RQLGE----LSGGQRQRALLAQGLAQ 136

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 961964003 435 QPRVLILDEATSALDAESEHIVQQALNsimQEH----TVLVIAHRLSTVEKADNIIVI 488
Cdd:NF040873 137 EADLLLLDEPTTGLDAESRERIIALLA---EEHargaTVVVVTHDLELVRRADPCVLL 191
GguA NF040905
sugar ABC transporter ATP-binding protein;
297-495 2.35e-16

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 81.76  E-value: 2.35e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 297 LKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYlPQG---GQVLLDGKPVnEFQ--HDYLHSKIALVGQE----PVLf 367
Cdd:NF040905  17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHGsyeGEILFDGEVC-RFKdiRDSEALGIVIIHQElaliPYL- 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 368 arTIKENI-------SYGLSDvsmemvvQAATKANAHDFITT--LPKGYDTSVGEKGLqlsgGQKQRVAIARALIRQPRV 438
Cdd:NF040905  94 --SIAENIflgneraKRGVID-------WNETNRRARELLAKvgLDESPDTLVTDIGV----GKQQLVEIAKALSKDVKL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 961964003 439 LILDEATSAL-DAESEHIV-------QQALNSIMqehtvlvIAHRLSTVEK-ADNIIVIDRGQVAE 495
Cdd:NF040905 161 LILDEPTAALnEEDSAALLdlllelkAQGITSII-------ISHKLNEIRRvADSITVLRDGRTIE 219
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 306-490 1.25e-11

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 62.78  E-value: 1.25e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   306 PGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLdgkpvnefqhdylhskialvgqepvlfartikenisyglsdVSME 385
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY-----------------------------------------IDGE 39

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   386 MVVQAATKANAHdfittlpkgydTSVGEKGLQLSGGQKQRVAIARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQ 465
Cdd:smart00382  40 DILEEVLDQLLL-----------IIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLL 108

                          170       180       190
                   ....*....|....*....|....*....|..
gi 961964003   466 EH-------TVLVIAHRLSTVEKADNIIVIDR 490
Cdd:smart00382 109 LLlkseknlTVILTTNDEKDLGPALLRRRFDR 140
GguA NF040905
sugar ABC transporter ATP-binding protein;
259-449 5.86e-11

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 64.81  E-value: 5.86e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 259 DRKPKH-PADGTEapnsctgLVEFKDVTFAYPTRPETDVLKGVSFTLRPGEVTALVGPSGSGKSS-CVSLLENFYlpqG- 335
Cdd:NF040905 244 DRYPERtPKIGEV-------VFEVKNWTVYHPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTElAMSVFGRSY---Gr 313

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 336 ---GQVLLDGKPVnEFQ--HDYLHSKIALVGQEpvlfaR---------TIKENISY-GLSDVSMEMVV--QAATKAnAHD 398
Cdd:NF040905 314 nisGTVFKDGKEV-DVStvSDAIDAGLAYVTED-----RkgyglnlidDIKRNITLaNLGKVSRRGVIdeNEEIKV-AEE 386

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 961964003 399 FITTL----PkgydtSVGEKGLQLSGGQKQRVAIARALIRQPRVLILDEATSALD 449
Cdd:NF040905 387 YRKKMniktP-----SVFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGID 436
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
410-507 2.21e-07

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 53.20  E-value: 2.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 410 SVGEKGLQLSGGQKQRVAIARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQE-HTVLVIAHRLSTVEK-ADNIIV 487
Cdd:NF000106 137 AAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDgATVLLTTQYMEEAEQlAHELTV 216

                         90       100
                 ....*....|....*....|
gi 961964003 488 IDRGQVAERGTHSQLMATGG 507
Cdd:NF000106 217 IDRGRVIADGKVDELKTKVG 236
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
297-506 4.20e-05

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 46.66  E-value: 4.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 297 LKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQH-DYLHSKIALVGQ------EPVLfar 369
Cdd:NF033858  17 LDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHrRAVCPRIAYMPQglgknlYPTL--- 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 370 TIKENIS-----YGLSDVSMEMVVQAATKAnahdfiTTL------PKGydtsvgekglQLSGGQKQRVAIARALIRQPRV 438
Cdd:NF033858  94 SVFENLDffgrlFGQDAAERRRRIDELLRA------TGLapfadrPAG----------KLSGGMKQKLGLCCALIHDPDL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 439 LILDEATSALDAES-----EHIvqqalNSIMQEH---TVLViahrlST--VEKA---DNIIVIDRGQVAERGTHSQLMA- 504
Cdd:NF033858 158 LILDEPTTGVDPLSrrqfwELI-----DRIRAERpgmSVLV-----ATayMEEAerfDWLVAMDAGRVLATGTPAELLAr 227


                 ..
gi 961964003 505 TG 506
Cdd:NF033858 228 TG 229
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
300-449 1.73e-03

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 41.26  E-value: 1.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 300 VSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEfqHD--------YLHSKIAL-----VGQEPVL 366
Cdd:NF033858 285 VSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDA--GDiatrrrvgYMSQAFSLygeltVRQNLEL 362

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 367 FARTikenisYGLSDVSM-EMVVQAATKANAHDFITTLPKGydtsvgekglqLSGGQKQRVAIARALIRQPRVLILDEAT 445
Cdd:NF033858 363 HARL------FHLPAAEIaARVAEMLERFDLADVADALPDS-----------LPLGIRQRLSLAVAVIHKPELLILDEPT 425


                 ....
gi 961964003 446 SALD 449
Cdd:NF033858 426 SGVD 429
 
Name Accession Description Interval E-value
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
 8-513 0e+00

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 711.49  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003    8 TLFFLLSSMAIGVRGGVFTLTMARLNVRLRSRLFRTLMTQEIAFFDENHTGDILSRLSADTTQVSDLISQNVNVFLRSVI 87
Cdd:TIGR00958 208 CLLSIASSVSAGLRGGSFNYTMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLV 287

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   88 KGTGFIIFMFRMSWKLTLVTMMGFPFIALVSKLYGEYYKKLTKEVQTVLAEANKVAEETISGMRTVRSFANESREANSYY 167
Cdd:TIGR00958 288 MLLGLLGFMLWLSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFK 367

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  168 AKLLVMFQLNKKQALAYACYMWSSCISELALEVAVLYYGGHLVLTDQLSSGGLISFFIYMLELGECFESIASVYSGLMQG 247
Cdd:TIGR00958 368 EALEETLQLNKRKALAYAGYLWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQA 447

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  248 VGAAEKVFEYLDRKPKHPADGTEAPNSCTGLVEFKDVTFAYPTRPETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLL 327
Cdd:TIGR00958 448 VGASEKVFEYLDRKPNIPLTGTLAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALL 527

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  328 ENFYLPQGGQVLLDGKPVNEFQHDYLHSKIALVGQEPVLFARTIKENISYGLSDVSMEMVVQAATKANAHDFITTLPKGY 407
Cdd:TIGR00958 528 QNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGY 607

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  408 DTSVGEKGLQLSGGQKQRVAIARALIRQPRVLILDEATSALDAESEHIVQQALNSimQEHTVLVIAHRLSTVEKADNIIV 487
Cdd:TIGR00958 608 DTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSR--ASRTVLLIAHRLSTVERADQILV 685

                         490       500
                  ....*....|....*....|....*.
gi 961964003  488 IDRGQVAERGTHSQLMATGGLYCKLV 513
Cdd:TIGR00958 686 LKKGSVVEMGTHKQLMEDQGCYKHLV 711
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
9-519 0e+00

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 571.34  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   9 LFFLLSSMAIGVRGGVFTLTMARLNVRLRSRLFRTLMTQEIAFFDENHTGDILSRLSADTTQVSDLISQNVNVFLRSVIK 88
Cdd:COG1132   69 GLALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVT 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  89 GTGFIIFMFRMSWKLTLVTMMGFPFIALVSKLYGEYYKKLTKEVQTVLAEANKVAEETISGMRTVRSFANESREANSYYA 168
Cdd:COG1132  149 LIGALVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFRE 228

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 169 KLLVMFQLNKKQALAYACYM-WSSCISELALeVAVLYYGGHLVLTDQLSSGGLISFFIYMLELGECFESIASVYSGLMQG 247
Cdd:COG1132  229 ANEELRRANLRAARLSALFFpLMELLGNLGL-ALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRA 307

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 248 VGAAEKVFEYLDRKPKHP-ADGTEAPNSCTGLVEFKDVTFAYPtrPETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSL 326
Cdd:COG1132  308 LASAERIFELLDEPPEIPdPPGAVPLPPVRGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNL 385

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 327 LENFYLPQGGQVLLDGKPVNEFQHDYLHSKIALVGQEPVLFARTIKENISYGLSDVSMEMVVQAATKANAHDFITTLPKG 406
Cdd:COG1132  386 LLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDG 465

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 407 YDTSVGEKGLQLSGGQKQRVAIARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQEHTVLVIAHRLSTVEKADNII 486
Cdd:COG1132  466 YDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRIL 545

                        490       500       510
                 ....*....|....*....|....*....|...
gi 961964003 487 VIDRGQVAERGTHSQLMATGGLYCKLVQRQVLG 519
Cdd:COG1132  546 VLDDGRIVEQGTHEELLARGGLYARLYRLQFGE 578
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
 7-517 3.80e-159

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: 470.86  E-value: 3.80e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   7 FTLFFLLSSMAIGVRGGVFTLTMARLNVRLRSRLFRTLMTQEIAFFDENHTGDILSRLSaDTTQVSDLISQNVNVFLRSV 86
Cdd:COG2274  202 LLLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFR-DVESIREFLTGSLLTALLDL 280

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  87 IKGTGFIIFMFRMSWKLTLVTMMGFPFIALVSKLYGEYYKKLTKEVQTVLAEANKVAEETISGMRTVRSFANESR---EA 163
Cdd:COG2274  281 LFVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRfrrRW 360

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 164 NSYYAKLL-VMFQLNKKQALAYAcymWSSCISELALeVAVLYYGGHLVLTDQLSSGGLISFFIYMLELGECFESIASVYS 242
Cdd:COG2274  361 ENLLAKYLnARFKLRRLSNLLST---LSGLLQQLAT-VALLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQ 436

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 243 GLMQGVGAAEKVFEYLDRKPKHPADGTEA-PNSCTGLVEFKDVTFAYPTRpETDVLKGVSFTLRPGEVTALVGPSGSGKS 321
Cdd:COG2274  437 RFQDAKIALERLDDILDLPPEREEGRSKLsLPRLKGDIELENVSFRYPGD-SPPVLDNISLTIKPGERVAIVGRSGSGKS 515

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 322 SCVSLLENFYLPQGGQVLLDGKPVNEFQHDYLHSKIALVGQEPVLFARTIKENISYGLSDVSMEMVVQAATKANAHDFIT 401
Cdd:COG2274  516 TLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIE 595

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 402 TLPKGYDTSVGEKGLQLSGGQKQRVAIARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQEHTVLVIAHRLSTVEK 481
Cdd:COG2274  596 ALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRL 675

                        490       500       510
                 ....*....|....*....|....*....|....*.
gi 961964003 482 ADNIIVIDRGQVAERGTHSQLMATGGLYCKLVQRQV 517
Cdd:COG2274  676 ADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQQL 711
MsbA_rel TIGR02204
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ...
 12-516 1.78e-156

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: 459.55  E-value: 1.78e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   12 LLSSMAIGVRGGVFTLTMARLNVRLRSRLFRTLMTQEIAFFDENHTGDILSRLSADTTQVSDLISQNVNVFLRSVIKGTG 91
Cdd:TIGR02204  69 LVLALGTAARFYLVTWLGERVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIG 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   92 FIIFMFRMSWKLTLVTMMGFPFIALVSKLYGEYYKKLTKEVQTVLAEANKVAEETISGMRTVRSFANESREANSYYAKLL 171
Cdd:TIGR02204 149 GLIMMFITSPKLTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVE 228

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  172 VMFQLnKKQALAYACYMWSSCIS-ELALEVAVLYYGGHLVLTDQLSSGGLISFFIYMLELGECFESIASVYSGLMQGVGA 250
Cdd:TIGR02204 229 KAYEA-ARQRIRTRALLTAIVIVlVFGAIVGVLWVGAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGA 307

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  251 AEKVFEYLDRKP--KHPADGTEAPNSCTGLVEFKDVTFAYPTRPETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLE 328
Cdd:TIGR02204 308 AERLIELLQAEPdiKAPAHPKTLPVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLL 387

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  329 NFYLPQGGQVLLDGKPVNEFQHDYLHSKIALVGQEPVLFARTIKENISYGLSDVSMEMVVQAATKANAHDFITTLPKGYD 408
Cdd:TIGR02204 388 RFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFISALPEGYD 467

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  409 TSVGEKGLQLSGGQKQRVAIARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQEHTVLVIAHRLSTVEKADNIIVI 488
Cdd:TIGR02204 468 TYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVM 547

                         490       500
                  ....*....|....*....|....*...
gi 961964003  489 DRGQVAERGTHSQLMATGGLYCKLVQRQ 516
Cdd:TIGR02204 548 DQGRIVAQGTHAELIAKGGLYARLARLQ 575
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
 36-512 1.28e-148

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: 439.15  E-value: 1.28e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   36 LRSRLFRTLMTQEIAFFDENHTGDILSRLSADTTQVSDLISQNVNVFLRSVIKGTGFIIFMFRMSWKLTLVTMMGFPFIA 115
Cdd:TIGR02203  89 IRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLTLIVVVMLPVLS 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  116 LVSKLYGEYYKKLTKEVQTVLAEANKVAEETISGMRTVRSFANESREANSYYAKLLVMFQLNKKQALAYACYmwsSCISE 195
Cdd:TIGR02203 169 ILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSAGSIS---SPITQ 245

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  196 LALEVA---VLYYGGHLVLTDQLSSGGLISFFIYMLELGECFESIASVYSGLMQGVGAAEKVFEYLDRKPKhPADGTEAP 272
Cdd:TIGR02203 246 LIASLAlavVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPPE-KDTGTRAI 324

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  273 NSCTGLVEFKDVTFAYPTRpETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHDY 352
Cdd:TIGR02203 325 ERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLAS 403

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  353 LHSKIALVGQEPVLFARTIKENISYG-LSDVSMEMVVQAATKANAHDFITTLPKGYDTSVGEKGLQLSGGQKQRVAIARA 431
Cdd:TIGR02203 404 LRRQVALVSQDVVLFNDTIANNIAYGrTEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARA 483

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  432 LIRQPRVLILDEATSALDAESEHIVQQALNSIMQEHTVLVIAHRLSTVEKADNIIVIDRGQVAERGTHSQLMATGGLYCK 511
Cdd:TIGR02203 484 LLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNGLYAQ 563


                  .
gi 961964003  512 L 512
Cdd:TIGR02203 564 L 564
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
 279-516 3.24e-138

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: 399.99  E-value: 3.24e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 279 VEFKDVTFAYPTRPETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHDYLHSKIA 358
Cdd:cd03249    1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 359 LVGQEPVLFARTIKENISYGLSDVSMEMVVQAATKANAHDFITTLPKGYDTSVGEKGLQLSGGQKQRVAIARALIRQPRV 438
Cdd:cd03249   81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 961964003 439 LILDEATSALDAESEHIVQQALNSIMQEHTVLVIAHRLSTVEKADNIIVIDRGQVAERGTHSQLMATGGLYCKLVQRQ 516
Cdd:cd03249  161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
ABC_6TM_ABCB9_like cd18784
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ...
 7-254 2.90e-137

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: 399.76  E-value: 2.90e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   7 FTLFFLLSSMAIGVRGGVFTLTMARLNVRLRSRLFRTLMTQEIAFFDENHTGDILSRLSADTTQVSDLISQNVNVFLRSV 86
Cdd:cd18784   42 MGLLAIASSVAAGIRGGLFTLAMARLNIRIRNLLFRSIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSL 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  87 IKGTGFIIFMFRMSWKLTLVTMMGFPFIALVSKLYGEYYKKLTKEVQTVLAEANKVAEETISGMRTVRSFANESREANSY 166
Cdd:cd18784  122 VKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYYKKLSKAVQDSLAKANEVAEETISSIRTVRSFANEDGEANRY 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 167 YAKLLVMFQLNKKQALAYACYMWSSCISELALEVAVLYYGGHLVLTDQLSSGGLISFFIYMLELGECFESIASVYSGLMQ 246
Cdd:cd18784  202 SEKLKDTYKLKIKEALAYGGYVWSNELTELALTVSTLYYGGHLVITGQISGGNLISFILYQLELGSCLESVGSVYTGLMQ 281


                 ....*...
gi 961964003 247 GVGAAEKV 254
Cdd:cd18784  282 AVGAAEKV 289
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
 268-493 1.59e-134

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: 390.29  E-value: 1.59e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 268 GTEAPNSCTGLVEFKDVTFAYPTRPETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNE 347
Cdd:cd03248    1 GSLAPDHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 348 FQHDYLHSKIALVGQEPVLFARTIKENISYGLSDVSMEMVVQAATKANAHDFITTLPKGYDTSVGEKGLQLSGGQKQRVA 427
Cdd:cd03248   81 YEHKYLHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVA 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 961964003 428 IARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQEHTVLVIAHRLSTVEKADNIIVIDRGQV 493
Cdd:cd03248  161 IARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
36-516 1.43e-120

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 367.42  E-value: 1.43e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  36 LRSRLFRTLMTQEIAFFDENHTGDILSRLSADTTQVSDLISQNVNVFLR---SVIkgtGFIIFMFRMSWKLTLVTMMGFP 112
Cdd:PRK11176 100 MRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVRegaSII---GLFIMMFYYSWQLSLILIVIAP 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 113 FIALVSKLYGEYYKKLTKEVQTVLAEANKVAEETISGMRTVRSFANESREANSYYAKLLVMFQLNKKQALAyacymwSS- 191
Cdd:PRK11176 177 IVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRQQGMKMVSA------SSi 250

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 192 ------CISELALeVAVLYYGGHLVLTDQLSSGGLISFFIYMLELGECFESIASVYSGLMQGVGAAEKVFEYLDRKPKHP 265
Cdd:PRK11176 251 sdpiiqLIASLAL-AFVLYAASFPSVMDTLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFAILDLEQEKD 329

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 266 aDGTEAPNSCTGLVEFKDVTFAYPTRpETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPV 345
Cdd:PRK11176 330 -EGKRVIERAKGDIEFRNVTFTYPGK-EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDL 407

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 346 NEFQHDYLHSKIALVGQEPVLFARTIKENISYGLSDV-SMEMVVQAATKANAHDFITTLPKGYDTSVGEKGLQLSGGQKQ 424
Cdd:PRK11176 408 RDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQ 487

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 425 RVAIARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQEHTVLVIAHRLSTVEKADNIIVIDRGQVAERGTHSQLMA 504
Cdd:PRK11176 488 RIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLA 567

                        490
                 ....*....|..
gi 961964003 505 TGGLYCKLVQRQ 516
Cdd:PRK11176 568 QNGVYAQLHKMQ 579
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
 152-516 1.74e-119

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: 365.30  E-value: 1.74e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 152 TVRSFANESREANSYYAKL-----------LVMFQLNKKQALAYACYMwssciselaleVAVLYYGGHLVLTDQLSSGGL 220
Cdd:COG5265  230 TVKYFGNEAREARRYDEALaryeraavksqTSLALLNFGQALIIALGL-----------TAMMLMAAQGVVAGTMTVGDF 298

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 221 ISFFIYMLELGECFESIASVYSGLMQGVGAAEKVFEYLDRKPKhPADGTEAPNSCT--GLVEFKDVTFAY-PTRPetdVL 297
Cdd:COG5265  299 VLVNAYLIQLYIPLNFLGFVYREIRQALADMERMFDLLDQPPE-VADAPDAPPLVVggGEVRFENVSFGYdPERP---IL 374

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 298 KGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHDYLHSKIALVGQEPVLFARTIKENISY 377
Cdd:COG5265  375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAY 454

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 378 GLSDVSMEMVVQAATKANAHDFITTLPKGYDTSVGEKGLQLSGGQKQRVAIARALIRQPRVLILDEATSALDAESEHIVQ 457
Cdd:COG5265  455 GRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQ 534

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 961964003 458 QALNSIMQEHTVLVIAHRLSTVEKADNIIVIDRGQVAERGTHSQLMATGGLYCKLVQRQ 516
Cdd:COG5265  535 AALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQ 593
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
 2-507 3.46e-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: 3.46e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   2 SVAPPFTLFFLlssmAIGVRGGvftLTMAR--------LNVR--LRSRLFRTLMTQEIAFFDENHTGDILSRLsadTTQV 71
Cdd:COG4988   56 ALLPLLGLLLA----VLLLRAL---LAWLReraafraaARVKrrLRRRLLEKLLALGPAWLRGKSTGELATLL---TEGV 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  72 SDL---ISQNVNVFLRSVIKGTGFIIFMFRMSWKLTLVTMMGFP----FIALV----SKLYGEYYKKLTKEVQTVLaean 140
Cdd:COG4988  126 EALdgyFARYLPQLFLAALVPLLILVAVFPLDWLSGLILLVTAPliplFMILVgkgaAKASRRQWRALARLSGHFL---- 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 141 kvaeETISGMRTVRSFANESREANSYYA----------KLLVMFQLnkkqalayacymwSSCISEL------ALeVAVly 204
Cdd:COG4988  202 ----DRLRGLTTLKLFGRAKAEAERIAEasedfrkrtmKVLRVAFL-------------SSAVLEFfaslsiAL-VAV-- 261

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 205 YGGHLVLTDQLS-SGGLI------SFFIYMLELGECFEsiASvysglMQGVGAAEKVFEYLDRKPKHPADGTEAPNSCTG 277
Cdd:COG4988  262 YIGFRLLGGSLTlFAALFvlllapEFFLPLRDLGSFYH--AR-----ANGIAAAEKIFALLDAPEPAAPAGTAPLPAAGP 334

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 278 L-VEFKDVTFAYPTRPEtdVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHDYLHSK 356
Cdd:COG4988  335 PsIELEDVSFSYPGGRP--ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQ 412

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 357 IALVGQEPVLFARTIKENISYGLSDVSMEMVVQAATKANAHDFITTLPKGYDTSVGEKGLQLSGGQKQRVAIARALIRQP 436
Cdd:COG4988  413 IAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDA 492

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 961964003 437 RVLILDEATSALDAESEHIVQQALNSIMQEHTVLVIAHRLSTVEKADNIIVIDRGQVAERGTHSQLMATGG 507
Cdd:COG4988  493 PLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
 279-512 5.51e-110

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: 327.65  E-value: 5.51e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 279 VEFKDVTFAYPTRPETdVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHDYLHSKIA 358
Cdd:cd03251    1 VEFKNVTFRYPGDGPP-VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 359 LVGQEPVLFARTIKENISYGLSDVSMEMVVQAATKANAHDFITTLPKGYDTSVGEKGLQLSGGQKQRVAIARALIRQPRV 438
Cdd:cd03251   80 LVSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 961964003 439 LILDEATSALDAESEHIVQQALNSIMQEHTVLVIAHRLSTVEKADNIIVIDRGQVAERGTHSQLMATGGLYCKL 512
Cdd:cd03251  160 LILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
 1-515 2.43e-107

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: 332.89  E-value: 2.43e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   1 MSVAPPFTLFFLLSSmaiGVRG-----GVF-----------TLtmaRLNVRLRSRLFRTLMTQEIAFFDENHTGDILSRL 64
Cdd:COG4987   45 AALAPPILNLFVPIV---GVRAfaigrTVFrylerlvshdaTL---RLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRL 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  65 SADttqVSDLisqnVNVFLR-------SVIKGTGFIIFMFRMSWKLTLVTMMGFPFIALV----SKLYGeyyKKLTKEVQ 133
Cdd:COG4987  119 VAD---VDAL----DNLYLRvllpllvALLVILAAVAFLAFFSPALALVLALGLLLAGLLlpllAARLG---RRAGRRLA 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 134 TVLAEANKVAEETISGMRTVRSFANESREANSYYAKLLVMFQLNKKQALAYAcymWSSCISELALE---VAVLYYGGHLV 210
Cdd:COG4987  189 AARAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLARLSA---LAQALLQLAAGlavVAVLWLAAPLV 265

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 211 LTDQLSSGGLISFFIYMLELGECFESIASVYSGLMQGVGAAEKVFEYLDRKPKHPADGTEAPNSCTGLVEFKDVTFAYPT 290
Cdd:COG4987  266 AAGALSGPLLALLVLAALALFEALAPLPAAAQHLGRVRAAARRLNELLDAPPAVTEPAEPAPAPGGPSLELEDVSFRYPG 345

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 291 RPEtDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHDYLHSKIALVGQEPVLFART 370
Cdd:COG4987  346 AGR-PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTT 424

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 371 IKENISYGLSDVSMEMVVQAATKANAHDFITTLPKGYDTSVGEKGLQLSGGQKQRVAIARALIRQPRVLILDEATSALDA 450
Cdd:COG4987  425 LRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDA 504

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 961964003 451 ESEHIVQQALNSIMQEHTVLVIAHRLSTVEKADNIIVIDRGQVAERGTHSQLMATGGLYCKLVQR 515
Cdd:COG4987  505 ATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRYRQLYQR 569
ABC_6TM_TAP cd18572
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ...
 7-254 7.95e-107

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: 321.80  E-value: 7.95e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   7 FTLFFLLSSMAIGVRGGVFTLTMARLNVRLRSRLFRTLMTQEIAFFDENHTGDILSRLSADTTQVSDLISQNVNVFLRSV 86
Cdd:cd18572   42 LLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNL 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  87 IKGTGFIIFMFRMSWKLTLVTMMGFPFIALVSKLYGEYYKKLTKEVQTVLAEANKVAEETISGMRTVRSFANESREANSY 166
Cdd:cd18572  122 VQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRYYRKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARRY 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 167 YAKLLVMFQLNKKQALAYACYMWSSCISELALEVAVLYYGGHLVLTDQLSSGGLISFFIYMLELGECFESIASVYSGLMQ 246
Cdd:cd18572  202 ERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFYGGHLVLSGRMSAGQLVTFMLYQQQLGEAFQSLGDVFSSLMQ 281


                 ....*...
gi 961964003 247 GVGAAEKV 254
Cdd:cd18572  282 AVGAAEKV 289
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
 279-516 1.05e-105

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: 316.86  E-value: 1.05e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 279 VEFKDVTFAYPtrPETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHDYLHSKIA 358
Cdd:cd03253    1 IEFENVTFAYD--PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 359 LVGQEPVLFARTIKENISYGLSDVSMEMVVQAATKANAHDFITTLPKGYDTSVGEKGLQLSGGQKQRVAIARALIRQPRV 438
Cdd:cd03253   79 VVPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPI 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 961964003 439 LILDEATSALDAESEHIVQQALNSIMQEHTVLVIAHRLSTVEKADNIIVIDRGQVAERGTHSQLMATGGLYCKLVQRQ 516
Cdd:cd03253  159 LLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
type_I_sec_HlyB TIGR01846
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ...
 19-517 2.50e-104

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: 329.01  E-value: 2.50e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   19 GVRGGVFTLTMARLNVRLRSRLFRTLMTQEIAFFDENHTGDILSRLSaDTTQVSDLISQNVNVFLRSVIKGTGFIIFMFR 98
Cdd:TIGR01846 197 GLRTYLFAHLTSRIDVELGARLYRHLLGLPLGYFESRRVGDTVARVR-ELEQIRNFLTGSALTVVLDLLFVVVFLAVMFF 275

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   99 MSWKLTLVTMMGFPFIALVSKLYGEYYKKLTKEVQTVLAEANKVAEETISGMRTVRSFANESREANSYYAKLLVmfQLNK 178
Cdd:TIGR01846 276 YSPTLTGVVIGSLVCYALLSVFVGPILRKRVEDKFERSAAATSFLVESVTGIETIKATATEPQFQNRWDRQLAA--YVAA 353

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  179 KQALAYACyMWSSCISELALEV---AVLYYGGHLVLTDQLSSGGLISFFIYMLELGECFESIASVYSGLMQGVGAAEKVF 255
Cdd:TIGR01846 354 SFRVTNLG-NIAGQAIELIQKLtfaILLWFGAHLVIGGALSPGQLVAFNMLAGRVTQPVLRLAQLWQDFQQTGIALERLG 432

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  256 EYLDRKPKHPADGTEAPNSCTGLVEFKDVTFAY-PTRPEtdVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQ 334
Cdd:TIGR01846 433 DILNSPTEPRSAGLAALPELRGAITFENIRFRYaPDSPE--VLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQ 510

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  335 GGQVLLDGKPVNEFQHDYLHSKIALVGQEPVLFARTIKENISYGLSDVSMEMVVQAATKANAHDFITTLPKGYDTSVGEK 414
Cdd:TIGR01846 511 HGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCNPGAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEK 590

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  415 GLQLSGGQKQRVAIARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQEHTVLVIAHRLSTVEKADNIIVIDRGQVA 494
Cdd:TIGR01846 591 GANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIA 670

                         490       500
                  ....*....|....*....|...
gi 961964003  495 ERGTHSQLMATGGLYCKLVQRQV 517
Cdd:TIGR01846 671 ESGRHEELLALQGLYARLWQQQS 693
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
 277-507 1.37e-97

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: 295.67  E-value: 1.37e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 277 GLVEFKDVTFAYptRPETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHDYLHSK 356
Cdd:cd03254    1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 357 IALVGQEPVLFARTIKENISYGLSDVSMEMVVQAATKANAHDFITTLPKGYDTSVGEKGLQLSGGQKQRVAIARALIRQP 436
Cdd:cd03254   79 IGVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDP 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 961964003 437 RVLILDEATSALDAESEHIVQQALNSIMQEHTVLVIAHRLSTVEKADNIIVIDRGQVAERGTHSQLMATGG 507
Cdd:cd03254  159 KILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
35-533 1.12e-94

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


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 300.87  E-value: 1.12e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  35 RLRSRLFRTLMTQEIAFFDENHTGDILSRLSADTTQVSDLISQNVNVFLRSVIKGTGFIIFMFRMSWKLTLVTMMGFPFI 114
Cdd:PRK10790  99 QLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWRMALVAIMIFPAV 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 115 ALVSKLYGEYYKKLTKEVQTVLAEANKVAEETISGMRTVRSFANESR------EAN-SYYakllvmfqLNKKQALAYACY 187
Cdd:PRK10790 179 LVVMVIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQARfgermgEASrSHY--------MARMQTLRLDGF 250

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 188 MWS---SCISELALEVAVLYYGghlvltdqLSSGGLI------SFFIYMLELGECFESIASVYSGLMQGVGAAEKVFEYL 258
Cdd:PRK10790 251 LLRpllSLFSALILCGLLMLFG--------FSASGTIevgvlyAFISYLGRLNEPLIELTTQQSMLQQAVVAGERVFELM 322

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 259 DRKPKHPADGTEAPNSctGLVEFKDVTFAYptRPETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQV 338
Cdd:PRK10790 323 DGPRQQYGNDDRPLQS--GRIDIDNVSFAY--RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEI 398

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 339 LLDGKPVNEFQHDYLHSKIALVGQEPVLFARTIKENISYGlSDVSMEMVVQAATKANAHDFITTLPKGYDTSVGEKGLQL 418
Cdd:PRK10790 399 RLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLG-RDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNL 477

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 419 SGGQKQRVAIARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQEHTVLVIAHRLSTVEKADNIIVIDRGQVAERGT 498
Cdd:PRK10790 478 SVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGT 557

                        490       500       510
                 ....*....|....*....|....*....|....*
gi 961964003 499 HSQLMATGGLYCKLVQRQVLGIETGAEVLNPSETV 533
Cdd:PRK10790 558 HQQLLAAQGRYWQMYQLQLAGEELAASVREEESLS 592
NHLM_micro_ABC1 TIGR03796
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ...
 6-514 1.34e-92

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: 298.40  E-value: 1.34e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003    6 PFTLFFLLSSMAIGV----RGGVFTLTMARLNVRLRSRLFRTLMTQEIAFFDENHTGDILSRLSADTtQVSDLISQNVNV 81
Cdd:TIGR03796 195 PLLLGMGLTALLQGVltwlQLYYLRRLEIKLAVGMSARFLWHILRLPVRFFAQRHAGDIASRVQLND-QVAEFLSGQLAT 273

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   82 FLRSVIKGTGFIIFMFRMSWKLTLVtmmGFPFIALVSKLYGEYYKKLTKEVQTVLAEANKVAEETISGMR---TVRSFAN 158
Cdd:TIGR03796 274 TALDAVMLVFYALLMLLYDPVLTLI---GIAFAAINVLALQLVSRRRVDANRRLQQDAGKLTGVAISGLQsieTLKASGL 350

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  159 ES---REANSYYAKLLVMFQ-LNKKQALAYACymwSSCISELAlEVAVLYYGGHLVLTDQLSSGGLISFFIYMLELGECF 234
Cdd:TIGR03796 351 ESdffSRWAGYQAKLLNAQQeLGVLTQILGVL---PTLLTSLN-SALILVVGGLRVMEGQLTIGMLVAFQSLMSSFLEPV 426

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  235 ESIASVYSGLMQ---GVGAAEKVFEY----LDRKPKHPADGTEAPNSCTGLVEFKDVTFAYpTRPETDVLKGVSFTLRPG 307
Cdd:TIGR03796 427 NNLVGFGGTLQElegDLNRLDDVLRNpvdpLLEEPEGSAATSEPPRRLSGYVELRNITFGY-SPLEPPLIENFSLTLQPG 505

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  308 EVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHDYLHSKIALVGQEPVLFARTIKENISYGLSDVSMEMV 387
Cdd:TIGR03796 506 QRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLWDPTIPDADL 585

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  388 VQAATKANAHDFITTLPKGYDTSVGEKGLQLSGGQKQRVAIARALIRQPRVLILDEATSALDAESEHIVQQALNSimQEH 467
Cdd:TIGR03796 586 VRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNLRR--RGC 663

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*..
gi 961964003  468 TVLVIAHRLSTVEKADNIIVIDRGQVAERGTHSQLMATGGLYCKLVQ 514
Cdd:TIGR03796 664 TCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELWAVGGAYARLIR 710
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
 279-516 2.89e-90

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: 277.45  E-value: 2.89e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 279 VEFKDVTFAYptRP-ETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHDYLHSKI 357
Cdd:cd03252    1 ITFEHVRFRY--KPdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 358 ALVGQEPVLFARTIKENISYGLSDVSMEMVVQAATKANAHDFITTLPKGYDTSVGEKGLQLSGGQKQRVAIARALIRQPR 437
Cdd:cd03252   79 GVVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPR 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 961964003 438 VLILDEATSALDAESEHIVQQALNSIMQEHTVLVIAHRLSTVEKADNIIVIDRGQVAERGTHSQLMATGGLYCKLVQRQ 516
Cdd:cd03252  159 ILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
97-522 1.44e-88

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 284.55  E-value: 1.44e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  97 FRMSWKLTLVTMMgfpfIALVSKLYGEYYKKLTKEVQT-VLAEANKVAE---ETISGMRTVRSFAN---ESREANSYYAK 169
Cdd:PRK13657 152 LFMNWRLSLVLVV----LGIVYTLITTLVMRKTKDGQAaVEEHYHDLFAhvsDAIGNVSVVQSYNRieaETQALRDIADN 227

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 170 LLvmfqlnKKQ-------ALAYACYMWSSCISELAlevaVLYYGGHLVLTDQLSSGGLISF--FIYMLeLGEcFESIASV 240
Cdd:PRK13657 228 LL------AAQmpvlswwALASVLNRAASTITMLA----ILVLGAALVQKGQLRVGEVVAFvgFATLL-IGR-LDQVVAF 295

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 241 YSGLMQGVGAAEKVFEYLDRKP--KHPADGTEAPNsCTGLVEFKDVTFAYPTRPETdvLKGVSFTLRPGEVTALVGPSGS 318
Cdd:PRK13657 296 INQVFMAAPKLEEFFEVEDAVPdvRDPPGAIDLGR-VKGAVEFDDVSFSYDNSRQG--VEDVSFEAKPGQTVAIVGPTGA 372

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 319 GKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHDYLHSKIALVGQEPVLFARTIKENISYGLSDVSMEMVVQAATKANAHD 398
Cdd:PRK13657 373 GKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHD 452

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 399 FITTLPKGYDTSVGEKGLQLSGGQKQRVAIARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQEHTVLVIAHRLST 478
Cdd:PRK13657 453 FIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLST 532

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 961964003 479 VEKADNIIVIDRGQVAERGTHSQLMATGGLYCKLVQRQVLGIET 522
Cdd:PRK13657 533 VRNADRILVFDNGRVVESGSFDELVARGGRFAALLRAQGMLQED 576
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
 279-492 3.52e-87

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: 266.94  E-value: 3.52e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 279 VEFKDVTFAYPTRPETdVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHDYLHSKIA 358
Cdd:cd03228    1 IEFKNVSFSYPGRPKP-VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 359 LVGQEPVLFARTIKENIsyglsdvsmemvvqaatkanahdfittlpkgydtsvgekglqLSGGQKQRVAIARALIRQPRV 438
Cdd:cd03228   80 YVPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPI 117

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 961964003 439 LILDEATSALDAESEHIVQQALNSIMQEHTVLVIAHRLSTVEKADNIIVIDRGQ 492
Cdd:cd03228  118 LILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
31-509 1.06e-85

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


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 276.59  E-value: 1.06e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  31 RLNVRLRSRLFRTLMTQEIAFFDENHTGDILSRLSADTTQVSDLISQNVNVFLRSVIKGTGFIIFM-FRMSWKLTLVTMM 109
Cdd:PRK10789  66 QLAVELREDFYRQLSRQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVMGCAVLIVMsTQISWQLTLLALL 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 110 GFPFIALVSKLYGEYYKKLTKEVQTVLAEANKVAEETISGMRTVRSFANESREANSYYAKLLVMFQLNKKQALAYACYMW 189
Cdd:PRK10789 146 PMPVMAIMIKRYGDQLHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARIDARFDP 225

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 190 SSCIselALEVAVLYY---GGHLVLTDQLSSGGLISFFIY-------MLELGECFESIAsvysglmQGVGAAEKVFEYLD 259
Cdd:PRK10789 226 TIYI---AIGMANLLAiggGSWMVVNGSLTLGQLTSFVMYlglmiwpMLALAWMFNIVE-------RGSAAYSRIRAMLA 295

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 260 RKPKhPADGTEAPNSCTGLVEFKDVTFAYPTRpETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVL 339
Cdd:PRK10789 296 EAPV-VKDGSEPVPEGRGELDVNIRQFTYPQT-DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIR 373

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 340 LDGKPVNEFQHDYLHSKIALVGQEPVLFARTIKENISYGLSDVSMEMVVQAATKANAHDFITTLPKGYDTSVGEKGLQLS 419
Cdd:PRK10789 374 FHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLS 453

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 420 GGQKQRVAIARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQEHTVLVIAHRLSTVEKADNIIVIDRGQVAERGTH 499
Cdd:PRK10789 454 GGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNH 533

                        490
                 ....*....|
gi 961964003 500 SQLMATGGLY 509
Cdd:PRK10789 534 DQLAQQSGWY 543
ABC_6TM_TAP_ABCB8_10_like cd18557
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ...
 7-254 3.72e-83

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: 260.96  E-value: 3.72e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   7 FTLFFLLSSMAIGVRGGVFTLTMARLNVRLRSRLFRTLMTQEIAFFDENHTGDILSRLSADTTQVSDLISQNVNVFLRSV 86
Cdd:cd18557   42 LLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNI 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  87 IKGTGFIIFMFRMSWKLTLVTMMGFPFIALVSKLYGEYYKKLTKEVQTVLAEANKVAEETISGMRTVRSFANESREANSY 166
Cdd:cd18557  122 LQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRY 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 167 YAKLLVMFQLNKKQALAYACYMWSSCISELALEVAVLYYGGHLVLTDQLSSGGLISFFIYMLELGECFESIASVYSGLMQ 246
Cdd:cd18557  202 SEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWYGGYLVLSGQLTVGELTSFILYTIMVASSVGGLSSLLADIMK 281


                 ....*...
gi 961964003 247 GVGAAEKV 254
Cdd:cd18557  282 ALGASERV 289
ABC_6TM_ABCB10_like cd18573
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ...
 10-254 1.28e-79

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: 252.05  E-value: 1.28e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  10 FFLLSSMAIGVRGGVFTLTMARLNVRLRSRLFRTLMTQEIAFFDENHTGDILSRLSADTTQVSDLISQNVNVFLRSVIKG 89
Cdd:cd18573   50 VFVVGAAANFGRVYLLRIAGERIVARLRKRLFKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSG 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  90 TGFIIFMFRMSWKLTLVTMMGFPFIALVSKLYGEYYKKLTKEVQTVLAEANKVAEETISGMRTVRSFANESREANSYYAK 169
Cdd:cd18573  130 VGGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKK 209

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 170 LLVMFQLNKKQALAYACYMWSSCISELALEVAVLYYGGHLVLTDQLSSGGLISFFIYMLELGECFESIASVYSGLMQGVG 249
Cdd:cd18573  210 VDEVFDLAKKEALASGLFFGSTGFSGNLSLLSVLYYGGSLVASGELTVGDLTSFLMYAVYVGSSVSGLSSFYSELMKGLG 289


                 ....*
gi 961964003 250 AAEKV 254
Cdd:cd18573  290 ASSRL 294
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
 30-488 4.79e-78

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: 255.29  E-value: 4.79e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   30 ARLNVRLRSRLFRTLMTQEIAFFDENHTGDILSRLsadTTQVSDL---ISQNVNVFLRSVIKGTGFIIFMFRMSWKLTLV 106
Cdd:TIGR02857  73 AAVKSQLRERLLEAVAALGPRWLQGRPSGELATLA---LEGVEALdgyFARYLPQLVLAVIVPLAILAAVFPQDWISGLI 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  107 TMMGFPFIALVSKLYGEYYKKLTKEVQTVLAEANKVAEETISGMRTVRSFANESREANSYyAKLLVMFQLNKKQALAYAc 186
Cdd:TIGR02857 150 LLLTAPLIPIFMILIGWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAAI-RRSSEEYRERTMRVLRIA- 227

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  187 yMWSSCISEL--ALEVAVL--YYGGHLVLTDQLSSGGlisFFIYMLeLGECFESI---ASVYSGLMQGVGAAEKVFEYLD 259
Cdd:TIGR02857 228 -FLSSAVLELfaTLSVALVavYIGFRLLAGDLDLATG---LFVLLL-APEFYLPLrqlGAQYHARADGVAAAEALFAVLD 302

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  260 RKPKHPADGTEAPNSCTGLVEFKDVTFAYPTRPEtdVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVL 339
Cdd:TIGR02857 303 AAPRPLAGKAPVTAAPASSLEFSGVSVAYPGRRP--ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIA 380

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  340 LDGKPVNEFQHDYLHSKIALVGQEPVLFARTIKENISYGLSDVSMEMVVQAATKANAHDFITTLPKGYDTSVGEKGLQLS 419
Cdd:TIGR02857 381 VNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLS 460

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 961964003  420 GGQKQRVAIARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQEHTVLVIAHRLSTVEKADNIIVI 488
Cdd:TIGR02857 461 GGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
chvA TIGR01192
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ...
 97-529 1.15e-75

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: 250.58  E-value: 1.15e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   97 FRMSWKLTLVTMMgfpfIALVSKLYGEYYKKLTKEVQTVLAEAN----KVAEETISGMRTVRSF---ANESREANSYYAK 169
Cdd:TIGR01192 152 FAMDWRLSIVLMV----LGILYILIAKLVMQRTKNGQAAVEHHYhnvfKHVSDSISNVSVVHSYnriEAETSALKQFTNN 227

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  170 LL-VMFQLNKKQALAYACYMWSSCISElaleVAVLYYGGHLVLTDQLSSGGLISFFIYMLELGECFESIASVYSGLMQGV 248
Cdd:TIGR01192 228 LLsAQYPVLDWWALASGLNRMASTISM----MCILVIGTVLVIKGELSVGEVIAFIGFANLLIGRLDQMSGFITQIFEAR 303

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  249 GAAEKVFEYLD--RKPKHPADGTEAPNsCTGLVEFKDVTFAYPTRPETdvLKGVSFTLRPGEVTALVGPSGSGKSSCVSL 326
Cdd:TIGR01192 304 AKLEDFFDLEDsvFQREEPADAPELPN-VKGAVEFRHITFEFANSSQG--VFDVSFEAKAGQTVAIVGPTGAGKTTLINL 380

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  327 LENFYLPQGGQVLLDGKPVNEFQHDYLHSKIALVGQEPVLFARTIKENISYGLSDVSMEMVVQAATKANAHDFITTLPKG 406
Cdd:TIGR01192 381 LQRVYDPTVGQILIDGIDINTVTRESLRKSIATVFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAHDFILKRSNG 460

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  407 YDTSVGEKGLQLSGGQKQRVAIARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQEHTVLVIAHRLSTVEKADNII 486
Cdd:TIGR01192 461 YDTLVGERGNRLSGGERQRLAIARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVL 540

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 961964003  487 VIDRGQVAERGTHSQLMATGGLYCKLVQRQvlGIETGAEVLNP 529
Cdd:TIGR01192 541 FLDQGRLIEKGSFQELIQKDGRFYKLLRRS--GLLTNQPATKP 581
ABC_6TM_TAP1 cd18589
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ...
 6-254 3.28e-75

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: 240.45  E-value: 3.28e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   6 PFTLFFLLSSMAIGVRGGVFTLTMARLNVRLRSRLFRTLMTQEIAFFDENHTGDILSRLSADTTQVSDLISQNVNVFLRS 85
Cdd:cd18589   41 VMSLLTIASAVSEFVCDLIYNITMSRIHSRLQGLVFAAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSENLSLLMWY 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  86 VIKGTGFIIFMFRMSWKLTLVTMMGFPFIALVSKLYGEYYKKLTKEVQTVLAEANKVAEETISGMRTVRSFANESREANS 165
Cdd:cd18589  121 LARGLFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEEGEAQR 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 166 YYAKLLVMFQLNKKQALAYACYMWSSCISELALEVAVLYYGGHLVLTDQLSSGGLISFFIYMLELGECFESIASVYSGLM 245
Cdd:cd18589  201 YRQRLQKTYRLNKKEAAAYAVSMWTSSFSGLALKVGILYYGGQLVTAGTVSSGDLVTFVLYELQFTSAVEVLLSYYPSVM 280


                 ....*....
gi 961964003 246 QGVGAAEKV 254
Cdd:cd18589  281 KAVGSSEKI 289
ABC_6TM_TAP2 cd18590
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ...
 9-254 9.90e-74

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: 236.47  E-value: 9.90e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   9 LFFLLSSMAIGVRGGVFTLTMARLNVRLRSRLFRTLMTQEIAFFDENHTGDILSRLSADTTQVSDLISQNVNVFLRSVIK 88
Cdd:cd18590   44 LFSLGSSLSAGLRGGLFMCTLSRLNLRLRHQLFSSLVQQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVK 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  89 GTGFIIFMFRMSWKLTLVTMMGFPFIALVSKLYGEYYKKLTKEVQTVLAEANKVAEETISGMRTVRSFANESREANSYYA 168
Cdd:cd18590  124 TLGMLGFMLSLSWQLTLLTLIEMPLTAIAQKVYNTYHQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSE 203

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 169 KLLVMFQLNKKQALAYACYMWSSCISELALEVAVLYYGGHLVLTDQLSSGGLISFFIYMLELGECFESIASVYSGLMQGV 248
Cdd:cd18590  204 ALERTYNLKDRRDTVRAVYLLVRRVLQLGVQVLMLYCGRQLIQSGHLTTGSLVSFILYQKNLGSYVRTLVYIYGDMLSNV 283


                 ....*.
gi 961964003 249 GAAEKV 254
Cdd:cd18590  284 GAAAKV 289
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
 246-517 1.87e-73

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 244.75  E-value: 1.87e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 246 QGVGAAEKVFEYLDRKPKHPADGTEAPNSCTGL-VEFKDVTFaypTRPETDVLKG-VSFTLRPGEVTALVGPSGSGKSSC 323
Cdd:PRK11174 316 QAVGAAESLVTFLETPLAHPQQGEKELASNDPVtIEAEDLEI---LSPDGKTLAGpLNFTLPAGQRIALVGPSGAGKTSL 392

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 324 VSLLENFyLPQGGQVLLDGKPVNEFQHDYLHSKIALVGQEPVLFARTIKENISYGLSDVSMEMVVQAATKANAHDFITTL 403
Cdd:PRK11174 393 LNALLGF-LPYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLL 471

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 404 PKGYDTSVGEKGLQLSGGQKQRVAIARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQEHTVLVIAHRLSTVEKAD 483
Cdd:PRK11174 472 PQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWD 551

                        250       260       270
                 ....*....|....*....|....*....|....
gi 961964003 484 NIIVIDRGQVAERGTHSQLMATGGLYCKLVQRQV 517
Cdd:PRK11174 552 QIWVMQDGQIVQQGDYAELSQAGGLFATLLAHRQ 585
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
 277-493 1.27e-72

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: 230.94  E-value: 1.27e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 277 GLVEFKDVTFAYPTRpETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHDYLHSK 356
Cdd:cd03245    1 GRIEFRNVSFSYPNQ-EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 357 IALVGQEPVLFARTIKENISYGLSDVSMEMVVQAATKANAHDFITTLPKGYDTSVGEKGLQLSGGQKQRVAIARALIRQP 436
Cdd:cd03245   80 IGYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDP 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 961964003 437 RVLILDEATSALDAESEHIVQQALNSIMQEHTVLVIAHRLSTVEKADNIIVIDRGQV 493
Cdd:cd03245  160 PILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
 49-513 2.85e-72

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: 244.65  E-value: 2.85e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   49 IAFFDENHTGDILSRLSADTTQVSDLISQNVNVFLR-SVIKGTGFiiFMFRMSWKLTLVTMMGFPFIALVSKLYGEYYKK 127
Cdd:TIGR01193 244 MSFFSTRRTGEIVSRFTDASSIIDALASTILSLFLDmWILVIVGL--FLVRQNMLLFLLSLLSIPVYAVIIILFKRTFNK 321

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  128 LTKEVQTVLAEANKVAEETISGMRTVRSFANESREansyYAKLLVMFQ--LNKKQALAYACY--MWSSCISELALEVAVL 203
Cdd:TIGR01193 322 LNHDAMQANAVLNSSIIEDLNGIETIKSLTSEAER----YSKIDSEFGdyLNKSFKYQKADQgqQAIKAVTKLILNVVIL 397

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  204 YYGGHLVLTDQLSSGGLISFFIYMLELGECFESIASVYSGLMQGVGAAEKVFE-YL---DRKPKHPADGTEAPNsctGLV 279
Cdd:TIGR01193 398 WTGAYLVMRGKLTLGQLITFNALLSYFLTPLENIINLQPKLQAARVANNRLNEvYLvdsEFINKKKRTELNNLN---GDI 474

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  280 EFKDVTFAYPTRPEtdVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHDYLHSKIAL 359
Cdd:TIGR01193 475 VINDVSYSYGYGSN--ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINY 552

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  360 VGQEPVLFARTIKENISYGLSD-VSMEMVVQAATKANAHDFITTLPKGYDTSVGEKGLQLSGGQKQRVAIARALIRQPRV 438
Cdd:TIGR01193 553 LPQEPYIFSGSILENLLLGAKEnVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKV 632

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 961964003  439 LILDEATSALDAESEH-IVQQALNsiMQEHTVLVIAHRLSTVEKADNIIVIDRGQVAERGTHSQLMATGGLYCKLV 513
Cdd:TIGR01193 633 LILDESTSNLDTITEKkIVNNLLN--LQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLI 706
ABC_6TM_AtABCB27_like cd18780
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ...
 11-254 1.17e-71

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: 231.37  E-value: 1.17e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  11 FLLSSMAIGVRGGVFTLTMARLNVRLRSRLFRTLMTQEIAFFDENHTGDILSRLSADTTQVSDLISQNVNVFLRSVIKGT 90
Cdd:cd18780   52 VLIGSIATFLRSWLFTLAGERVVARLRKRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQII 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  91 GFIIFMFRMSWKLTLVTMMGFPFIALVSKLYGEYYKKLTKEVQTVLAEANKVAEETISGMRTVRSFANESREANSYYAKL 170
Cdd:cd18780  132 GGLVFMFTTSWKLTLVMLSVVPPLSIGAVIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKI 211

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 171 LVMFQLNKKQALAYACYM-WSSCISELALeVAVLYYGGHLVLTDQLSSGGLISFFIYMLELGECFESIASVYSGLMQGVG 249
Cdd:cd18780  212 NESYLLGKKLARASGGFNgFMGAAAQLAI-VLVLWYGGRLVIDGELTTGLLTSFLLYTLTVAMSFAFLSSLYGDFMQAVG 290


                 ....*
gi 961964003 250 AAEKV 254
Cdd:cd18780  291 ASVRV 295
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
 11-504 9.47e-70

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: 234.26  E-value: 9.47e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  11 FLLSSMAI--GVRGGVFTLTMARLNVRLRSRLFRtlmtqeiAFFDENhtgdiLSRLSADTTQV-SDLISqnvnvfLRSVI 87
Cdd:COG4618   68 GLYAVMGLldAVRSRILVRVGARLDRRLGPRVFD-------AAFRAA-----LRGGGGAAAQAlRDLDT------LRQFL 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  88 KGTG------------FIIFMFRMSWKLTLVTMMGFPFIALVSkLYGEYY-KKLTKEVQTVLAEANKVAE------ETIS 148
Cdd:COG4618  130 TGPGlfalfdlpwapiFLAVLFLFHPLLGLLALVGALVLVALA-LLNERLtRKPLKEANEAAIRANAFAEaalrnaEVIE 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 149 GMRTVRSFANESREANSYYAKLlvmfqlnkkQALAYAcymWSSCISE------LALEVAVLYYGGHLVLTDQLSSGGLI- 221
Cdd:COG4618  209 AMGMLPALRRRWQRANARALAL---------QARASD---RAGGFSAlskflrLLLQSAVLGLGAYLVIQGEITPGAMIa 276

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 222 SFFIYMLELGEcFESIASVYSGLMQGVGAAEKVFEYLDRKPKHPaDGTEAPNScTGLVEFKDVTFAYP--TRPetdVLKG 299
Cdd:COG4618  277 ASILMGRALAP-IEQAIGGWKQFVSARQAYRRLNELLAAVPAEP-ERMPLPRP-KGRLSVENLTVVPPgsKRP---ILRG 350

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 300 VSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHDYLHSKIALVGQEPVLFARTIKENISyGL 379
Cdd:COG4618  351 VSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIA-RF 429

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 380 SDVSMEMVVQAATKANAHDFITTLPKGYDTSVGEKGLQLSGGQKQRVAIARALIRQPRVLILDEATSALDAESEHIVQQA 459
Cdd:COG4618  430 GDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAA 509

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*.
gi 961964003 460 LNSIMQE-HTVLVIAHRLSTVEKADNIIVIDRGQVAERGTHSQLMA 504
Cdd:COG4618  510 IRALKARgATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLA 555
NHLM_micro_ABC2 TIGR03797
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ...
 13-516 1.12e-69

NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]


Pssm-ID: 274789 [Multi-domain]  Cd Length: 686  Bit Score: 237.16  E-value: 1.12e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   13 LSSMAIGVRGGVFTL----TMARLNVRLRSRL----FRTLMTQEIAFFDENHTGDILSRLSAdTTQVSDLISqnvNVFLR 84
Cdd:TIGR03797 180 LALLAAAVGAAAFQLaqslAVLRLETRMDASLqaavWDRLLRLPVSFFRQYSTGDLASRAMG-ISQIRRILS---GSTLT 255

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   85 SVIKGTgFIIF----MFRMSWKLTLVTMMGFPFIALVSKLYGeyYKKLTKEVQtVLAEANKVAEET---ISGMRTVRSFA 157
Cdd:TIGR03797 256 TLLSGI-FALLnlglMFYYSWKLALVAVALALVAIAVTLVLG--LLQVRKERR-LLELSGKISGLTvqlINGISKLRVAG 331

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  158 NESReANSYYAKLLvmfqlNKKQALAYACYMWSSCISEL-----ALEVAVLYY-GGHLVLTDQLSSGGLISFFIYMLELG 231
Cdd:TIGR03797 332 AENR-AFARWAKLF-----SRQRKLELSAQRIENLLTVFnavlpVLTSAALFAaAISLLGGAGLSLGSFLAFNTAFGSFS 405

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  232 ECFESIASVYSGLMQGVGAAEKVFEYLDRKPKHPADGTeAPNSCTGLVEFKDVTFAYptRPETD-VLKGVSFTLRPGEVT 310
Cdd:TIGR03797 406 GAVTQLSNTLISILAVIPLWERAKPILEALPEVDEAKT-DPGKLSGAIEVDRVTFRY--RPDGPlILDDVSLQIEPGEFV 482

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  311 ALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHDYLHSKIALVGQEPVLFARTIKENISyGLSDVSMEMVVQA 390
Cdd:TIGR03797 483 AIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIA-GGAPLTLDEAWEA 561

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  391 ATKANAHDFITTLPKGYDTSVGEKGLQLSGGQKQRVAIARALIRQPRVLILDEATSALDAESEHIVQQALNSImqEHTVL 470
Cdd:TIGR03797 562 ARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERL--KVTRI 639

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*.
gi 961964003  471 VIAHRLSTVEKADNIIVIDRGQVAERGTHSQLMATGGLYCKLVQRQ 516
Cdd:TIGR03797 640 VIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGLFAQLARRQ 685
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
 35-476 9.30e-67

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: 225.70  E-value: 9.30e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   35 RLRSRLFRTLMTQEIAFFDENHTGDILSRLSADTTQVSDLISQNVNVFLRSVIKGTGFIIFMFRMSWK--LTLVTMM--- 109
Cdd:TIGR02868  87 ALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAAIAVLSVPaaLILAAGLlla 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  110 GF--PFIAL---------VSKLYGEYYKKLTkevqTVLAEAnkvAEETISGmrTVRSFANESREANSYYAKLLvmfqlnK 178
Cdd:TIGR02868 167 GFvaPLVSLraaraaeqaLARLRGELAAQLT----DALDGA---AELVASG--ALPAALAQVEEADRELTRAE------R 231

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  179 KQALAYAcymWSSCISELALEVAVLyyGGHLVLTDQLSSGGL----ISFFIYM-LELGECFESIASVYSGLMQGVGAAEK 253
Cdd:TIGR02868 232 RAAAATA---LGAALTLLAAGLAVL--GALWAGGPAVADGRLapvtLAVLVLLpLAAFEAFAALPAAAQQLTRVRAAAER 306

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  254 VFEYLDRKPK-----HPADGTEAPNSCTglVEFKDVTFAYPTRPEtdVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLE 328
Cdd:TIGR02868 307 IVEVLDAAGPvaegsAPAAGAVGLGKPT--LELRDLSAGYPGAPP--VLDGVSLDLPPGERVAILGPSGSGKSTLLATLA 382

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  329 NFYLPQGGQVLLDGKPVNEFQHDYLHSKIALVGQEPVLFARTIKENISYGLSDVSMEMVVQAATKANAHDFITTLPKGYD 408
Cdd:TIGR02868 383 GLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLD 462

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 961964003  409 TSVGEKGLQLSGGQKQRVAIARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQEHTVLVIAHRL 476
Cdd:TIGR02868 463 TVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
 277-498 7.13e-65

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: 210.81  E-value: 7.13e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 277 GLVEFKDVTFAYptRPETD-VLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHDYLHS 355
Cdd:cd03244    1 GDIEFKNVSLRY--RPNLPpVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 356 KIALVGQEPVLFARTIKENI-SYGL-SDvsmEMVVQAATKANAHDFITTLPKGYDTSVGEKGLQLSGGQKQRVAIARALI 433
Cdd:cd03244   79 RISIIPQDPVLFSGTIRSNLdPFGEySD---EELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALL 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 961964003 434 RQPRVLILDEATSALDAESEHIVQQALNSIMQEHTVLVIAHRLSTVEKADNIIVIDRGQVAERGT 498
Cdd:cd03244  156 RKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
 200-516 9.36e-63

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 215.84  E-value: 9.36e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 200 VAVLYYGGHLVlTDQLSSGGLISFFIYMLElgECFESIASV---YSGLMQGVGAAEKVFEYLDRKP--KHPADGTEAPNS 274
Cdd:PRK11160 260 VLMLWLAAGGV-GGNAQPGALIALFVFAAL--AAFEALMPVagaFQHLGQVIASARRINEITEQKPevTFPTTSTAAADQ 336

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 275 ctGLVEFKDVTFAYPTRPETdVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHDYLH 354
Cdd:PRK11160 337 --VSLTLNNVSFTYPDQPQP-VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALR 413

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 355 SKIALVGQEPVLFARTIKENISYGLSDVSMEMVVQAATKANAHDFITTlPKGYDTSVGEKGLQLSGGQKQRVAIARALIR 434
Cdd:PRK11160 414 QAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIARALLH 492

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 435 QPRVLILDEATSALDAESEHIVQQALNSIMQEHTVLVIAHRLSTVEKADNIIVIDRGQVAERGTHSQLMATGGLYCKLVQ 514
Cdd:PRK11160 493 DAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQLKQ 572


                 ..
gi 961964003 515 RQ 516
Cdd:PRK11160 573 RL 574
ABC_6TM_bac_exporter_ABCB8_10_like cd18576
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ...
 11-254 2.58e-61

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: 203.87  E-value: 2.58e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  11 FLLSSMAIGVRGGVFTLTMARLNVRLRSRLFRTLMTQEIAFFDENHTGDILSRLSADTTQVSDLISQNVNVFLRSVIKGT 90
Cdd:cd18576   46 FLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLI 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  91 GFIIFMFRMSWKLTLVTMMGFPFIALVSKLYGEYYKKLTKEVQTVLAEANKVAEETISGMRTVRSFANESREANSYYAKL 170
Cdd:cd18576  126 GGVVLLFFISWKLTLLMLATVPVVVLVAVLFGRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKAL 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 171 LVMFQLNKKQALAYACYMWSSCISELALEVAVLYYGGHLVLTDQLSSGGLISFFIYMLELGECFESIASVYSGLMQGVGA 250
Cdd:cd18576  206 ERVVKLALKRARIRALFSSFIIFLLFGAIVAVLWYGGRLVLAGELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKALGA 285


                 ....
gi 961964003 251 AEKV 254
Cdd:cd18576  286 SERV 289
type_I_sec_PrtD TIGR01842
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ...
 9-504 1.05e-59

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: 207.20  E-value: 1.05e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003    9 LFFLLSSMAIgVRGGVFTLTMARLNVRLRSRLFRtlmtqeiAFFDENhtgdiLSRLSADTTQ-VSDLISqnvnvfLRSVI 87
Cdd:TIGR01842  55 LYLFLGLLDA-LRSFVLVRIGEKLDGALNQPIFA-------ASFSAT-----LRRGSGDGLQaLRDLDQ------LRQFL 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   88 KGTGFIIFmFRMSWK--LTLVTMMGFPFIALVS----------KLYGEYY-KKLTKEVQTVLAEANKVAE------ETIS 148
Cdd:TIGR01842 116 TGPGLFAF-FDAPWMpiYLLVCFLLHPWIGILAlggavvlvglALLNNRAtKKPLKEATEASIRANNLADsalrnaEVIE 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  149 GMRTVRSFanESREANSYYAKLlvmfqlnKKQALA-YACYMWS--SCISELALEVAVLYYGGHLVLTDQLSSGGLISFFI 225
Cdd:TIGR01842 195 AMGMMGNL--TKRWGRFHSKYL-------SAQSAAsDRAGMLSnlSKYFRIVLQSLVLGLGAYLAIDGEITPGMMIAGSI 265

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  226 YMLELGECFESIASVYSGLMQGVGAAEKVFEYLDRKPKhPADGTEAPNScTGLVEFKDVTFAyPTRPETDVLKGVSFTLR 305
Cdd:TIGR01842 266 LVGRALAPIDGAIGGWKQFSGARQAYKRLNELLANYPS-RDPAMPLPEP-EGHLSVENVTIV-PPGGKKPTLRGISFSLQ 342

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  306 PGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHDYLHSKIALVGQEPVLFARTIKENISYGLSDVSME 385
Cdd:TIGR01842 343 AGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENIARFGENADPE 422

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  386 MVVQAATKANAHDFITTLPKGYDTSVGEKGLQLSGGQKQRVAIARALIRQPRVLILDEATSALDAESEHIVQQALNSI-M 464
Cdd:TIGR01842 423 KIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALkA 502

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|
gi 961964003  465 QEHTVLVIAHRLSTVEKADNIIVIDRGQVAERGTHSQLMA 504
Cdd:TIGR01842 503 RGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLA 542
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
 36-506 1.18e-57

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 208.73  E-value: 1.18e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   36 LRSRLFRTLMTQEIAFFDENHTGDILSRLSADTTQVSDLISQNVNVFLRSVIKGTGFIIFMFRMSWKLTLVTMMGFPFIA 115
Cdd:PTZ00265  132 LKLEFLKSVFYQDGQFHDNNPGSKLTSDLDFYLEQVNAGIGTKFITIFTYASAFLGLYIWSLFKNARLTLCITCVFPLIY 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  116 LVSKLYGeyyKKLTKEVQTVLAEANK---VAEETISGMRTVRSFANESreansyyaKLLVMFQLNKKqalAYACYMWSSC 192
Cdd:PTZ00265  212 ICGVICN---KKVKINKKTSLLYNNNtmsIIEEALVGIRTVVSYCGEK--------TILKKFNLSEK---LYSKYILKAN 277

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  193 ISElALEVAVL------------YYGGHLVLTDQLSS----------------GGLISFFIYMLELGECFEsiasvysgL 244
Cdd:PTZ00265  278 FME-SLHIGMIngfilasyafgfWYGTRIIISDLSNQqpnndfhggsvisillGVLISMFMLTIILPNITE--------Y 348

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  245 MQGVGAAEKVFEYLDRKP--KHPADGTEAPNscTGLVEFKDVTFAYPTRPETDVLKGVSFTLRPGEVTALVGPSGSGKSS 322
Cdd:PTZ00265  349 MKSLEATNSLYEIINRKPlvENNDDGKKLKD--IKKIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKST 426

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  323 CVSLLENFYLPQGGQVLL-DGKPVNEFQHDYLHSKIALVGQEPVLFARTIKENISYGL---------------------- 379
Cdd:PTZ00265  427 ILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSLyslkdlealsnyynedgndsqe 506

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  380 ----------------SDVSMEM-------------------VVQAATKANAHDFITTLPKGYDTSVGEKGLQLSGGQKQ 424
Cdd:PTZ00265  507 nknkrnscrakcagdlNDMSNTTdsneliemrknyqtikdseVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQ 586

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  425 RVAIARALIRQPRVLILDEATSALDAESEHIVQQALNSIM--QEHTVLVIAHRLSTVEKADNIIVIDRgqvAERGTHSQL 502
Cdd:PTZ00265  587 RISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLSTIRYANTIFVLSN---RERGSTVDV 663


                  ....
gi 961964003  503 MATG 506
Cdd:PTZ00265  664 DIIG 667
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
 12-509 2.42e-54

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: 199.02  E-value: 2.42e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003    12 LLSSMAIGVrGGVFTltmARlnvRLRSRLFRTLMTQEIAFFDENHTGDILSRLSADTTQVSDLISQNVNVFLRSVIKGTG 91
Cdd:TIGR00957 1023 FGYSMAVSI-GGIQA---SR---VLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIG 1095

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003    92 FIIFMFRMSWKLTLVtmmgFPFIALVSKLYGEYYKKLTKEVQTVLAEANKVA----EETISGMRTVRSFaNESREansyy 167
Cdd:TIGR00957 1096 ALIVILLATPIAAVI----IPPLGLLYFFVQRFYVASSRQLKRLESVSRSPVyshfNETLLGVSVIRAF-EEQER----- 1165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   168 aklLVMFQLNKKQALAYACYmwSSCISELALEVAVLYYGGHLVLTDQLS--------SGGLISFFI-YMLELGECFESIA 238
Cdd:TIGR00957 1166 ---FIHQSDLKVDENQKAYY--PSIVANRWLAVRLECVGNCIVLFAALFavisrhslSAGLVGLSVsYSLQVTFYLNWLV 1240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   239 SVYSGLMQGVGAAEKVFEYLDRKPKHP--ADGTEAPNSC--TGLVEFKDVTFAYptRPETD-VLKGVSFTLRPGEVTALV 313
Cdd:TIGR00957 1241 RMSSEMETNIVAVERLKEYSETEKEAPwqIQETAPPSGWppRGRVEFRNYCLRY--REDLDlVLRHINVTIHGGEKVGIV 1318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   314 GPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHDYLHSKIALVGQEPVLFARTIKENISyGLSDVSMEMVVQAATK 393
Cdd:TIGR00957 1319 GRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLD-PFSQYSDEEVWWALEL 1397

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   394 ANAHDFITTLPKGYDTSVGEKGLQLSGGQKQRVAIARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQEHTVLVIA 473
Cdd:TIGR00957 1398 AHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIA 1477

                          490       500       510
                   ....*....|....*....|....*....|....*.
gi 961964003   474 HRLSTVEKADNIIVIDRGQVAERGTHSQLMATGGLY 509
Cdd:TIGR00957 1478 HRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIF 1513
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
 36-514 1.38e-53

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 196.79  E-value: 1.38e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   36 LRSRLFRTLMTQEIAFFDEN-HTGDILS-RLSADTTQVSDLISQNVNVFlrsvikgTGFIIfmfrmswkLTLVTM-MGFP 112
Cdd:PTZ00265  901 MKRRLFENILYQEISFFDQDkHAPGLLSaHINRDVHLLKTGLVNNIVIF-------THFIV--------LFLVSMvMSFY 965

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  113 FIALVSK-LYGEYY-------------------KKLTKEVQTVLAEANK---------VAEETISGMRTVRSFANESrea 163
Cdd:PTZ00265  966 FCPIVAAvLTGTYFifmrvfairarltankdveKKEINQPGTVFAYNSDdeifkdpsfLIQEAFYNMNTVIIYGLED--- 1042

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  164 nsYYAKLL--VMFQLNK--KQALAYACYMWS-SCISELALEVAVLYYGGHLVLTDQLSSGGLISFFIYMLELGECFESIA 238
Cdd:PTZ00265 1043 --YFCNLIekAIDYSNKgqKRKTLVNSMLWGfSQSAQLFINSFAYWFGSFLIRRGTILVDDFMKSLFTFLFTGSYAGKLM 1120

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  239 SVYSGLMQGVGAAEKVFEYLDRKPKHPA--DG---TEAPNSCTGLVEFKDVTFAYPTRPETDVLKGVSFTLRPGEVTALV 313
Cdd:PTZ00265 1121 SLKGDSENAKLSFEKYYPLIIRKSNIDVrdNGgirIKNKNDIKGKIEIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIV 1200

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  314 GPSGSGKSSCVSLLENFY----------------------LPQG--------------------------------GQVL 339
Cdd:PTZ00265 1201 GETGSGKSTVMSLLMRFYdlkndhhivfknehtndmtneqDYQGdeeqnvgmknvnefsltkeggsgedstvfknsGKIL 1280

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  340 LDGKPVNEFQHDYLHSKIALVGQEPVLFARTIKENISYGLSDVSMEMVVQAATKANAHDFITTLPKGYDTSVGEKGLQLS 419
Cdd:PTZ00265 1281 LDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLS 1360

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  420 GGQKQRVAIARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQ--EHTVLVIAHRLSTVEKADNIIVI---DRGQ-- 492
Cdd:PTZ00265 1361 GGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkaDKTIITIAHRIASIKRSDKIVVFnnpDRTGsf 1440

                         570       580
                  ....*....|....*....|...
gi 961964003  493 VAERGTHSQLM-ATGGLYCKLVQ 514
Cdd:PTZ00265 1441 VQAHGTHEELLsVQDGVYKKYVK 1463
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
 279-504 5.45e-53

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: 179.84  E-value: 5.45e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 279 VEFKDVTFAYPtrPETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHDYLHSKIA 358
Cdd:COG1122    1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 359 LVGQEPV--LFARTIKENISYG-----LSDVSMEMVVQAATKAnahdfittlpkgydtsVGEKGL------QLSGGQKQR 425
Cdd:COG1122   79 LVFQNPDdqLFAPTVEEDVAFGpenlgLPREEIRERVEEALEL----------------VGLEHLadrpphELSGGQKQR 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 426 VAIARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQE-HTVLVIAHRLSTVEK-ADNIIVIDRGQVAERGTHSQLM 503
Cdd:COG1122  143 VAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEgKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREVF 222


                 .
gi 961964003 504 A 504
Cdd:COG1122  223 S 223
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
280-493 2.33e-50

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 172.31  E-value: 2.33e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 280 EFKDVTFAYPTRPetdVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHDYLHSKIAL 359
Cdd:COG4619    2 ELEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAY 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 360 VGQEPVLFARTIKENISYGLS----DVSMEMVVQAATKANahdfittLPKGY-DTSVGEkglqLSGGQKQRVAIARALIR 434
Cdd:COG4619   79 VPQEPALWGGTVRDNLPFPFQlrerKFDRERALELLERLG-------LPPDIlDKPVER----LSGGERQRLALIRALLL 147

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 961964003 435 QPRVLILDEATSALDAESEHIVQQALNSIMQEH--TVLVIAH------RLstvekADNIIVIDRGQV 493
Cdd:COG4619  148 QPDVLLLDEPTSALDPENTRRVEELLREYLAEEgrAVLWVSHdpeqieRV-----ADRVLTLEAGRL 209
ABC_6TM_MsbA_like cd18552
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ...
 3-254 3.15e-50

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: 174.53  E-value: 3.15e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   3 VAPPFTLFFLLSSMAIG---VRG-----GVFTLTMARLNV--RLRSRLFRTLMTQEIAFFDENHTGDILSRLSADTTQVS 72
Cdd:cd18552   31 VEKDLEALLLVPLAIIGlflLRGlasylQTYLMAYVGQRVvrDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQ 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  73 DLISQNVNVFLRSVIKGTGFIIFMFRMSWKLTLVTMMGFPFIALVSKLYGEYYKKLTKEVQTVLAEANKVAEETISGMRT 152
Cdd:cd18552  111 NALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPIRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRV 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 153 VRSFANESREANSYYAKLLVMFQLNKKQALAYAcymWSSCISE----LALeVAVLYYGGHLVLTDQLSSGGLISFFIYML 228
Cdd:cd18552  191 VKAFGAEDYEIKRFRKANERLRRLSMKIARARA---LSSPLMEllgaIAI-ALVLWYGGYQVISGELTPGEFISFITALL 266

                        250       260
                 ....*....|....*....|....*.
gi 961964003 229 ELGECFESIASVYSGLMQGVGAAEKV 254
Cdd:cd18552  267 LLYQPIKRLSNVNANLQRGLAAAERI 292
ABC_6TM_exporters cd07346
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ...
 7-254 3.40e-50

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: 174.66  E-value: 3.40e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   7 FTLFFLLSSMAIGVRGGVFTLTMARLNVRLRSRLFRTLMTQEIAFFDENHTGDILSRLSADTTQVSDLISQNVNVFLRSV 86
Cdd:cd07346   45 LLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDV 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  87 IKGTGFIIFMFRMSWKLTLVTMMGFPFIALVSKLYGEYYKKLTKEVQTVLAEANKVAEETISGMRTVRSFANESREANSY 166
Cdd:cd07346  125 LTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERF 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 167 YAKLLVMFQLNKKQA-LAYACYMWSSCISELALeVAVLYYGGHLVLTDQLSSGGLISFFIYMLELGECFESIASVYSGLM 245
Cdd:cd07346  205 REANRDLRDANLRAArLSALFSPLIGLLTALGT-ALVLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQ 283


                 ....*....
gi 961964003 246 QGVGAAEKV 254
Cdd:cd07346  284 QALASLERI 292
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
 280-493 1.06e-49

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: 169.32  E-value: 1.06e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 280 EFKDVTFAYPTRpETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHDYLHSKIAL 359
Cdd:cd03246    2 EVENVSFRYPGA-EPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 360 VGQEPVLFARTIKENIsyglsdvsmemvvqaatkanahdfittlpkgydtsvgekglqLSGGQKQRVAIARALIRQPRVL 439
Cdd:cd03246   81 LPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRIL 118

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 961964003 440 ILDEATSALDAESEHIVQQALNSI-MQEHTVLVIAHRLSTVEKADNIIVIDRGQV 493
Cdd:cd03246  119 VLDEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
279-504 3.14e-49

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 170.24  E-value: 3.14e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 279 VEFKDVTFAYPTRPetdVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEfQHDYLHSKIA 358
Cdd:COG1131    1 IEVRGLTKRYGDKT---ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 359 LVGQEPVLFAR-TIKENISY--GLSDVSmemvvQAATKANAHDFITT--LPKGYDTSVGekglQLSGGQKQRVAIARALI 433
Cdd:COG1131   77 YVPQEPALYPDlTVRENLRFfaRLYGLP-----RKEARERIDELLELfgLTDAADRKVG----TLSGGMKQRLGLALALL 147

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 961964003 434 RQPRVLILDEATSALDAESEHIVQQALNSIMQE-HTVLVIAHRLSTVEK-ADNIIVIDRGQVAERGTHSQLMA 504
Cdd:COG1131  148 HDPELLILDEPTSGLDPEARRELWELLRELAAEgKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELKA 220
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
 237-504 5.51e-49

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: 177.40  E-value: 5.51e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 237 IASVYSGLMQGVGAAEKVFEYLDRKPKHPADGTEAPNSCTG------LVEFKDVTFAYPTRP--ETDVLKGVSFTLRPGE 308
Cdd:COG1123  213 VVVMDDGRIVEDGPPEEILAAPQALAAVPRLGAARGRAAPAaaaaepLLEVRNLSKRYPVRGkgGVRAVDDVSLTLRRGE 292

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 309 VTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHD---YLHSKIALVGQEPV--LFAR-TIKENISYGLsdv 382
Cdd:COG1123  293 TLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRslrELRRRVQMVFQDPYssLNPRmTVGDIIAEPL--- 369

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 383 smeMVVQAATKANAHDFITTLPK--GYDTSVGEK-GLQLSGGQKQRVAIARALIRQPRVLILDEATSALDAesehIVQ-Q 458
Cdd:COG1123  370 ---RLHGLLSRAERRERVAELLErvGLPPDLADRyPHELSGGQRQRVAIARALALEPKLLILDEPTSALDV----SVQaQ 442

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 961964003 459 ALNSIM---QEH--TVLVIAHRLSTVEK-ADNIIVIDRGQVAERGTHSQLMA 504
Cdd:COG1123  443 ILNLLRdlqRELglTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTEEVFA 494
ABC_membrane pfam00664
ABC transporter transmembrane region; This family represents a unit of six transmembrane ...
 7-228 6.17e-49

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


Pssm-ID: 459896 [Multi-domain]  Cd Length: 274  Bit Score: 170.52  E-value: 6.17e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003    7 FTLFFLLSSMAIGVRGGVFTLTMARLNVRLRSRLFRTLMTQEIAFFDENHTGDILSRLSADTTQVSDLISQNVNVFLRSV 86
Cdd:pfam00664  47 LLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSL 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   87 IKGTGFIIFMFRMSWKLTLVTMMGFPFIALVSKLYGEYYKKLTKEVQTVLAEANKVAEETISGMRTVRSFANESREANSY 166
Cdd:pfam00664 127 ATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKY 206

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 961964003  167 YAKLLVMFQLNKKQALAYA-CYMWSSCISELALeVAVLYYGGHLVLTDQLSSGGLISFFIYML 228
Cdd:pfam00664 207 DKALEEALKAGIKKAVANGlSFGITQFIGYLSY-ALALWFGAYLVISGELSVGDLVAFLSLFA 268
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
 278-495 1.02e-48

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


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 169.50  E-value: 1.02e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 278 LVEFKDVTFAYPTRP-ETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHDylhsk 356
Cdd:COG1116    7 ALELRGVSKRFPTGGgGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD----- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 357 IALVGQEPVLFA-RTIKENISYGLSDVSMEMVvQAATKANAH-------DFITTLPKgydtsvgekglQLSGGQKQRVAI 428
Cdd:COG1116   82 RGVVFQEPALLPwLTVLDNVALGLELRGVPKA-ERRERARELlelvglaGFEDAYPH-----------QLSGGMRQRVAI 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 961964003 429 ARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQEH--TVLVIAH------RLstvekADNIIVIDR--GQVAE 495
Cdd:COG1116  150 ARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETgkTVLFVTHdvdeavFL-----ADRVVVLSArpGRIVE 221
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
 280-492 1.20e-48

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: 167.64  E-value: 1.20e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 280 EFKDVTFAYPTRpETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHDYLHSKIAL 359
Cdd:cd03225    1 ELKNLSFSYPDG-ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 360 VGQEP--VLFARTIKENISYGL-----SDVSMEMVVQAATKAnahdfittlpkgydtsVGEKGL------QLSGGQKQRV 426
Cdd:cd03225   80 VFQNPddQFFGPTVEEEVAFGLenlglPEEEIEERVEEALEL----------------VGLEGLrdrspfTLSGGQKQRV 143

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 961964003 427 AIARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQE-HTVLVIAHRLSTV-EKADNIIVIDRGQ 492
Cdd:cd03225  144 AIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEgKTIIIVTHDLDLLlELADRVIVLEDGK 211
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
 279-496 2.72e-48

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


Pssm-ID: 213260 [Multi-domain]  Cd Length: 220  Bit Score: 167.26  E-value: 2.72e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 279 VEFKDVTFAYPT-RPETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEfqhdyLHSKI 357
Cdd:cd03293    1 LEVRNVSKTYGGgGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG-----PGPDR 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 358 ALVGQEPVLFA-RTIKENISYGLSdvsMEMVVQAATKANAHDFITTlpkgydtsVGEKGL------QLSGGQKQRVAIAR 430
Cdd:cd03293   76 GYVFQQDALLPwLTVLDNVALGLE---LQGVPKAEARERAEELLEL--------VGLSGFenayphQLSGGMRQRVALAR 144

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 961964003 431 ALIRQPRVLILDEATSALDAESEHIVQQALNSIMQEH--TVLVIAHRLS-TVEKADNIIVIDR--GQVAER 496
Cdd:cd03293  145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETgkTVLLVTHDIDeAVFLADRVVVLSArpGRIVAE 215
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
 278-497 1.18e-47

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: 165.76  E-value: 1.18e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 278 LVEFKDVTFAYPTRP-ETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPV---NEFQHDYL 353
Cdd:cd03257    1 LLEVKNLSVSFPTGGgSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLlklSRRLRKIR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 354 HSKIALVGQEPVL---FARTIKENISYGLSDVSMEMVVQAATKA---------NAHDFITTLPkgydtsvgekgLQLSGG 421
Cdd:cd03257   81 RKEIQMVFQDPMSslnPRMTIGEQIAEPLRIHGKLSKKEARKEAvllllvgvgLPEEVLNRYP-----------HELSGG 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 961964003 422 QKQRVAIARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQEH--TVLVIAHRLSTVEK-ADNIIVIDRGQVAERG 497
Cdd:cd03257  150 QRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELglTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
 279-502 4.99e-47

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: 163.89  E-value: 4.99e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 279 VEFKDVTFAYPTRpetDVLKGVSFTLRPGEVTALVGPSGSGKSS---CVSLLENFY--LPQGGQVLLDGKPVNEFQHD-- 351
Cdd:cd03260    1 IELRDLNVYYGDK---HALKDISLDIPKGEITALIGPSGCGKSTllrLLNRLNDLIpgAPDEGEVLLDGKDIYDLDVDvl 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 352 YLHSKIALVGQEPVLFARTIKENISYGL-------SDVSMEMVVQAATKANAHDfittlpKGYDTSvgeKGLQLSGGQKQ 424
Cdd:cd03260   78 ELRRRVGMVFQKPNPFPGSIYDNVAYGLrlhgiklKEELDERVEEALRKAALWD------EVKDRL---HALGLSGGQQQ 148

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 961964003 425 RVAIARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQEHTVLVIAHRLSTVEK-ADNIIVIDRGQVAERGTHSQL 502
Cdd:cd03260  149 RLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
 279-492 7.75e-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: 7.75e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 279 VEFKDVTFAYPTRPETD--VLKGVSFTLRPGEVTALVGPSGSGKSS-CVSLLENFYLpQGGQVlldgkpvnefqhdYLHS 355
Cdd:cd03250    1 ISVEDASFTWDSGEQETsfTLKDINLEVPKGELVAIVGPVGSGKSSlLSALLGELEK-LSGSV-------------SVPG 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 356 KIALVGQEPVLFARTIKENISYGlSDVSMEM---VVQAAtkANAHDfITTLPKGYDTSVGEKGLQLSGGQKQRVAIARAL 432
Cdd:cd03250   67 SIAYVSQEPWIQNGTIRENILFG-KPFDEERyekVIKAC--ALEPD-LEILPDGDLTEIGEKGINLSGGQKQRISLARAV 142

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 961964003 433 IRQPRVLILDEATSALDAE-SEHIVQQALNSIMQEH-TVLVIAHRLSTVEKADNIIVIDRGQ 492
Cdd:cd03250  143 YSDADIYLLDDPLSAVDAHvGRHIFENCILGLLLNNkTRILVTHQLQLLPHADQIVVLDNGR 204
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
 279-497 1.58e-46

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


Pssm-ID: 213214 [Multi-domain]  Cd Length: 178  Bit Score: 160.94  E-value: 1.58e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 279 VEFKDVTFAYPTRPETdVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQhDYLHSKIA 358
Cdd:cd03247    1 LSINNVSFSYPEQEQQ-VLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLIS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 359 LVGQEPVLFARTIKENIsyglsdvsmemvvqaatkanahdfittlpkgydtsvgekGLQLSGGQKQRVAIARALIRQPRV 438
Cdd:cd03247   79 VLNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPI 119

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 961964003 439 LILDEATSALDAESEHIVQQALNSIMQEHTVLVIAHRLSTVEKADNIIVIDRGQVAERG 497
Cdd:cd03247  120 VLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
ABC_6TM_Pgp_ABCB1_D1_like cd18577
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ...
 7-254 1.03e-45

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: 162.64  E-value: 1.03e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   7 FTLFFLLSSMAIGVRGGVFTLTMARLNVRLRSRLFRTLMTQEIAFFDENHTGDILSRLSADTTQVSDLISQNVNVFLRSV 86
Cdd:cd18577   53 FVYLGIGSFVLSYIQTACWTITGERQARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSL 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  87 IKG-TGFIIfMFRMSWKLTLVTMMGFPFIALVSKLYGEYYKKLTKEVQTVLAEANKVAEETISGMRTVRSFANESREANS 165
Cdd:cd18577  133 STFiAGFII-AFIYSWKLTLVLLATLPLIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKR 211

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 166 YYAKLLVMFQLNKKQALAYAC-----YMWSSCISELAlevavLYYGGHLVLTDQLSSGGLISFFIYMLELGECFESIASV 240
Cdd:cd18577  212 YSKALEKARKAGIKKGLVSGLglgllFFIIFAMYALA-----FWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIAPN 286

                        250
                 ....*....|....
gi 961964003 241 YSGLMQGVGAAEKV 254
Cdd:cd18577  287 LQAFAKARAAAAKI 300
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 297-446 1.87e-45

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: 157.04  E-value: 1.87e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  297 LKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHDYLHSKIALVGQEPVLFAR-TIKENI 375
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 961964003  376 SYGLsdvSMEMVVQAATKANAHDFITTLPKGY--DTSVGEKGLQLSGGQKQRVAIARALIRQPRVLILDEATS 446
Cdd:pfam00005  81 RLGL---LLKGLSKREKDARAEEALEKLGLGDlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
 278-504 3.08e-45

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: 159.64  E-value: 3.08e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 278 LVEFKDVTFAYPTRPetdVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVnEFQHDYLHSKI 357
Cdd:COG4555    1 MIEVENLSKKYGKVP---ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDV-RKEPREARRQI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 358 ALVGQEPVLFAR-TIKENISY-----GLSDVSMEMVVQAATKAnahdfiTTLPKGYDTSVGEkglqLSGGQKQRVAIARA 431
Cdd:COG4555   77 GVLPDERGLYDRlTVRENIRYfaelyGLFDEELKKRIEELIEL------LGLEEFLDRRVGE----LSTGMKKKVALARA 146

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 961964003 432 LIRQPRVLILDEATSALDAESEHIVQQALNSIMQE-HTVLVIAHRLSTVEK-ADNIIVIDRGQVAERGTHSQLMA 504
Cdd:COG4555  147 LVHDPKVLLLDEPTNGLDVMARRLLREILRALKKEgKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELRE 221
PLN03232 PLN03232
ABC transporter C family member; Provisional
 35-514 1.75e-44

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 169.77  E-value: 1.75e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   35 RLRSRLFRTLMTQEIAFFDENHTGDILSRLSADTTQVSDLISQNVNVFLRSVIKGTGFIIFMFRMSwKLTLVTMMgfPFI 114
Cdd:PLN03232  984 RLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFMNQLWQLLSTFALIGTVS-TISLWAIM--PLL 1060

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  115 ALVSKLYgEYYKKLTKEVQTV--LAEANKVAE--ETISGMRTVRSFANESREA--NSYYAKLLVMFQL---NKKQALAYA 185
Cdd:PLN03232 1061 ILFYAAY-LYYQSTSREVRRLdsVTRSPIYAQfgEALNGLSSIRAYKAYDRMAkiNGKSMDNNIRFTLantSSNRWLTIR 1139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  186 CYMWSSCISELALEVAVLYYG---GHLVLTDQLssGGLISffiYMLELGECFESIASVYSGLMQGVGAAEKVFEYLDRKP 262
Cdd:PLN03232 1140 LETLGGVMIWLTATFAVLRNGnaeNQAGFASTM--GLLLS---YTLNITTLLSGVLRQASKAENSLNSVERVGNYIDLPS 1214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  263 KHPA-DGTEAPNS---CTGLVEFKDVTFAYptRPE-TDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQ 337
Cdd:PLN03232 1215 EATAiIENNRPVSgwpSRGSIKFEDVHLRY--RPGlPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGR 1292

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  338 VLLDGKPVNEFQHDYLHSKIALVGQEPVLFARTIKENISyGLSDVSMEMVVQAATKANAHDFITTLPKGYDTSVGEKGLQ 417
Cdd:PLN03232 1293 IMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNID-PFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGEN 1371

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  418 LSGGQKQRVAIARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQEHTVLVIAHRLSTVEKADNIIVIDRGQVAERG 497
Cdd:PLN03232 1372 FSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYD 1451

                         490
                  ....*....|....*...
gi 961964003  498 THSQLMAT-GGLYCKLVQ 514
Cdd:PLN03232 1452 SPQELLSRdTSAFFRMVH 1469
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
 276-498 1.83e-44

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: 156.42  E-value: 1.83e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 276 TGLVEFKDVTFAY-PTRPEtdVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHDYLH 354
Cdd:cd03369    4 HGEIEVENLSVRYaPDLPP--VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 355 SKIALVGQEPVLFARTIKENIS-YG-LSDVsmemvvqaatkanahDFITTLpkgydtSVGEKGLQLSGGQKQRVAIARAL 432
Cdd:cd03369   82 SSLTIIPQDPTLFSGTIRSNLDpFDeYSDE---------------EIYGAL------RVSEGGLNLSQGQRQLLCLARAL 140

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 961964003 433 IRQPRVLILDEATSALDAESEHIVQQALNSIMQEHTVLVIAHRLSTVEKADNIIVIDRGQVAERGT 498
Cdd:cd03369  141 LKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
 278-504 2.68e-44

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: 156.97  E-value: 2.68e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 278 LVEFKDVTFAYPTRP-ETDVLKGVSFTLRPGEVTALVGPSGSGKSS---CVSLLENfylPQGGQVLLDGKPVNEFQHDYL 353
Cdd:cd03258    1 MIELKNVSKVFGDTGgKVTALKDVSLSVPKGEIFGIIGRSGAGKSTlirCINGLER---PTSGSVLVDGTDLTLLSGKEL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 354 ---HSKIALVGQEPVLF-ARTIKENISYGLSDVSMEMVVQAAtKANA-------HDFITTLPKgydtsvgekglQLSGGQ 422
Cdd:cd03258   78 rkaRRRIGMIFQHFNLLsSRTVFENVALPLEIAGVPKAEIEE-RVLEllelvglEDKADAYPA-----------QLSGGQ 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 423 KQRVAIARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQEH--TVLVIAHRLSTVEK-ADNIIVIDRGQVAERGTH 499
Cdd:cd03258  146 KQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELglTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTV 225


                 ....*
gi 961964003 500 SQLMA 504
Cdd:cd03258  226 EEVFA 230
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
 278-505 1.06e-43

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: 155.73  E-value: 1.06e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 278 LVEFKDVTFAYPTRPE-TDVLKGVSFTLRPGEVTALVGPSGSGKSS---CVSLLENfylPQGGQVLLDGKPVNEFQHDYL 353
Cdd:COG1124    1 MLEVRNLSVSYGQGGRrVPVLKDVSLEVAPGESFGLVGESGSGKSTllrALAGLER---PWSGEVTFDGRPVTRRRRKAF 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 354 HSKIALVGQEP--VLFAR-TIKENIS-----YGLSDVsMEMVVQAATKANahdfittLPKGYdtsvgekgL-----QLSG 420
Cdd:COG1124   78 RRRVQMVFQDPyaSLHPRhTVDRILAeplriHGLPDR-EERIAELLEQVG-------LPPSF--------LdryphQLSG 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 421 GQKQRVAIARALIRQPRVLILDEATSALDAesehIVQ----QALNSIMQEH--TVLVIAHRLSTVEK-ADNIIVIDRGQV 493
Cdd:COG1124  142 GQRQRVAIARALILEPELLLLDEPTSALDV----SVQaeilNLLKDLREERglTYLFVSHDLAVVAHlCDRVAVMQNGRI 217

                        250
                 ....*....|..
gi 961964003 494 AERGTHSQLMAT 505
Cdd:COG1124  218 VEELTVADLLAG 229
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
 278-504 1.67e-43

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: 161.99  E-value: 1.67e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 278 LVEFKDVTFAYPTRpETDVLKGVSFTLRPGEVTALVGPSGSGKSScVSLLENFYLPQG----GQVLLDGKPVNEFQHDYL 353
Cdd:COG1123    4 LLEVRDLSVRYPGG-DVPAVDGVSLTIAPGETVALVGESGSGKST-LALALMGLLPHGgrisGEVLLDGRDLLELSEALR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 354 HSKIALVGQEP--VLFARTIKENISYGLsdvsmemVVQAATKANAHDFITTLPK--GYDTSVGEKGLQLSGGQKQRVAIA 429
Cdd:COG1123   82 GRRIGMVFQDPmtQLNPVTVGDQIAEAL-------ENLGLSRAEARARVLELLEavGLERRLDRYPHQLSGGQRQRVAIA 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 961964003 430 RALIRQPRVLILDEATSALDAESEHIVQQALNSIMQEH--TVLVIAHRLSTV-EKADNIIVIDRGQVAERGTHSQLMA 504
Cdd:COG1123  155 MALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILA 232
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
 280-492 3.56e-43

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: 151.24  E-value: 3.56e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 280 EFKDVTFAYPTRPetdVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHDYLHSKIAL 359
Cdd:cd00267    1 EIENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 360 VgqepvlfartikenisyglsdvsmemvvqaatkanahdfittlpkgydtsvgekgLQLSGGQKQRVAIARALIRQPRVL 439
Cdd:cd00267   78 V-------------------------------------------------------PQLSGGQRQRVALARALLLNPDLL 102

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 961964003 440 ILDEATSALDAESEHIVQQALNSIMQEH-TVLVIAHRLSTVEKA-DNIIVIDRGQ 492
Cdd:cd00267  103 LLDEPTSGLDPASRERLLELLRELAEEGrTVIIVTHDPELAELAaDRVIVLKDGK 157
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
278-495 7.42e-43

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 152.89  E-value: 7.42e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 278 LVEFKDVTFAYPT-RPETDVLKGVSFTLRPGEVTALVGPSGSGKS---SCVSLLENfylPQGGQVLLDGKPVNEFQHDYL 353
Cdd:COG1136    4 LLELRNLTKSYGTgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKStllNILGGLDR---PTSGEVLIDGQDISSLSEREL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 354 ----HSKIALVGQEPVLFAR-TIKENISYGL------SDVSMEMVVQAATKANAHDFITTLPKgydtsvgekglQLSGGQ 422
Cdd:COG1136   81 arlrRRHIGFVFQFFNLLPElTALENVALPLllagvsRKERRERARELLERVGLGDRLDHRPS-----------QLSGGQ 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 961964003 423 KQRVAIARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQEH--TVLVIAHRLSTVEKADNIIVIDRGQVAE 495
Cdd:COG1136  150 QQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELgtTIVMVTHDPELAARADRVIRLRDGRIVS 224
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
 278-502 7.53e-43

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


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 153.23  E-value: 7.53e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 278 LVEFKDVTFAYPtrpETDVLKGVSFTLRPGEVTALVGPSGSGKSS---CVSLLENfylPQGGQVLLDGKPV--NEFQHDY 352
Cdd:COG1126    1 MIEIENLHKSFG---DLEVLKGISLDVEKGEVVVIIGPSGSGKSTllrCINLLEE---PDSGTITVDGEDLtdSKKDINK 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 353 LHSKIALVGQEPVLFA-RTIKENISYGLsdvsmeMVVQAATKANAHDfittlpKGYD--TSVG--EKG----LQLSGGQK 423
Cdd:COG1126   75 LRRKVGMVFQQFNLFPhLTVLENVTLAP------IKVKKMSKAEAEE------RAMEllERVGlaDKAdaypAQLSGGQQ 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 424 QRVAIARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQEH-TVLVIAHRLSTVEK-ADNIIVIDRGQVAERGTHSQ 501
Cdd:COG1126  143 QRVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEGmTMVVVTHEMGFAREvADRVVFMDGGRIVEEGPPEE 222


                 .
gi 961964003 502 L 502
Cdd:COG1126  223 F 223
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
 278-503 1.11e-42

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: 153.28  E-value: 1.11e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 278 LVEFKDVTFAYPTRPetdVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHDYLHSKI 357
Cdd:COG1120    1 MLEAENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 358 ALVGQEPVL-FARTIKENISYG----------LSDVSMEMVVQAATKANAHDFIttlpkgyDTSVGEkglqLSGGQKQRV 426
Cdd:COG1120   78 AYVPQEPPApFGLTVRELVALGryphlglfgrPSAEDREAVEEALERTGLEHLA-------DRPVDE----LSGGERQRV 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 427 AIARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQEH--TVLVIAH------RLstvekADNIIVIDRGQVAERGT 498
Cdd:COG1120  147 LIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERgrTVVMVLHdlnlaaRY-----ADRLVLLKDGRIVAQGP 221


                 ....*
gi 961964003 499 HSQLM 503
Cdd:COG1120  222 PEEVL 226
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
 279-493 1.91e-42

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: 149.86  E-value: 1.91e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 279 VEFKDVTFAYPTRPetdVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHDYLHsKIA 358
Cdd:cd03230    1 IEVRNLSKRYGKKT---ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKR-RIG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 359 LVGQEPVLFAR-TIKENisyglsdvsmemvvqaatkanahdfittlpkgydtsvgekgLQLSGGQKQRVAIARALIRQPR 437
Cdd:cd03230   77 YLPEEPSLYENlTVREN-----------------------------------------LKLSGGMKQRLALAQALLHDPE 115

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 961964003 438 VLILDEATSALDAESEHIVQQALNSIMQE-HTVLVIAHRLSTVEK-ADNIIVIDRGQV 493
Cdd:cd03230  116 LLILDEPTSGLDPESRREFWELLRELKKEgKTILLSSHILEEAERlCDRVAILNNGRI 173
ECF_ATPase_1 TIGR04520
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
 279-535 2.08e-42

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: 152.97  E-value: 2.08e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  279 VEFKDVTFAYPtRPETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDG-KPVNEFQHDYLHSKI 357
Cdd:TIGR04520   1 IEVENVSFSYP-ESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGlDTLDEENLWEIRKKV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  358 ALVGQEP--VLFARTIKENISYGLSDVSM---EMV--VQAATKA-NAHDFITTLPKgydtsvgekglQLSGGQKQRVAIA 429
Cdd:TIGR04520  80 GMVFQNPdnQFVGATVEDDVAFGLENLGVpreEMRkrVDEALKLvGMEDFRDREPH-----------LLSGGQKQRVAIA 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  430 RALIRQPRVLILDEATSALDAESEHIVQQALNSIMQEH--TVLVIAHRLSTVEKADNIIVIDRGQVAERGT------HSQ 501
Cdd:TIGR04520 149 GVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEgiTVISITHDMEEAVLADRVIVMNKGKIVAEGTpreifsQVE 228

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 961964003  502 LMATGGL----YCKLVQR-QVLGIETGAEVLNPSETVRW 535
Cdd:TIGR04520 229 LLKEIGLdvpfITELAKAlKKRGIPLPPDILTEEELVDE 267
ABC_6TM_bac_exporter_ABCB8_10_like cd18575
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ...
 31-254 2.38e-42

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: 153.41  E-value: 2.38e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  31 RLNVRLRSRLFRTLMTQEIAFFDENHTGDILSRLSADTTQVSDLISQNVNVFLRSVIKGTGFIIFMFRMSWKLTLVTMMG 110
Cdd:cd18575   66 RVVADLRKAVFAHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLV 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 111 FPFIALVSKLYGEYYKKLTKEVQTVLAEANKVAEETISGMRTVRSFANESREANSYYAKLLVMFQLNKKQALAYACYMWS 190
Cdd:cd18575  146 IPLVVLPIILFGRRVRRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRARALLTAL 225

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 961964003 191 SCISELALEVAVLYYGGHLVLTDQLSSGGLISFFIYMLELGECFESIASVYSGLMQGVGAAEKV 254
Cdd:cd18575  226 VIFLVFGAIVFVLWLGAHDVLAGRMSAGELSQFVFYAVLAAGSVGALSEVWGDLQRAAGAAERL 289
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
 279-493 7.06e-42

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: 149.95  E-value: 7.06e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 279 VEFKDVTFAYPTRPE-TDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEF----QHDYL 353
Cdd:cd03255    1 IELKNLSKTYGGGGEkVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLsekeLAAFR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 354 HSKIALVGQEPVLFAR-TIKENISYGL------SDVSMEMVVQAATKANAHDFITTLPKgydtsvgekglQLSGGQKQRV 426
Cdd:cd03255   81 RRHIGFVFQSFNLLPDlTALENVELPLllagvpKKERRERAEELLERVGLGDRLNHYPS-----------ELSGGQQQRV 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 961964003 427 AIARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQE--HTVLVIAHRLSTVEKADNIIVIDRGQV 493
Cdd:cd03255  150 AIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEagTTIVVVTHDPELAEYADRIIELRDGKI 218
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
279-498 1.15e-41

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 152.92  E-value: 1.15e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 279 VEFKDVTFAYPTRP-ETDVLKGVSFTLRPGEVTALVGPSGSGKSS---CVSLLENfylPQGGQVLLDGKPVNE------- 347
Cdd:COG1135    2 IELENLSKTFPTKGgPVTALDDVSLTIEKGEIFGIIGYSGAGKSTlirCINLLER---PTSGSVLVDGVDLTAlserelr 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 348 ---------FQHDYLhskialvgqepvLFARTIKENISY-----------------------GLSDvsmemvvqaatKAN 395
Cdd:COG1135   79 aarrkigmiFQHFNL------------LSSRTVAENVALpleiagvpkaeirkrvaellelvGLSD-----------KAD 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 396 AHdfittlPKgydtsvgekglQLSGGQKQRVAIARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQEH--TVLVIA 473
Cdd:COG1135  136 AY------PS-----------QLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELglTIVLIT 198

                        250       260
                 ....*....|....*....|....*.
gi 961964003 474 HRLSTVEK-ADNIIVIDRGQVAERGT 498
Cdd:COG1135  199 HEMDVVRRiCDRVAVLENGRIVEQGP 224
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
 278-495 2.63e-41

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 149.08  E-value: 2.63e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 278 LVEFKDVTFAYPTRPetdVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHdylhsKI 357
Cdd:COG1121    6 AIELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARR-----RI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 358 ALVGQ-------------EPVLFARTIKENISYGLSDVSMEMVVQAATKANAHDFIttlpkgyDTSVGEkglqLSGGQKQ 424
Cdd:COG1121   78 GYVPQraevdwdfpitvrDVVLMGRYGRRGLFRRPSRADREAVDEALERVGLEDLA-------DRPIGE----LSGGQQQ 146

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 961964003 425 RVAIARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQE-HTVLVIAHRLSTVEK-ADNIIVIDRGQVAE 495
Cdd:COG1121  147 RVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREgKTILVVTHDLGAVREyFDRVLLLNRGLVAH 219
ABC_6TM_Pgp_ABCB1_D2_like cd18578
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ...
 9-263 5.20e-41

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: 150.68  E-value: 5.20e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   9 LFFLL---SSMAIGVRGGVFTLTMARLNVRLRSRLFRTLMTQEIAFFD--ENHTGDILSRLSADTTQVSDLISQNVNVFL 83
Cdd:cd18578   57 MFLVLaivAGIAYFLQGYLFGIAGERLTRRLRKLAFRAILRQDIAWFDdpENSTGALTSRLSTDASDVRGLVGDRLGLIL 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  84 RSVIK-GTGFIIfMFRMSWKLTLVTMMGFPFIALVSKLYGEYYKKLTKEVQTVLAEANKVAEETISGMRTVRSFANESRE 162
Cdd:cd18578  137 QAIVTlVAGLII-AFVYGWKLALVGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYF 215

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 163 ANSYYAKLLVMFQLNKKQA----LAYACymwSSCISeLALEVAVLYYGGHLVLTDQLSsggLISFFIymlelgeCFESI- 237
Cdd:cd18578  216 LEKYEEALEEPLKKGLRRAlisgLGFGL---SQSLT-FFAYALAFWYGGRLVANGEYT---FEQFFI-------VFMALi 281

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 961964003 238 -ASVYSGLM--------QGVGAAEKVFEYLDRKPK 263
Cdd:cd18578  282 fGAQSAGQAfsfapdiaKAKAAAARIFRLLDRKPE 316
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
 279-492 1.14e-40

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: 145.02  E-value: 1.14e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 279 VEFKDVTFAYPtrpETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVN--EFQHDYLHSK 356
Cdd:cd03229    1 LELKNVSKRYG---QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTdlEDELPPLRRR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 357 IALVGQEPVLFAR-TIKENISYGLSdvsmemvvqaatkanahdfittlpkgydtsvgekglqlsGGQKQRVAIARALIRQ 435
Cdd:cd03229   78 IGMVFQDFALFPHlTVLENIALGLS---------------------------------------GGQQQRVALARALAMD 118

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 436 PRVLILDEATSALDAESEHIVQQALNSIMQEH--TVLVIAHRLSTVEK-ADNIIVIDRGQ 492
Cdd:cd03229  119 PDVLLLDEPTSALDPITRREVRALLKSLQAQLgiTVVLVTHDLDEAARlADRVVVLRDGK 178
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
 279-493 4.55e-40

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: 144.59  E-value: 4.55e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 279 VEFKDVTFAYPTRPetdVLKGVSFTLRPGEVTALVGPSGSGKSS---CVSLLENfylPQGGQVLLDGKPVN--EFQHDYL 353
Cdd:cd03262    1 IEIKNLHKSFGDFH---VLKGIDLTVKKGEVVVIIGPSGSGKSTllrCINLLEE---PDSGTIIIDGLKLTddKKNINEL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 354 HSKIALVGQEPVLFA-RTIKENISYGLsdvsmeMVVQAATKANAhdfiTTLPKGYDTSVG--EKG----LQLSGGQKQRV 426
Cdd:cd03262   75 RQKVGMVFQQFNLFPhLTVLENITLAP------IKVKGMSKAEA----EERALELLEKVGlaDKAdaypAQLSGGQQQRV 144

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 961964003 427 AIARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQEH-TVLVIAHRLSTVEK-ADNIIVIDRGQV 493
Cdd:cd03262  145 AIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGmTMVVVTHEMGFAREvADRVIFMDDGRI 213
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
278-535 1.23e-38

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 142.85  E-value: 1.23e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 278 LVEFKDVTFAYPTRpETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHDYLHSKI 357
Cdd:PRK13635   5 IIRVEHISFRYPDA-ATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 358 ALVGQEP--VLFARTIKENISYGLSDVSM---EMV--VQAATK-ANAHDFITTLPKgydtsvgekglQLSGGQKQRVAIA 429
Cdd:PRK13635  84 GMVFQNPdnQFVGATVQDDVAFGLENIGVpreEMVerVDQALRqVGMEDFLNREPH-----------RLSGGQKQRVAIA 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 430 RALIRQPRVLILDEATSALDAESEHIVQQALNSIMQEH--TVLVIAHRLSTVEKADNIIVIDRGQVAERGTHSQLMATGG 507
Cdd:PRK13635 153 GVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKgiTVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKSGH 232

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 961964003 508 --------------LYCKLVQRqvlGIETGAEVLNPSETVRW 535
Cdd:PRK13635 233 mlqeigldvpfsvkLKELLKRN---GILLPNTYLTMESLVDE 271
PLN03130 PLN03130
ABC transporter C family member; Provisional
 250-514 1.78e-38

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 151.81  E-value: 1.78e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  250 AAEKVFEYLDRKPKHPA--DGTEAPNS--CTGLVEFKDVTFAYptRPE-TDVLKGVSFTLRPGEVTALVGPSGSGKSSCV 324
Cdd:PLN03130 1205 AVERVGTYIDLPSEAPLviENNRPPPGwpSSGSIKFEDVVLRY--RPElPPVLHGLSFEISPSEKVGIVGRTGAGKSSML 1282

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  325 SLLENFYLPQGGQVLLDGKPVNEFQHDYLHSKIALVGQEPVLFARTIKENISyGLSDVSMEMVVQAATKANAHDFITTLP 404
Cdd:PLN03130 1283 NALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLD-PFNEHNDADLWESLERAHLKDVIRRNS 1361

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  405 KGYDTSVGEKGLQLSGGQKQRVAIARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQEHTVLVIAHRLSTVEKADN 484
Cdd:PLN03130 1362 LGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDR 1441

                         250       260       270
                  ....*....|....*....|....*....|.
gi 961964003  485 IIVIDRGQVAERGTHSQLMAT-GGLYCKLVQ 514
Cdd:PLN03130 1442 ILVLDAGRVVEFDTPENLLSNeGSAFSKMVQ 1472
ABC_6TM_ABCB8_like cd18574
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ...
 4-225 3.02e-38

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: 142.30  E-value: 3.02e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   4 APPFTLFFLLSSMAIGVRGGVFTLTMA--RLNVRLRSRLFRTLMTQEIAFFDENHTGDILSRLSADttqVSDLIS---QN 78
Cdd:cd18574   43 KPALKLLGLYLLQSLLTFAYISLLSVVgeRVAARLRNDLFSSLLRQDIAFFDTHRTGELVNRLTAD---VQEFKSsfkQC 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  79 VNVFLRSVIKGTGFIIFMFRMSWKLTLVTMMGFPFIALVSKLYGEYYKKLTKEVQTVLAEANKVAEETISGMRTVRSFAN 158
Cdd:cd18574  120 VSQGLRSVTQTVGCVVSLYLISPKLTLLLLVIVPVVVLVGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAM 199

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 159 ESREANSYYAKLLVMFQLNKKQALAYACYmwsSCISELALE---VAVLYYGGHLVLTDQLSSGGLISFFI 225
Cdd:cd18574  200 EDRELELYEEEVEKAAKLNEKLGLGIGIF---QGLSNLALNgivLGVLYYGGSLVSRGELTAGDLMSFLV 266
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
 278-498 3.95e-38

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 143.70  E-value: 3.95e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 278 LVEFKDVTFAYPtrpETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNE---FQHDylh 354
Cdd:COG3842    5 ALELENVSKRYG---DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGlppEKRN--- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 355 skIALVGQEPVLFA-RTIKENISYGLSdvsMEMVVQAATKANAHDFITTlpkgydtsVGEKGL------QLSGGQKQRVA 427
Cdd:COG3842   79 --VGMVFQDYALFPhLTVAENVAFGLR---MRGVPKAEIRARVAELLEL--------VGLEGLadryphQLSGGQQQRVA 145

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 961964003 428 IARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQEH--TVLVIAHRLS---TVekADNIIVIDRGQVAERGT 498
Cdd:COG3842  146 LARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELgiTFIYVTHDQEealAL--ADRIAVMNDGRIEQVGT 219
ABC_6TM_YknU_like cd18542
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ...
 9-227 1.21e-37

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: 140.64  E-value: 1.21e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   9 LFFLLSSMAIGVRGGVFTLTMARLNV--------RLRSRLFRTLMTQEIAFFDENHTGDILSRLSADTTQVSDLISQNVN 80
Cdd:cd18542   39 WLLALLILGVALLRGVFRYLQGYLAEkasqkvayDLRNDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLV 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  81 VFLRSVIKGTGFIIFMFRMSWKLTLVTMMGFPFIALVSKLYGEYYKKLTKEVQTVLAEANKVAEETISGMRTVRSFANES 160
Cdd:cd18542  119 ELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYVFFKKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFARED 198

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 961964003 161 RE------ANSYYakllvmFQLNKKQALAYACYM-WSSCISELALeVAVLYYGGHLVLTDQLSSGGLISFFIYM 227
Cdd:cd18542  199 YEiekfdkENEEY------RDLNIKLAKLLAKYWpLMDFLSGLQI-VLVLWVGGYLVINGEITLGELVAFISYL 265
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
 279-497 1.58e-37

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: 137.65  E-value: 1.58e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 279 VEFKDVTFAYPtrpETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVnefQHDYLHSK-I 357
Cdd:cd03259    1 LELKGLSKTYG---SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV---TGVPPERRnI 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 358 ALVGQEPVLFA-RTIKENISYGLSDVSMEmvvQAATKANAHDFITTLpkGYDTSVGEKGLQLSGGQKQRVAIARALIRQP 436
Cdd:cd03259   75 GMVFQDYALFPhLTVAENIAFGLKLRGVP---KAEIRARVRELLELV--GLEGLLNRYPHELSGGQQQRVALARALAREP 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 961964003 437 RVLILDEATSALDAESEHIVQQALNSIMQEH--TVLVIAHRLS-TVEKADNIIVIDRGQVAERG 497
Cdd:cd03259  150 SLLLLDEPLSALDAKLREELREELKELQRELgiTTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
280-504 1.65e-37

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 138.35  E-value: 1.65e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 280 EFKDVTFAYPTRPetdvlKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKpvnefqhDYLHS---- 355
Cdd:COG3840    3 RLDDLTYRYGDFP-----LRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQ-------DLTALppae 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 356 -KIALVGQEPVLFAR-TIKENISYG------LSDVSMEMVVQAATKANAHDFITTLPKgydtsvgekglQLSGGQKQRVA 427
Cdd:COG3840   71 rPVSMLFQENNLFPHlTVAQNIGLGlrpglkLTAEQRAQVEQALERVGLAGLLDRLPG-----------QLSGGQRQRVA 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 428 IARALIRQPRVLILDEATSALD----AESEHIVQQalnsIMQEH--TVLVIAHRLSTVEK-ADNIIVIDRGQVAERGTHS 500
Cdd:COG3840  140 LARCLVRKRPILLLDEPFSALDpalrQEMLDLVDE----LCRERglTVLMVTHDPEDAARiADRVLLVADGRIAADGPTA 215


                 ....
gi 961964003 501 QLMA 504
Cdd:COG3840  216 ALLD 219
ABC_6TM_LmrA_like cd18551
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ...
 7-254 1.68e-37

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: 140.26  E-value: 1.68e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   7 FTLFFLLSSMAIGVRGGVFTLTMARLNVRLRSRLFRTLMTQEIAFFDENHTGDILSRLSADTTQVSDLISQNVNVFLRSV 86
Cdd:cd18551   42 LVALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGV 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  87 IKGTGFIIFMFRMSWKLTLVTMMGFPFIALVSKLYGEYYKKLTKEVQTVLAEANKVAEETISGMRTVRSFANESREANSY 166
Cdd:cd18551  122 LTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRG 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 167 YAKLLVMFQLNKKQALAYACyMW--SSCISELALeVAVLYYGGHLVLTDQLSSGGLISFFIYMLELGECFESIASVYSGL 244
Cdd:cd18551  202 GEAAERLYRAGLKAAKIEAL-IGplMGLAVQLAL-LVVLGVGGARVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQL 279

                        250
                 ....*....|
gi 961964003 245 MQGVGAAEKV 254
Cdd:cd18551  280 QKALGALERI 289
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
 280-494 2.65e-37

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: 137.28  E-value: 2.65e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 280 EFKDVTFAYPTRPetdVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHdylhsKIAL 359
Cdd:cd03235    1 EVEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERK-----RIGY 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 360 VGQEPVL---FARTIKENISYGL-SDVSMEMVVQAATKA---NAHDFittlpkgydtsVGEKGL------QLSGGQKQRV 426
Cdd:cd03235   73 VPQRRSIdrdFPISVRDVVLMGLyGHKGLFRRLSKADKAkvdEALER-----------VGLSELadrqigELSGGQQQRV 141

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 427 AIARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQE-HTVLVIAHRLSTVEK-ADNIIVIDRGQVA 494
Cdd:cd03235  142 LLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREgMTILVVTHDLGLVLEyFDRVLLLNRTVVA 211
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
 280-497 3.34e-37

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


Pssm-ID: 213181 [Multi-domain]  Cd Length: 180  Bit Score: 135.64  E-value: 3.34e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 280 EFKDVTFAYPTRPetdVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHDYLHSKIAL 359
Cdd:cd03214    1 EVENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAY 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 360 VGQepvlfartikenisyglsdvSMEMVvqaatkaNAHDFittLPKGYDTsvgekglqLSGGQKQRVAIARALIRQPRVL 439
Cdd:cd03214   78 VPQ--------------------ALELL-------GLAHL---ADRPFNE--------LSGGERQRVLLARALAQEPPIL 119

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 961964003 440 ILDEATSALDAESEHIVQQALNSIMQEH--TVLVIAHRLSTVEK-ADNIIVIDRGQVAERG 497
Cdd:cd03214  120 LLDEPTSHLDIAHQIELLELLRRLARERgkTVVMVLHDLNLAARyADRVILLKDGRIVAQG 180
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
 279-505 8.45e-37

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: 136.48  E-value: 8.45e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 279 VEFKDVTFAYPTRPetdVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHDYLHS--- 355
Cdd:cd03261    1 IELRGLTKSFGGRT---VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRlrr 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 356 KIALVGQEPVLF-ARTIKENISYGLsdvsmemvvqaatkaNAHdfiTTLPKG-YDTSVGEK----GL---------QLSG 420
Cdd:cd03261   78 RMGMLFQSGALFdSLTVFENVAFPL---------------REH---TRLSEEeIREIVLEKleavGLrgaedlypaELSG 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 421 GQKQRVAIARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQEH--TVLVIAHRLSTVEK-ADNIIVIDRGQVAERG 497
Cdd:cd03261  140 GMKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELglTSIMVTHDLDTAFAiADRIAVLYDGKIVAEG 219


                 ....*...
gi 961964003 498 THSQLMAT 505
Cdd:cd03261  220 TPEELRAS 227
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
278-505 1.40e-36

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 135.99  E-value: 1.40e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 278 LVEFKDVTFAYPtrpETDVLKGVSFTLRPGEVTALVGPSGSGKSS---CVSLLENFylpQGGQVLLDGKPVNEFQHD--Y 352
Cdd:PRK09493   1 MIEFKNVSKHFG---PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTllrCINKLEEI---TSGDLIVDGLKVNDPKVDerL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 353 LHSKIALVGQEPVLFAR-TIKENISYGlsdvsmEMVVQAATKANAHDFITTLpkgydtsVGEKGL---------QLSGGQ 422
Cdd:PRK09493  75 IRQEAGMVFQQFYLFPHlTALENVMFG------PLRVRGASKEEAEKQAREL-------LAKVGLaerahhypsELSGGQ 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 423 KQRVAIARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQE-HTVLVIAHRLSTVEK-ADNIIVIDRGQVAERGTHS 500
Cdd:PRK09493 142 QQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEgMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQ 221


                 ....*
gi 961964003 501 QLMAT 505
Cdd:PRK09493 222 VLIKN 226
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
279-495 1.64e-36

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 135.18  E-value: 1.64e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 279 VEFKDVTFAYPTRPEtdVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHD---YLHS 355
Cdd:COG2884    2 IRFENVSKRYPGGRE--ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRReipYLRR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 356 KIALVGQE-PVLFARTIKENISY-----GLSDVSMEMVVQAA-------TKANAhdfittLPKgydtsvgekglQLSGGQ 422
Cdd:COG2884   80 RIGVVFQDfRLLPDRTVYENVALplrvtGKSRKEIRRRVREVldlvglsDKAKA------LPH-----------ELSGGE 142

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 961964003 423 KQRVAIARALIRQPRVLILDEATSALDAE-SEHIVqQALNSIMQEHTVLVIA-HRLSTVEKADN-IIVIDRGQVAE 495
Cdd:COG2884  143 QQRVAIARALVNRPELLLADEPTGNLDPEtSWEIM-ELLEEINRRGTTVLIAtHDLELVDRMPKrVLELEDGRLVR 217
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
 278-505 2.85e-36

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: 135.11  E-value: 2.85e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 278 LVEFKDVTFAYPTRPetdVLKGVSFTLRPGEVTALVGPSGSGKS----SCVSLLEnfylPQGGQVLLDGKPVNEF---QH 350
Cdd:COG1127    5 MIEVRNLTKSFGDRV---VLDGVSLDVPRGEILAIIGGSGSGKSvllkLIIGLLR----PDSGEILVDGQDITGLsekEL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 351 DYLHSKIALVGQEPVLF-ARTIKENISYGL---SDVSMEMVVQ-AATKANA---HDFITTLPKgydtsvgekglQLSGGQ 422
Cdd:COG1127   78 YELRRRIGMLFQGGALFdSLTVFENVAFPLrehTDLSEAEIRElVLEKLELvglPGAADKMPS-----------ELSGGM 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 423 KQRVAIARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQEH--TVLVIAHRLSTVEK-ADNIIVIDRGQVAERGTH 499
Cdd:COG1127  147 RKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELglTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTP 226


                 ....*.
gi 961964003 500 SQLMAT 505
Cdd:COG1127  227 EELLAS 232
PhnC COG3638
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ...
 278-493 2.98e-36

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


Pssm-ID: 442855 [Multi-domain]  Cd Length: 249  Bit Score: 135.57  E-value: 2.98e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 278 LVEFKDVTFAYPTRpeTDVLKGVSFTLRPGEVTALVGPSGSGKSS---CVSLLENfylPQGGQVLLDGKPVNEFQHDYLH 354
Cdd:COG3638    2 MLELRNLSKRYPGG--TPALDDVSLEIERGEFVALIGPSGAGKSTllrCLNGLVE---PTSGEILVDGQDVTALRGRALR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 355 ---SKIALVGQEPVLFAR-TIKENISYG-LSDV----SMEMVVQAATKANAHDFITTLpkgydtsvgekGL--------- 416
Cdd:COG3638   77 rlrRRIGMIFQQFNLVPRlSVLTNVLAGrLGRTstwrSLLGLFPPEDRERALEALERV-----------GLadkayqrad 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 417 QLSGGQKQRVAIARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQEH--TVLVIAHRLSTVEK-ADNIIVIDRGQV 493
Cdd:COG3638  146 QLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDgiTVVVNLHQVDLARRyADRIIGLRDGRV 225
ABC_6TM_TmrB_like cd18541
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ...
 36-227 3.16e-36

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: 136.77  E-value: 3.16e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  36 LRSRLFRTLMTQEIAFFDENHTGDILSRLSADTTQVSDLISQNVNVFLRSVIKGTGFIIFMFRMSWKLTLVTMMGFPFIA 115
Cdd:cd18541   75 LRNDLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLA 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 116 LVSKLYGEYYKKLTKEVQTVLAEANKVAEETISGMRTVRSFANESREANSYYAKLLVMFQLNKKQALAYACYM-WSSCIS 194
Cdd:cd18541  155 LLVYRLGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFpLIGLLI 234

                        170       180       190
                 ....*....|....*....|....*....|...
gi 961964003 195 ELALeVAVLYYGGHLVLTDQLSSGGLISFFIYM 227
Cdd:cd18541  235 GLSF-LIVLWYGGRLVIRGTITLGDLVAFNSYL 266
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
 279-498 5.79e-35

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 132.81  E-value: 5.79e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 279 VEFKDVTFAYPTRpETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHDYLHSKIA 358
Cdd:PRK13632   8 IKVENVSFSYPNS-ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 359 LVGQEP--VLFARTIKENISYGLSDVSM---EM---VVQAATKANAHDFITTLPkgydtsvgekgLQLSGGQKQRVAIAR 430
Cdd:PRK13632  87 IIFQNPdnQFIGATVEDDIAFGLENKKVppkKMkdiIDDLAKKVGMEDYLDKEP-----------QNLSGGQKQRVAIAS 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 431 ALIRQPRVLILDEATSALDAESEHIVQQALNSIMQE--HTVLVIAHRLSTVEKADNIIVIDRGQVAERGT 498
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTrkKTLISITHDMDEAILADKVIVFSEGKLIAQGK 225
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
 279-497 1.01e-34

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: 130.31  E-value: 1.01e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 279 VEFKDVTFAYPTRPETdvlkgVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKpvnefqhDYLHSKIA 358
Cdd:cd03298    1 VRLDKIRFSYGEQPMH-----FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGV-------DVTAAPPA 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 359 -----LVGQEPVLFAR-TIKENISYGLS------DVSMEMVVQAATKANAHDFITTLPKgydtsvgekglQLSGGQKQRV 426
Cdd:cd03298   69 drpvsMLFQENNLFAHlTVEQNVGLGLSpglkltAEDRQAIEVALARVGLAGLEKRLPG-----------ELSGGERQRV 137

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 961964003 427 AIARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQEH--TVLVIAHRLSTVEK-ADNIIVIDRGQVAERG 497
Cdd:cd03298  138 ALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETkmTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
 300-497 1.07e-34

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: 130.11  E-value: 1.07e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 300 VSFTLrPGEVTALVGPSGSGKSS---CVSLLENfylPQGGQVLLDGKPVNEFQ-------HDylhSKIALVGQEPVLFAR 369
Cdd:cd03297   17 IDFDL-NEEVTGIFGASGAGKSTllrCIAGLEK---PDGGTIVLNGTVLFDSRkkinlppQQ---RKIGLVFQQYALFPH 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 370 -TIKENISYGLSDVS-MEMVVQAatkanahDFITTLpKGYDTSVGEKGLQLSGGQKQRVAIARALIRQPRVLILDEATSA 447
Cdd:cd03297   90 lNVRENLAFGLKRKRnREDRISV-------DELLDL-LGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSA 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 961964003 448 LDAESEHIVQQALNSIMQEH--TVLVIAHRLSTVEK-ADNIIVIDRGQVAERG 497
Cdd:cd03297  162 LDRALRLQLLPELKQIKKNLniPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
ABC_6TM_TmrA_like cd18544
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ...
 7-254 1.26e-34

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: 132.13  E-value: 1.26e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   7 FTLFFLLSSMAIGVRGGVFTLTMARL--NV--RLRSRLFRTLMTQEIAFFDENHTGDILSRLSADTTQVSDLISQNVNVF 82
Cdd:cd18544   43 LALLYLGLLLLSFLLQYLQTYLLQKLgqRIiyDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTL 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  83 LRSVIKGTGFIIFMFRMSWKLTLVTMMGFPFIALVSKLYGEYYKKLTKEVQTVLAEANKVAEETISGMRTVRSFANESRE 162
Cdd:cd18544  123 IGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATYLFRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKRE 202

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 163 ANSYYAKLLVMFQLNKKQALAYACYMWS-SCISELALeVAVLYYGGHLVLTDQLSSGGLISFFIYMLELGECFESIASVY 241
Cdd:cd18544  203 FEEFDEINQEYRKANLKSIKLFALFRPLvELLSSLAL-ALVLWYGGGQVLSGAVTLGVLYAFIQYIQRFFRPIRDLAEKF 281

                        250
                 ....*....|...
gi 961964003 242 SGLMQGVGAAEKV 254
Cdd:cd18544  282 NILQSAMASAERI 294
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
 280-502 3.14e-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: 129.61  E-value: 3.14e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 280 EFKDVTFAYPTrpETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHDYLH---SK 356
Cdd:cd03256    2 EVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRqlrRQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 357 IALVGQEPVLFAR-TIKENISYGlsdvsmemvvqaatKANAHDFITTLPKGYD-----------TSVGEKGL------QL 418
Cdd:cd03256   80 IGMIFQQFNLIERlSVLENVLSG--------------RLGRRSTWRSLFGLFPkeekqralaalERVGLLDKayqradQL 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 419 SGGQKQRVAIARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQEH--TVLVIAHRLSTVEK-ADNIIVIDRGQVAE 495
Cdd:cd03256  146 SGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEgiTVIVSLHQVDLAREyADRIVGLKDGRIVF 225


                 ....*..
gi 961964003 496 RGTHSQL 502
Cdd:cd03256  226 DGPPAEL 232
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
 279-498 4.75e-34

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


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 132.19  E-value: 4.75e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 279 VEFKDVTFAYPTRPetdVLKGVSFTLRPGEVTALVGPSGSGKSS---CVSLLENfylPQGGQVLLDGKPVneFQHdyLHS 355
Cdd:COG1118    3 IEVRNISKRFGSFT---LLDDVSLEIASGELVALLGPSGSGKTTllrIIAGLET---PDSGRIVLNGRDL--FTN--LPP 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 356 ---KIALVGQEPVLFaR--TIKENISYGLSdvsMEMVVQAATKANAHDFITTlpkgydtsVGEKGL------QLSGGQKQ 424
Cdd:COG1118   73 rerRVGFVFQHYALF-PhmTVAENIAFGLR---VRPPSKAEIRARVEELLEL--------VQLEGLadrypsQLSGGQRQ 140

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 961964003 425 RVAIARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQE--HTVLVIAH-RLSTVEKADNIIVIDRGQVAERGT 498
Cdd:COG1118  141 RVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDElgGTTVFVTHdQEEALELADRVVVMNQGRIEQVGT 217
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
 278-485 4.81e-34

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: 127.98  E-value: 4.81e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 278 LVEFKDVTFAYPTRPetdVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHDYlHSKI 357
Cdd:COG4133    2 MLEAENLSCRRGERL---LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDY-RRRL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 358 ALVGQEPVLFAR-TIKENIS-----YGLsDVSMEMVVQAATKANAHDFITTLPKgydtsvgekglQLSGGQKQRVAIARA 431
Cdd:COG4133   78 AYLGHADGLKPElTVRENLRfwaalYGL-RADREAIDEALEAVGLAGLADLPVR-----------QLSAGQKRRVALARL 145

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 961964003 432 LIRQPRVLILDEATSALDAESehivQQALNSIMQEH-----TVLVIAHRLSTVEKADNI 485
Cdd:COG4133  146 LLSPAPLWLLDEPFTALDAAG----VALLAELIAAHlarggAVLLTTHQPLELAAARVL 200
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
 279-498 5.31e-34

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


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 132.12  E-value: 5.31e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 279 VEFKDVTFAYPtrpETDVLKGVSFTLRPGEVTALVGPSGSGKSS---CVSLLENfylPQGGQVLLDGKPVNEfqhdyLHS 355
Cdd:COG3839    4 LELENVSKSYG---GVEALKDIDLDIEDGEFLVLLGPSGCGKSTllrMIAGLED---PTSGEILIGGRDVTD-----LPP 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 356 K---IALVGQEPVLF-ARTIKENISYGL--SDVS----MEMVVQAATKANAHDFITTLPKgydtsvgekglQLSGGQKQR 425
Cdd:COG3839   73 KdrnIAMVFQSYALYpHMTVYENIAFPLklRKVPkaeiDRRVREAAELLGLEDLLDRKPK-----------QLSGGQRQR 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 426 VAIARALIRQPRVLILDEATSALDAES-----EHI--VQQALNSIMqehtVLViahrlsT---VEK---ADNIIVIDRGQ 492
Cdd:COG3839  142 VALGRALVREPKVFLLDEPLSNLDAKLrvemrAEIkrLHRRLGTTT----IYV------ThdqVEAmtlADRIAVMNDGR 211


                 ....*.
gi 961964003 493 VAERGT 498
Cdd:COG3839  212 IQQVGT 217
cbiO PRK13650
energy-coupling factor transporter ATPase;
278-507 5.46e-34

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 130.24  E-value: 5.46e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 278 LVEFKDVTFAYPTRPETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHDYLHSKI 357
Cdd:PRK13650   4 IIEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 358 ALVGQEP--VLFARTIKENISYGLSDVSM------EMVVQAATKANAHDFITTLPKgydtsvgekglQLSGGQKQRVAIA 429
Cdd:PRK13650  84 GMVFQNPdnQFVGATVEDDVAFGLENKGIpheemkERVNEALELVGMQDFKEREPA-----------RLSGGQKQRVAIA 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 430 RALIRQPRVLILDEATSALDAESEHIVQQALNSIMQEH--TVLVIAHRLSTVEKADNIIVIDRGQVAERGTHSQLMATGG 507
Cdd:PRK13650 153 GAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYqmTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSRGN 232
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
 278-498 2.63e-33

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: 129.40  E-value: 2.63e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 278 LVEFKDVTFAYPTRPET-DVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQG---GQVLLDGKPVNEFQH--- 350
Cdd:COG0444    1 LLEVRNLKVYFPTRRGVvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGitsGEILFDGEDLLKLSEkel 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 351 -DYLHSKIALVGQEPvlFA-----RTIKENISYGLsdvsmeMVVQAATKANAHD-FITTLpkgydTSVG----EKGL--- 416
Cdd:COG0444   81 rKIRGREIQMIFQDP--MTslnpvMTVGDQIAEPL------RIHGGLSKAEARErAIELL-----ERVGlpdpERRLdry 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 417 --QLSGGQKQRVAIARALIRQPRVLILDEATSALDAesehIVQ-QALN---SIMQEH--TVLVIAHRLSTVEK-ADNIIV 487
Cdd:COG0444  148 phELSGGMRQRVMIARALALEPKLLIADEPTTALDV----TIQaQILNllkDLQRELglAILFITHDLGVVAEiADRVAV 223

                        250
                 ....*....|.
gi 961964003 488 IDRGQVAERGT 498
Cdd:COG0444  224 MYAGRIVEEGP 234
ABC_6TM_exporter_like cd18563
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
 12-254 2.64e-33

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: 128.78  E-value: 2.64e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  12 LLSSMAIGVRGGVFTLTMARLNVRLRSRLFRTLMTQEIAFFDENHTGDILSRLSADTTQVSDLISQNVNVFLRSVIKGTG 91
Cdd:cd18563   54 VLSALLGILRGRLLARLGERITADLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIG 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  92 FIIFMFRMSWKLTLVTMMGFPFIALVSKLYGEYYKKLTKEVQTVLAEANKVAEETISGMRTVRSFANESRE------ANS 165
Cdd:cd18563  134 IGVVLFSLNWKLALLVLIPVPLVVWGSYFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREikrfdeANQ 213

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 166 YYAKllVMFQLNKKQALAYAcyMWSSCISelALEVAVLYYGGHLVLTDQLSSGGLISFFIYMLELGECFESIASVYSGLM 245
Cdd:cd18563  214 ELLD--ANIRAEKLWATFFP--LLTFLTS--LGTLIVWYFGGRQVLSGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWIT 287


                 ....*....
gi 961964003 246 QGVGAAEKV 254
Cdd:cd18563  288 RALTSAERI 296
ABC_6TM_Tm288_like cd18547
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ...
 9-254 3.66e-33

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: 128.29  E-value: 3.66e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   9 LFFLLSSMA-IGVRGGVFTLTMARLNV--------RLRSRLFRTLMTQEIAFFDENHTGDILSRLSADTTQVSDLISQNV 79
Cdd:cd18547   44 LLRILLLLLgLYLLSALFSYLQNRLMArvsqrtvyDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSL 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  80 NVFLRSVIKGTGFIIFMFRMSWKLTLVTMMGFPFIALVSKLYGEYYKKLTKEVQTVLAEANKVAEETISGMRTVRSF--- 156
Cdd:cd18547  124 TQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLLVTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFnre 203

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 157 ---------ANE-----SREANsYYAKLL--VMFQLNkkqALAYACymwssciselaleVAVLyyGGHLVLTDQLSSGGL 220
Cdd:cd18547  204 eeaieefdeINEelykaSFKAQ-FYSGLLmpIMNFIN---NLGYVL-------------VAVV--GGLLVINGALTVGVI 264

                        250       260       270
                 ....*....|....*....|....*....|....
gi 961964003 221 ISFFIYMLELGECFESIASVYSGLMQGVGAAEKV 254
Cdd:cd18547  265 QAFLQYSRQFSQPINQISQQINSLQSALAGAERV 298
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
 279-497 8.82e-33

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: 124.20  E-value: 8.82e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 279 VEFKDVTFA---YPTRPETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLEN--FYLPQGGQVLLDGKPVNEFQhdyL 353
Cdd:cd03213    4 LSFRNLTVTvksSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRPLDKRS---F 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 354 HSKIALVGQEPVLFAR-TIKENISYglsdvsmemvvqaatkanahdfittlpkgydtSVGEKGLqlSGGQKQRVAIARAL 432
Cdd:cd03213   81 RKIIGYVPQDDILHPTlTVRETLMF--------------------------------AAKLRGL--SGGERKRVSIALEL 126

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 961964003 433 IRQPRVLILDEATSALDAESEHIVQQALNSIMQEH-TVLVIAHRLST--VEKADNIIVIDRGQVAERG 497
Cdd:cd03213  127 VSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGrTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
 293-504 1.46e-32

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: 124.47  E-value: 1.46e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 293 ETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQ-HDYLHSKIALVGQEPVLFAR-T 370
Cdd:cd03224   12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPpHERARAGIGYVPEGRRIFPElT 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 371 IKENIsyglsdvsmEMVVQAATKANAHDfitTLPKGYD------TSVGEKGLQLSGGQKQRVAIARALIRQPRVLILDEA 444
Cdd:cd03224   92 VEENL---------LLGAYARRRAKRKA---RLERVYElfprlkERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEP 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 961964003 445 TSALdaeSEHIVQQALNSIMQEH----TVLVIAHRLSTVEK-ADNIIVIDRGQVAERGTHSQLMA 504
Cdd:cd03224  160 SEGL---APKIVEEIFEAIRELRdegvTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLA 221
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
278-488 1.58e-32

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 130.52  E-value: 1.58e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 278 LVEFKDVTFAYPTRPetdVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVnEFQ--HDYLHS 355
Cdd:COG1129    4 LLEMRGISKSFGGVK---ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPV-RFRspRDAQAA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 356 KIALVGQEPVLFA-RTIKENISYGLSDVSMEMVVQAATKANAHDFITTLpkGYDTSVGEKGLQLSGGQKQRVAIARALIR 434
Cdd:COG1129   80 GIAIIHQELNLVPnLSVAENIFLGREPRRGGLIDWRAMRRRARELLARL--GLDIDPDTPVGDLSVAQQQLVEIARALSR 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 961964003 435 QPRVLILDEATSAL-DAESEHivqqaLNSIMQE-----HTVLVIAHRLSTVEK-ADNIIVI 488
Cdd:COG1129  158 DARVLILDEPTASLtEREVER-----LFRIIRRlkaqgVAIIYISHRLDEVFEiADRVTVL 213
ABC_phnC TIGR02315
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ...
 278-502 1.93e-32

phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]


Pssm-ID: 131368 [Multi-domain]  Cd Length: 243  Bit Score: 124.72  E-value: 1.93e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  278 LVEFKDVTFAYPTrpETDVLKGVSFTLRPGEVTALVGPSGSGKSS---CVSLLENfylPQGGQVLLDGKPVNEFQHDYLH 354
Cdd:TIGR02315   1 MLEVENLSKVYPN--GKQALKNINLNINPGEFVAIIGPSGAGKSTllrCINRLVE---PSSGSILLEGTDITKLRGKKLR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  355 S---KIALVGQEPVLFAR-TIKENISYGlsdvsmemvvqaatKANAHDFITTLPKGYDTSVGEKGL-------------- 416
Cdd:TIGR02315  76 KlrrRIGMIFQHYNLIERlTVLENVLHG--------------RLGYKPTWRSLLGRFSEEDKERALsalervgladkayq 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  417 ---QLSGGQKQRVAIARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQEH--TVLVIAHRLSTVEK-ADNIIVIDR 490
Cdd:TIGR02315 142 radQLSGGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDgiTVIINLHQVDLAKKyADRIVGLKA 221

                         250
                  ....*....|..
gi 961964003  491 GQVAERGTHSQL 502
Cdd:TIGR02315 222 GEIVFDGAPSEL 233
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
 296-504 3.84e-32

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: 123.70  E-value: 3.84e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 296 VLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQ-HDYLHSKIALVGQEPVLFAR-TIKE 373
Cdd:cd03219   15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPpHEIARLGIGRTFQIPRLFPElTVLE 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 374 NI--------SYGLSDVSMEMVVQAATKAnAHDFITT--LPKGYDTSVGEkglqLSGGQKQRVAIARALIRQPRVLILDE 443
Cdd:cd03219   95 NVmvaaqartGSGLLLARARREEREARER-AEELLERvgLADLADRPAGE----LSYGQQRRLEIARALATDPKLLLLDE 169

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 961964003 444 ATSAL-DAESEHIVQ--QALNSimQEHTVLVIAHRLSTVEK-ADNIIVIDRGQVAERGTHSQLMA 504
Cdd:cd03219  170 PAAGLnPEETEELAEliRELRE--RGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRN 232
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
 296-521 2.25e-31

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 122.19  E-value: 2.25e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 296 VLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHDYLHSKIALVGQEPVL-FARTIKEN 374
Cdd:PRK13548  17 LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFTVEEV 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 375 ISYGLSDVSMEM-----VVQAA-TKANAHDFittlpkgydtsVGEKGLQLSGGQKQRVAIARALIR------QPRVLILD 442
Cdd:PRK13548  97 VAMGRAPHGLSRaeddaLVAAAlAQVDLAHL-----------AGRDYPQLSGGEQQRVQLARVLAQlwepdgPPRWLLLD 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 443 EATSALDAESEHIVQQALNSIMQEH--TVLVIAHRLS-TVEKADNIIVIDRGQVAERGTHSQLMATGGLycklvqRQVLG 519
Cdd:PRK13548 166 EPTSALDLAHQHHVLRLARQLAHERglAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPAEVLTPETL------RRVYG 239


                 ..
gi 961964003 520 IE 521
Cdd:PRK13548 240 AD 241
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
 279-498 2.60e-31

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 124.14  E-value: 2.60e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 279 VEFKDVTFAYPT-RPETDVLKGVSFTLRPGEVTALVGPSGSGKSS---CVSLLENfylPQGGQVLLDGKPVNE------- 347
Cdd:PRK11153   2 IELKNISKVFPQgGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTlirCINLLER---PTSGRVLVDGQDLTAlsekelr 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 348 ---------FQHDYLHSK------IALvgqePVLFARTIKENIS---------YGLSDvsmemvvqaatKANAHdfittl 403
Cdd:PRK11153  79 karrqigmiFQHFNLLSSrtvfdnVAL----PLELAGTPKAEIKarvtellelVGLSD-----------KADRY------ 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 404 PKgydtsvgekglQLSGGQKQRVAIARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQEH--TVLVIAHRLSTV-E 480
Cdd:PRK11153 138 PA-----------QLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELglTIVLITHEMDVVkR 206

                        250
                 ....*....|....*...
gi 961964003 481 KADNIIVIDRGQVAERGT 498
Cdd:PRK11153 207 ICDRVAVIDAGRLVEQGT 224
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
 276-498 4.47e-31

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 121.78  E-value: 4.47e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 276 TGLVEFKDVTFAYPTrPETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHDYLHS 355
Cdd:PRK13648   5 NSIIVFKNVSFQYQS-DASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 356 KIALVGQEP--VLFARTIKENISYGLSDVSM------EMVVQAATKANAHDFITTLPKGydtsvgekglqLSGGQKQRVA 427
Cdd:PRK13648  84 HIGIVFQNPdnQFVGSIVKYDVAFGLENHAVpydemhRRVSEALKQVDMLERADYEPNA-----------LSGGQKQRVA 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 961964003 428 IARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQEH--TVLVIAHRLSTVEKADNIIVIDRGQVAERGT 498
Cdd:PRK13648 153 IAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGT 225
ABCC_SUR2 cd03288
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...
 296-514 4.49e-31

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: 121.55  E-value: 4.49e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 296 VLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHDYLHSKIALVGQEPVLFARTIKENI 375
Cdd:cd03288   36 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 376 SyGLSDVSMEMVVQAATKANAHDFITTLPKGYDTSVGEKGLQLSGGQKQRVAIARALIRQPRVLILDEATSALDAESEHI 455
Cdd:cd03288  116 D-PECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENI 194

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 456 VQQALNSIMQEHTVLVIAHRLSTVEKADNIIVIDRGQVAERGTHSQLMA-TGGLYCKLVQ 514
Cdd:cd03288  195 LQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAqEDGVFASLVR 254
ABC_6TM_YknV_like cd18545
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ...
 7-254 4.95e-31

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: 122.19  E-value: 4.95e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   7 FTLFFLLSSMAIGVRggvfTLTMARLN----VRLRSRLFRTLMTQEIAFFDENHTGDILSRLSADTTQVSDLISQNVNVF 82
Cdd:cd18545   46 FLALNLVNWVASRLR----IYLMAKVGqrilYDLRQDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINL 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  83 LRSVIKGTGFIIFMFRMSWKLTLVTMMGFPFIALVSKLYGEYYKKLTKEVQTVLAEANKVAEETISGMRTVRSFANESRE 162
Cdd:cd18545  122 IPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVVFLLRRRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDEN 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 163 ANSYYAKLLVMFQLNKKqALAYACYMWSSC--ISELALeVAVLYYGGHLVLTDQLSSGGLISFFIYMLELGECFESIASV 240
Cdd:cd18545  202 EEIFDELNRENRKANMR-AVRLNALFWPLVelISALGT-ALVYWYGGKLVLGGAITVGVLVAFIGYVGRFWQPIRNLSNF 279

                        250
                 ....*....|....
gi 961964003 241 YSGLMQGVGAAEKV 254
Cdd:cd18545  280 YNQLQSAMASAERI 293
cbiO PRK13640
energy-coupling factor transporter ATPase;
279-498 5.87e-31

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 121.83  E-value: 5.87e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 279 VEFKDVTFAYPTRPETdVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQG---GQVLLDGKPVNEFQHDYLHS 355
Cdd:PRK13640   6 VEFKHVSFTYPDSKKP-ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTAKTVWDIRE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 356 KIALVGQEP--VLFARTIKENISYGLSDVSM---EM---VVQAATKANAHDFITTLPKgydtsvgekglQLSGGQKQRVA 427
Cdd:PRK13640  85 KVGIVFQNPdnQFVGATVGDDVAFGLENRAVprpEMikiVRDVLADVGMLDYIDSEPA-----------NLSGGQKQRVA 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 961964003 428 IARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQEH--TVLVIAHRLSTVEKADNIIVIDRGQVAERGT 498
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLLAQGS 226
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
 282-474 8.30e-31

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: 118.90  E-value: 8.30e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 282 KDVTFAYptRPETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQhdyLHSKIALVG 361
Cdd:cd03226    3 ENISFSY--KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKE---RRKSIGYVM 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 362 QEP--VLFARTIKENISYGLSDVS--MEMVVQAATKANAHDFITTLPkgydtsvgekgLQLSGGQKQRVAIARALIRQPR 437
Cdd:cd03226   78 QDVdyQLFTDSVREELLLGLKELDagNEQAETVLKDLDLYALKERHP-----------LSLSGGQKQRLAIAAALLSGKD 146

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 961964003 438 VLILDEATSALDAESEHIVQQALNSIM-QEHTVLVIAH 474
Cdd:cd03226  147 LLIFDEPTSGLDYKNMERVGELIRELAaQGKAVIVITH 184
COG4559 COG4559
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
282-503 8.70e-31

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


Pssm-ID: 443620 [Multi-domain]  Cd Length: 258  Bit Score: 120.61  E-value: 8.70e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 282 KDVTFAYPTRPetdVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHDYLHSKIALVG 361
Cdd:COG4559    5 ENLSVRLGGRT---LLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVLP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 362 QEPVL-FARTIKENISYGLSDVSM------EMVVQAATKANAHDFITTLpkgYdtsvgekgLQLSGGQKQRVAIARALI- 433
Cdd:COG4559   82 QHSSLaFPFTVEEVVALGRAPHGSsaaqdrQIVREALALVGLAHLAGRS---Y--------QTLSGGEQQRVQLARVLAq 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 434 ------RQPRVLILDEATSALD-AeseHivQQALNSIMQEHT-----VLVIAHRLS-TVEKADNIIVIDRGQVAERGTHS 500
Cdd:COG4559  151 lwepvdGGPRWLFLDEPTSALDlA---H--QHAVLRLARQLArrgggVVAVLHDLNlAAQYADRILLLHQGRLVAQGTPE 225


                 ...
gi 961964003 501 QLM 503
Cdd:COG4559  226 EVL 228
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
 279-505 8.75e-31

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: 120.10  E-value: 8.75e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 279 VEFKDVTFAYPTRPEtdVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHDYLHSKIA 358
Cdd:cd03295    1 IEFENVTKRYGGGKK--AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 359 LVGQEPVLFA-RTIKENISYGLsdvSMEMVVQAATKANAHDFITTL---PKGYdtsVGEKGLQLSGGQKQRVAIARALIR 434
Cdd:cd03295   79 YVIQQIGLFPhMTVEENIALVP---KLLKWPKEKIRERADELLALVgldPAEF---ADRYPHELSGGQQQRVGVARALAA 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 961964003 435 QPRVLILDEATSALDAESEHIVQQALNSIMQE--HTVLVIAHRLSTVEK-ADNIIVIDRGQVAERGTHSQLMAT 505
Cdd:cd03295  153 DPPLLLMDEPFGALDPITRDQLQEEFKRLQQElgKTIVFVTHDIDEAFRlADRIAIMKNGEIVQVGTPDEILRS 226
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
 296-494 1.42e-30

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: 117.14  E-value: 1.42e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 296 VLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNefqhdylhskialvgqepvlfARTIKENI 375
Cdd:cd03216   15 ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVS---------------------FASPRDAR 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 376 SYGlsdvsMEMVvqaatkanaHdfittlpkgydtsvgekglQLSGGQKQRVAIARALIRQPRVLILDEATSAL-DAESEH 454
Cdd:cd03216   74 RAG-----IAMV---------Y-------------------QLSVGERQMVEIARALARNARLLILDEPTAALtPAEVER 120

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 961964003 455 ivqqaLNSIM-----QEHTVLVIAHRLSTV-EKADNIIVIDRGQVA 494
Cdd:cd03216  121 -----LFKVIrrlraQGVAVIFISHRLDEVfEIADRVTVLRDGRVV 161
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
 279-497 2.00e-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: 118.06  E-value: 2.00e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 279 VEFKDVTFAYPTRpetDVLKGVSFTLRPGeVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEfQHDYLHSKIA 358
Cdd:cd03264    1 LQLENLTKRYGKK---RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 359 LVGQEPVLFAR-TIKENISY--GLSDVS----MEMVVQAATKANAHDFittlpkgYDTSVGekglQLSGGQKQRVAIARA 431
Cdd:cd03264   76 YLPQEFGVYPNfTVREFLDYiaWLKGIPskevKARVDEVLELVNLGDR-------AKKKIG----SLSGGMRRRVGIAQA 144

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 961964003 432 LIRQPRVLILDEATSALDAESEHIVQQALNSIMQEHTVLVIAHRLSTVEK-ADNIIVIDRGQVAERG 497
Cdd:cd03264  145 LVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
ABC_6TM_Rv0194_D1_like cd18543
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ...
 35-254 2.37e-30

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: 120.28  E-value: 2.37e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  35 RLRSRLFRTLMTQEIAFFDENHTGDILSRLSADTTQVSDLISQNVNVFLRSVIKGTGFIIfMFRMSWKLTLVTMMGFPFI 114
Cdd:cd18543   73 DLRTDLFAHLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLAFGPFLLGNLLTLVVGLVV-MLVLSPPLALVALASLPPL 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 115 ALVSKLYGEYYKKLTKEVQTVLAEANKVAEETISGMRTVRSFANESREANSYYAKLLVMFQLNKKQALAYACYM-WSSCI 193
Cdd:cd18543  152 VLVARRFRRRYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWpLLEAL 231

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 961964003 194 SELALeVAVLYYGGHLVLTDQLSSGGLISFFIYMLELGECFESIASVYSGLMQGVGAAEKV 254
Cdd:cd18543  232 PELGL-AAVLALGGWLVANGSLTLGTLVAFSAYLTMLVWPVRMLGWLLAMAQRARAAAERV 291
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
 296-504 2.49e-30

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 119.08  E-value: 2.49e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 296 VLKGVSFTLRPGEVTALVGPSGSGKSS---CVSLLENfylPQGGQV-----LLDG-KPVNEFQH--DYLHSKIALVGQEP 364
Cdd:PRK11264  18 VLHGIDLEVKPGEVVAIIGPSGSGKTTllrCINLLEQ---PEAGTIrvgdiTIDTaRSLSQQKGliRQLRQHVGFVFQNF 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 365 VLFA-RTIKENISYGLSDVSMEMVVQAATKANAhdfitTLPKgydtsVGEKGLQ------LSGGQKQRVAIARALIRQPR 437
Cdd:PRK11264  95 NLFPhRTVLENIIEGPVIVKGEPKEEATARARE-----LLAK-----VGLAGKEtsyprrLSGGQQQRVAIARALAMRPE 164

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 961964003 438 VLILDEATSALDAEsehIVQQALNSIMQ----EHTVLVIAHRLSTV-EKADNIIVIDRGQVAERGTHSQLMA 504
Cdd:PRK11264 165 VILFDEPTSALDPE---LVGEVLNTIRQlaqeKRTMVIVTHEMSFArDVADRAIFMDQGRIVEQGPAKALFA 233
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
 279-502 2.87e-30

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 119.46  E-value: 2.87e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 279 VEFKDVTFAYptRPETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHDYLHSKIA 358
Cdd:PRK13647   5 IEVEDLHFRY--KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 359 LVGQEP--VLFARTIKENISYG-----LSDVSMEMVVQAATKA-NAHDFITTLPKgydtsvgekglQLSGGQKQRVAIAR 430
Cdd:PRK13647  83 LVFQDPddQVFSSTVWDDVAFGpvnmgLDKDEVERRVEEALKAvRMWDFRDKPPY-----------HLSYGQKKRVAIAG 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 961964003 431 ALIRQPRVLILDEATSALDAESEHIVQQALNSIMQEHTVLVIA-HRLS-TVEKADNIIVIDRGQVAERGTHSQL 502
Cdd:PRK13647 152 VLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDlAAEWADQVIVLKEGRVLAEGDKSLL 225
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
 279-476 3.32e-30

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


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 118.99  E-value: 3.32e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 279 VEFKDVTFAYPTRPetdVLKGVSFTLRPGEVTALVGPSGSGKSscvSLL----------ENFYLpqGGQVLLDGKPVNEF 348
Cdd:COG1117   12 IEVRNLNVYYGDKQ---ALKDINLDIPENKVTALIGPSGCGKS---TLLrclnrmndliPGARV--EGEILLDGEDIYDP 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 349 QHD--YLHSKIALVGQEPVLFARTIKENISYGL-------SDVSMEMVVQAATKANAHDfittlpkgydtSV----GEKG 415
Cdd:COG1117   84 DVDvvELRRRVGMVFQKPNPFPKSIYDNVAYGLrlhgiksKSELDEIVEESLRKAALWD-----------EVkdrlKKSA 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 961964003 416 LQLSGGQKQRVAIARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQEHTVLVIAHRL 476
Cdd:COG1117  153 LGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNM 213
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
 296-498 6.85e-30

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: 117.44  E-value: 6.85e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 296 VLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHDylHSKIALVGQEPVLFAR-TIKEN 374
Cdd:cd03299   14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFPHmTVYKN 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 375 ISYGLSdvsMEMVVQAATKANAHDFITTLpkGYDTSVGEKGLQLSGGQKQRVAIARALIRQPRVLILDEATSALDAESEH 454
Cdd:cd03299   92 IAYGLK---KRKVDKKEIERKVLEIAEML--GIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKE 166

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 961964003 455 IVQQALNSIMQEH--TVLVIAHRLSTVEK-ADNIIVIDRGQVAERGT 498
Cdd:cd03299  167 KLREELKKIRKEFgvTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGK 213
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
 249-504 8.16e-30

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: 123.26  E-value: 8.16e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 249 GAAEKVFEyldrKPKHP-----------ADGTEAPNSCTGLVEFKDVTFAYPTR--------PETDVLKGVSFTLRPGEV 309
Cdd:COG4172  239 GPTAELFA----APQHPytrkllaaeprGDPRPVPPDAPPLLEARDLKVWFPIKrglfrrtvGHVKAVDGVSLTLRRGET 314

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 310 TALVGPSGSGKSS---CVSLLenfyLPQGGQVLLDGKPVNEFQHDYLH---SKIALVGQEPvlFA-----RTIKENISYG 378
Cdd:COG4172  315 LGLVGESGSGKSTlglALLRL----IPSEGEIRFDGQDLDGLSRRALRplrRRMQVVFQDP--FGslsprMTVGQIIAEG 388

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 379 L-------SDVSMEMVVQAATKanahdfittlpkgydtsvgEKGL----------QLSGGQKQRVAIARALIRQPRVLIL 441
Cdd:COG4172  389 LrvhgpglSAAERRARVAEALE-------------------EVGLdpaarhryphEFSGGQRQRIAIARALILEPKLLVL 449

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 442 DEATSALDAesehIVQQA----LNSIMQEH--TVLVIAHRLSTVEK-ADNIIVIDRGQVAERGTHSQLMA 504
Cdd:COG4172  450 DEPTSALDV----SVQAQildlLRDLQREHglAYLFISHDLAVVRAlAHRVMVMKDGKVVEQGPTEQVFD 515
ABC_6TM_exporter_like cd18778
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
 36-254 8.72e-30

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: 118.79  E-value: 8.72e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  36 LRSRLFRTLMTQEIAFFDENHTGDILSRLSADTTQVSDLISQNVNVFLRSVIKGTGFIIFMFRMSWKLTLVTMMGFPFIA 115
Cdd:cd18778   75 LRSDLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLA 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 116 LVSKLYGEYYKKLTKEVQTVLAEANKVAEETISGMRTVRSFANESRE-------ANSYYAKLL-VMFqlnkkqalayacy 187
Cdd:cd18778  155 LGAWLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEakrfealSRRYRKAQLrAMK------------- 221

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 961964003 188 MWS------SCISELALeVAVLYYGGHLVLTDQLSSGGLISFFIYMLELGECFESIASVYSGLMQGVGAAEKV 254
Cdd:cd18778  222 LWAifhplmEFLTSLGT-VLVLGFGGRLVLAGELTIGDLVAFLLYLGLFYEPITSLHGLNEMLQRALAGAERV 293
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
 279-497 1.23e-29

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: 116.20  E-value: 1.23e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 279 VEFKDVTFAYPTRPetdVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHDylHSKIA 358
Cdd:cd03301    1 VELENVTKRFGNVT---ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK--DRDIA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 359 LVGQEPVLFAR-TIKENISYGLSdvsMEMVVQAATKANAHDFITTLpkGYDTSVGEKGLQLSGGQKQRVAIARALIRQPR 437
Cdd:cd03301   76 MVFQNYALYPHmTVYDNIAFGLK---LRKVPKDEIDERVREVAELL--QIEHLLDRKPKQLSGGQRQRVALGRAIVREPK 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 961964003 438 VLILDEATSALDAESEHIVQQALNSIMQEH--TVLVIAHrlSTVEK---ADNIIVIDRGQVAERG 497
Cdd:cd03301  151 VFLMDEPLSNLDAKLRVQMRAELKRLQQRLgtTTIYVTH--DQVEAmtmADRIAVMNDGQIQQIG 213
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
 279-498 1.77e-29

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: 116.18  E-value: 1.77e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 279 VEFKDVTFAYPTRPetdVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVnefqHDYLHSK-- 356
Cdd:cd03300    1 IELENVSKFYGGFV---ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI----TNLPPHKrp 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 357 IALVGQEPVLFAR-TIKENISYGLSdvsMEMVVQAATKANAHDFITTlpkgydtsVGEKGL------QLSGGQKQRVAIA 429
Cdd:cd03300   74 VNTVFQNYALFPHlTVFENIAFGLR---LKKLPKAEIKERVAEALDL--------VQLEGYanrkpsQLSGGQQQRVAIA 142

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 961964003 430 RALIRQPRVLILDEATSALDAESEHIVQQALNSIMQE--HTVLVIAHRLS-TVEKADNIIVIDRGQVAERGT 498
Cdd:cd03300  143 RALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKElgITFVFVTHDQEeALTMSDRIAVMNKGKIQQIGT 214
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
 278-504 2.37e-29

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


Pssm-ID: 443658 [Multi-domain]  Cd Length: 329  Bit Score: 118.30  E-value: 2.37e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 278 LVEFKDVTFAYPTRP-----ETDVLK---GVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQ 349
Cdd:COG4608    7 LLEVRDLKKHFPVRGglfgrTVGVVKavdGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLS 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 350 HDYL---HSKIALVGQEPvlFA-----RTIKENISYGLsdVSMEMVVQAATKANAHDFITTLpkgydtsvgekGL----- 416
Cdd:COG4608   87 GRELrplRRRMQMVFQDP--YAslnprMTVGDIIAEPL--RIHGLASKAERRERVAELLELV-----------GLrpeha 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 417 -----QLSGGQKQRVAIARALIRQPRVLILDEATSALDAeSehiVQ-QALNSIM---QEH--TVLVIAHRLSTVEK-ADN 484
Cdd:COG4608  152 dryphEFSGGQRQRIGIARALALNPKLIVCDEPVSALDV-S---IQaQVLNLLEdlqDELglTYLFISHDLSVVRHiSDR 227

                        250       260
                 ....*....|....*....|
gi 961964003 485 IIVIDRGQVAERGTHSQLMA 504
Cdd:COG4608  228 VAVMYLGKIVEIAPRDELYA 247
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
 279-493 2.64e-29

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: 115.20  E-value: 2.64e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 279 VEFKDVTFAYPtrPETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHD---YLHS 355
Cdd:cd03292    1 IEFINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRaipYLRR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 356 KIALVGQE-PVLFARTIKENISYGL--SDVS----MEMVVQAATKANAHDFITTLPKgydtsvgekglQLSGGQKQRVAI 428
Cdd:cd03292   79 KIGVVFQDfRLLPDRNVYENVAFALevTGVPpreiRKRVPAALELVGLSHKHRALPA-----------ELSGGEQQRVAI 147

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 961964003 429 ARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQEHTVLVIA-HRLSTVEKADN-IIVIDRGQV 493
Cdd:cd03292  148 ARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVAtHAKELVDTTRHrVIALERGKL 214
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...
 296-498 3.37e-29

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: 115.91  E-value: 3.37e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 296 VLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQ-HdylhsKIALVG-----QEPVLFAR 369
Cdd:COG0411   19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPpH-----RIARLGiartfQNPRLFPE 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 370 -TIKENisyglsdvsMEMVVQAATKANAHDFITTLPKGY-----------------------DTSVGEkglqLSGGQKQR 425
Cdd:COG0411   94 lTVLEN---------VLVAAHARLGRGLLAALLRLPRARreereareraeellervgladraDEPAGN----LSYGQQRR 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 961964003 426 VAIARALIRQPRVLILDEATSAL-DAESEHIVqQALNSIMQEH--TVLVIAHRLSTVEK-ADNIIVIDRGQVAERGT 498
Cdd:COG0411  161 LEIARALATEPKLLLLDEPAAGLnPEETEELA-ELIRRLRDERgiTILLIEHDMDLVMGlADRIVVLDFGRVIAEGT 236
TauB COG4525
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
280-496 5.96e-29

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


Pssm-ID: 443596 [Multi-domain]  Cd Length: 262  Bit Score: 115.34  E-value: 5.96e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 280 EFKDVTFAYP-TRPETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNE--------FQH 350
Cdd:COG4525    5 TVRHVSVRYPgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGpgadrgvvFQK 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 351 DylhskiALVgqePVLFARtikENISYGLSdvsMEMVVQAATKANAHDFITTlpkgydtsVGEKGL------QLSGGQKQ 424
Cdd:COG4525   85 D------ALL---PWLNVL---DNVAFGLR---LRGVPKAERRARAEELLAL--------VGLADFarrriwQLSGGMRQ 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 425 RVAIARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQE--HTVLVIAHrlsTVEKA----DNIIVIDR--GQVAER 496
Cdd:COG4525  142 RVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRtgKGVFLITH---SVEEAlflaTRLVVMSPgpGRIVER 218
PTZ00243 PTZ00243
ABC transporter; Provisional
 6-502 7.08e-29

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 122.19  E-value: 7.08e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003    6 PFTLFFLLSSMAIGVRggvftltmarlnvRLRSRLFRTLMTQEIAFFDENHTGDILSRLSADTtqvsDLISQNVNVFLRS 85
Cdd:PTZ00243 1016 PLRFFLSYEAMRRGSR-------------NMHRDLLRSVSRGTMSFFDTTPLGRILNRFSRDI----DILDNTLPMSYLY 1078

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   86 VIKgtgfiiFMFRMSWKLtLVTMMGFPF--IALVSKLYGEY-----YKKLTKEVQTVLAEANK----VAEETISGMRTVR 154
Cdd:PTZ00243 1079 LLQ------CLFSICSSI-LVTSASQPFvlVALVPCGYLYYrlmqfYNSANREIRRIKSVAKSpvftLLEEALQGSATIT 1151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  155 SFANESreansyyaklLVMFQLNKKQALAYAC-YM------W-------SSCIseLALEVAVLYYGGHLVLTDQLSSGgL 220
Cdd:PTZ00243 1152 AYGKAH----------LVMQEALRRLDVVYSCsYLenvanrWlgvrvefLSNI--VVTVIALIGVIGTMLRATSQEIG-L 1218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  221 ISFFIYML-----ELGECFESIASVYSGlMQGVgaaEKVFEYLDRKPKH------------------PADGTEA----PN 273
Cdd:PTZ00243 1219 VSLSLTMAmqttaTLNWLVRQVATVEAD-MNSV---ERLLYYTDEVPHEdmpeldeevdalerrtgmAADVTGTvviePA 1294

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  274 SCT---------GLVEFKDVTFAY----PTrpetdVLKGVSFTLRPGEVTALVGPSGSGKSScvsLLENFYLPQ---GGQ 337
Cdd:PTZ00243 1295 SPTsaaphpvqaGSLVFEGVQMRYreglPL-----VLRGVSFRIAPREKVGIVGRTGSGKST---LLLTFMRMVevcGGE 1366

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  338 VLLDGKPVNEFQHDYLHSKIALVGQEPVLFARTIKENISYGLSDVSMEmVVQAATKANAHDFITTLPKGYDTSVGEKGLQ 417
Cdd:PTZ00243 1367 IRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVDPFLEASSAE-VWAALELVGLRERVASESEGIDSRVLEGGSN 1445

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  418 LSGGQKQRVAIARALIRQPRVLIL-DEATSALDAESEHIVQQALNSIMQEHTVLVIAHRLSTVEKADNIIVIDRGQVAER 496
Cdd:PTZ00243 1446 YSVGQRQLMCMARALLKKGSGFILmDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEM 1525


                  ....*.
gi 961964003  497 GTHSQL 502
Cdd:PTZ00243 1526 GSPREL 1531
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
 279-498 8.76e-29

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: 114.36  E-value: 8.76e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 279 VEFKDVTFAYPTRPetdVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNefQHDYLHSKIA 358
Cdd:cd03296    3 IEVRNVSKRFGDFV---ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDAT--DVPVQERNVG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 359 LVGQEPVLFAR-TIKENISYGLS-DVSMEMVVQAATKANAHDFI-----TTLPKGYDTsvgekglQLSGGQKQRVAIARA 431
Cdd:cd03296   78 FVFQHYALFRHmTVFDNVAFGLRvKPRSERPPEAEIRAKVHELLklvqlDWLADRYPA-------QLSGGQRQRVALARA 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 961964003 432 LIRQPRVLILDEATSALDAEsehiVQQALNSIMQE-H------TVLVIAHRLSTVEKADNIIVIDRGQVAERGT 498
Cdd:cd03296  151 LAVEPKVLLLDEPFGALDAK----VRKELRRWLRRlHdelhvtTVFVTHDQEEALEVADRVVVMNKGRIEQVGT 220
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
 282-493 9.37e-29

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 114.77  E-value: 9.37e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 282 KDVTFAYPTRpetDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHDylhskIALVG 361
Cdd:PRK11247  16 NAVSKRYGER---TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEARED-----TRLMF 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 362 QEPVLFA-RTIKENISYGLSdvsmemvvqAATKANAHDFITTLpkGYDTSVGEKGLQLSGGQKQRVAIARALIRQPRVLI 440
Cdd:PRK11247  88 QDARLLPwKKVIDNVGLGLK---------GQWRDAALQALAAV--GLADRANEWPAALSGGQKQRVALARALIHRPGLLL 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 961964003 441 LDEATSALDAESEHIVQQALNSIMQEH--TVLVIAHRLS-TVEKADNIIVIDRGQV 493
Cdd:PRK11247 157 LDEPLGALDALTRIEMQDLIESLWQQHgfTVLLVTHDVSeAVAMADRVLLIEEGKI 212
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
301-504 1.11e-28

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 113.91  E-value: 1.11e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 301 SFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKpvnefqhDYLHSKIAlvgQEPV--------LFAR-TI 371
Cdd:PRK10771  19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQ-------DHTTTPPS---RRPVsmlfqennLFSHlTV 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 372 KENISYG------LSDVSMEMVVQAATKANAHDFITTLPKgydtsvgekglQLSGGQKQRVAIARALIRQPRVLILDEAT 445
Cdd:PRK10771  89 AQNIGLGlnpglkLNAAQREKLHAIARQMGIEDLLARLPG-----------QLSGGQRQRVALARCLVREQPILLLDEPF 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 961964003 446 SALDAESEHIVQQALNSIMQEH--TVLVIAHRLSTVEK-ADNIIVIDRGQVAERGTHSQLMA 504
Cdd:PRK10771 158 SALDPALRQEMLTLVSQVCQERqlTLLMVSHSLEDAARiAPRSLVVADGRIAWDGPTDELLS 219
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
 300-508 1.12e-28

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: 117.14  E-value: 1.12e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  300 VSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHDYLHS----KIALVGQEPVLFAR-TIKEN 374
Cdd:TIGR02142  16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPpekrRIGYVFQEARLFPHlSVRGN 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  375 ISYGLSDVsmemvvQAATKANAHDFITTLpKGYDTSVGEKGLQLSGGQKQRVAIARALIRQPRVLILDEATSALDAESEH 454
Cdd:TIGR02142  96 LRYGMKRA------RPSERRISFERVIEL-LGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKY 168

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 961964003  455 IVQQALNSIMQEHT--VLVIAHRLSTVEK-ADNIIVIDRGQVAERGTHSQLMATGGL 508
Cdd:TIGR02142 169 EILPYLERLHAEFGipILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWASPDL 225
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
 300-504 2.15e-28

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: 116.35  E-value: 2.15e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 300 VSFTLRPGEVTALVGPSGSGKSS---CVSLLENfylPQGGQVLLDGKPVneFQHDYLHS------KIALVGQEPVLFA-R 369
Cdd:COG4148   18 VDFTLPGRGVTALFGPSGSGKTTllrAIAGLER---PDSGRIRLGGEVL--QDSARGIFlpphrrRIGYVFQEARLFPhL 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 370 TIKENISYGLSDVSmemvvQAATKANAHDFITTLpkgydtsvgekGL---------QLSGGQKQRVAIARALIRQPRVLI 440
Cdd:COG4148   93 SVRGNLLYGRKRAP-----RAERRISFDEVVELL-----------GIghlldrrpaTLSGGERQRVAIGRALLSSPRLLL 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 961964003 441 LDEATSALDAESEHIVQQALNSIMQEHT--VLVIAHRLSTVEK-ADNIIVIDRGQVAERGTHSQLMA 504
Cdd:COG4148  157 MDEPLAALDLARKAEILPYLERLRDELDipILYVSHSLDEVARlADHVVLLEQGRVVASGPLAEVLS 223
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
 278-486 2.68e-28

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 112.50  E-value: 2.68e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 278 LVEFKDVTFAYPTRPetdVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHDYLHSKI 357
Cdd:PRK10247   7 LLQLQNVGYLAGDAK---ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 358 ALVGQEPVLFARTIKENI--SYGLSDVSMEMVVQAATKANAHDFITTLPKGYDtsvgekglQLSGGQKQRVAIARALIRQ 435
Cdd:PRK10247  84 SYCAQTPTLFGDTVYDNLifPWQIRNQQPDPAIFLDDLERFALPDTILTKNIA--------ELSGGEKQRISLIRNLQFM 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 961964003 436 PRVLILDEATSALDAESEHIVQQALNSIMQEHTVLVI--AHRLSTVEKADNII 486
Cdd:PRK10247 156 PKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLwvTHDKDEINHADKVI 208
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
 278-493 3.25e-28

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 118.21  E-value: 3.25e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 278 LVEFKDVTFAYPtrpetDV--LKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVnEFQ--HDYL 353
Cdd:COG3845    5 ALELRGITKRFG-----GVvaNDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPV-RIRspRDAI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 354 HSKIALVGQEPVLFAR-TIKENISYGLSDVSMEMVvqaaTKANAHDFITTLPKGY------DTSVGekglQLSGGQKQRV 426
Cdd:COG3845   79 ALGIGMVHQHFMLVPNlTVAENIVLGLEPTKGGRL----DRKAARARIRELSERYgldvdpDAKVE----DLSVGEQQRV 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 961964003 427 AIARALIRQPRVLILDEATSAL-DAESEHivqqaLNSIMQE-----HTVLVIAHRLSTV-EKADNIIVIDRGQV 493
Cdd:COG3845  151 EILKALYRGARILILDEPTAVLtPQEADE-----LFEILRRlaaegKSIIFITHKLREVmAIADRVTVLRRGKV 219
ABC_6TM_exporter_like cd18564
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
 6-227 3.96e-28

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: 114.53  E-value: 3.96e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   6 PFTLFFLLSSM--AIGVRGGVF----TLTMA----RLNVRLRSRLFRTLMTQEIAFFDENHTGDILSRLSADTTQVSDLI 75
Cdd:cd18564   49 PLALLLLAAAAlvGIALLRGLAsyagTYLTAlvgqRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLL 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  76 SQNVNVFLRSVIKGTGFIIFMFRMSWKLTLVTMMGFPFIALVSKLYGEYYKKLTKEVQTVLAEANKVAEETISGMRTVRS 155
Cdd:cd18564  129 VSGVLPLLTNLLTLVGMLGVMFWLDWQLALIALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQA 208

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 961964003 156 FANESREANSYYAKLLVMFQLNKKQALAYACYMWSSCISELALEVAVLYYGGHLVLTDQLSSGGLISFFIYM 227
Cdd:cd18564  209 FGREEHEERRFARENRKSLRAGLRAARLQALLSPVVDVLVAVGTALVLWFGAWLVLAGRLTPGDLLVFLAYL 280
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
 256-496 3.97e-28

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 118.37  E-value: 3.97e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 256 EYLDRKPKHPADGTEAPNSCTGLVEFKDVTFAYPT-RPetdVLKGVSFTLRPGEVTALVGPSGSGKSS---CVSLLENFY 331
Cdd:COG4178  340 EALEAADALPEAASRIETSEDGALALEDLTLRTPDgRP---LLEDLSLSLKPGERLLITGPSGSGKSTllrAIAGLWPYG 416

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 332 -----LPQGGQVLLdgkpvnefqhdylhskialVGQEPVLFARTIKENISY--GLSDVSMEMVVQAATKANAHDFITTLp 404
Cdd:COG4178  417 sgriaRPAGARVLF-------------------LPQRPYLPLGTLREALLYpaTAEAFSDAELREALEAVGLGHLAERL- 476

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 405 kgyDTsVGEKGLQLSGGQKQRVAIARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQEHTVLVIAHRLSTVEKADN 484
Cdd:COG4178  477 ---DE-EADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDR 552

                        250
                 ....*....|..
gi 961964003 485 IIVIDRGQVAER 496
Cdd:COG4178  553 VLELTGDGSWQL 564
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
 300-505 4.69e-28

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: 113.12  E-value: 4.69e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 300 VSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHDYLHS----KIALVGQEPVLFA-RTIKEN 374
Cdd:cd03294   43 VSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkKISMVFQSFALLPhRTVLEN 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 375 ISYGLS--DVSMEMVVQAATKA----NAHDFITTLPKgydtsvgekglQLSGGQKQRVAIARALIRQPRVLILDEATSAL 448
Cdd:cd03294  123 VAFGLEvqGVPRAEREERAAEAlelvGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMDEAFSAL 191

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 449 DAESEHIVQQALNSIMQEH--TVLVIAHRLS-TVEKADNIIVIDRGQVAERGTHSQLMAT 505
Cdd:cd03294  192 DPLIRREMQDELLRLQAELqkTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILTN 251
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
 278-504 7.09e-28

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: 117.48  E-value: 7.09e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 278 LVEFKD--VTFAYPTRpETDVLKGVSFTLRPGEVTALVGPSGSGKS----SCVSLLENFYLPQGGQVLLDGKpvnefqhD 351
Cdd:COG4172    6 LLSVEDlsVAFGQGGG-TVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQ-------D 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 352 YLH-----------SKIALVGQEPV-----LFarTIKENISYGLsdvsmeMVVQAATKANAHDFITTLPkgydTSVG--- 412
Cdd:COG4172   78 LLGlserelrrirgNRIAMIFQEPMtslnpLH--TIGKQIAEVL------RLHRGLSGAAARARALELL----ERVGipd 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 413 -EKGL-----QLSGGQKQRVAIARALIRQPRVLILDEATSALDAesehIVQ----QALNSIMQEH--TVLVIAHRLSTVE 480
Cdd:COG4172  146 pERRLdayphQLSGGQRQRVMIAMALANEPDLLIADEPTTALDV----TVQaqilDLLKDLQRELgmALLLITHDLGVVR 221

                        250       260
                 ....*....|....*....|....*
gi 961964003 481 K-ADNIIVIDRGQVAERGTHSQLMA 504
Cdd:COG4172  222 RfADRVAVMRQGEIVEQGPTAELFA 246
cbiO PRK13642
energy-coupling factor transporter ATPase;
278-505 8.20e-28

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 112.88  E-value: 8.20e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 278 LVEFKDVTFAYPTRPETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHDYLHSKI 357
Cdd:PRK13642   4 ILEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 358 ALVGQEP--VLFARTIKENISYGLSDVSM---EM---VVQAATKANAHDFITTLPKgydtsvgekglQLSGGQKQRVAIA 429
Cdd:PRK13642  84 GMVFQNPdnQFVGATVEDDVAFGMENQGIpreEMikrVDEALLAVNMLDFKTREPA-----------RLSGGQKQRVAVA 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 961964003 430 RALIRQPRVLILDEATSALDAESEHIVQQALNSIMQEH--TVLVIAHRLSTVEKADNIIVIDRGQVAERGTHSQLMAT 505
Cdd:PRK13642 153 GIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFAT 230
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
 296-497 1.48e-27

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: 110.15  E-value: 1.48e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 296 VLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHDYLhSKIALVGQEPVLFAR-TIKEN 374
Cdd:cd03266   20 AVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEAR-RRLGFVSDSTGLYDRlTAREN 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 375 ISY--GLSDVSmemvvQAATKANAHDFITTLpkGYDTSVGEKGLQLSGGQKQRVAIARALIRQPRVLILDEATSALDAES 452
Cdd:cd03266   99 LEYfaGLYGLK-----GDELTARLEELADRL--GMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMA 171

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 961964003 453 EHIVQQALNSIMQE-HTVLVIAHRLSTVEK-ADNIIVIDRGQVAERG 497
Cdd:cd03266  172 TRALREFIRQLRALgKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
 278-498 1.95e-27

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 111.71  E-value: 1.95e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 278 LVEFKDVTFAYPTrpETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHDYL--HS 355
Cdd:PRK13639   1 ILETRDLKYSYPD--GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLevRK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 356 KIALVGQEP--VLFARTIKENISYG-----LSDVSMEMVVQAATKAnahdfittlpkgydtsVGEKGLQ------LSGGQ 422
Cdd:PRK13639  79 TVGIVFQNPddQLFAPTVEEDVAFGplnlgLSKEEVEKRVKEALKA----------------VGMEGFEnkpphhLSGGQ 142

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 961964003 423 KQRVAIARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQEHTVLVIA-HRLSTVEK-ADNIIVIDRGQVAERGT 498
Cdd:PRK13639 143 KKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIIStHDVDLVPVyADKVYVMSDGKIIKEGT 220
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
288-496 2.87e-27

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 110.56  E-value: 2.87e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 288 YPTRPetdVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNE--------FQHDYLhskial 359
Cdd:PRK11248  11 YGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGpgaergvvFQNEGL------ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 360 vgqepvLFARTIKENISYGLS----------DVSMEMVVQAATKANAHDFIttlpkgydtsvgekgLQLSGGQKQRVAIA 429
Cdd:PRK11248  82 ------LPWRNVQDNVAFGLQlagvekmqrlEIAHQMLKKVGLEGAEKRYI---------------WQLSGGQRQRVGIA 140

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 961964003 430 RALIRQPRVLILDEATSALDAESEHIVQQALNSIMQE--HTVLVIAHRL-STVEKADNIIVI--DRGQVAER 496
Cdd:PRK11248 141 RALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQEtgKQVLLITHDIeEAVFMATELVLLspGPGRVVER 212
ABC_6TM_YwjA_like cd18549
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ...
 30-226 3.25e-27

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: 111.39  E-value: 3.25e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  30 ARLNVRLRSRLFRTLMTQEIAFFDENHTGDILSRLSADTTQVSDLISQNVNVFLRSVIKGTGFIIFMFRMSWKLTLVTMM 109
Cdd:cd18549   71 ARIETDMRRDLFEHLQKLSFSFFDNNKTGQLMSRITNDLFDISELAHHGPEDLFISIITIIGSFIILLTINVPLTLIVFA 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 110 GFPFIALVSKLYGEYYKKLTKEVQTVLAEANKVAEETISGMRTVRSFANESREANSyYAKLLVMFQLNKKQALAY-ACYM 188
Cdd:cd18549  151 LLPLMIIFTIYFNKKMKKAFRRVREKIGEINAQLEDSLSGIRVVKAFANEEYEIEK-FDEGNDRFLESKKKAYKAmAYFF 229

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 961964003 189 WSSCISELALEVAVLYYGGHLVLTDQLSSGGLISFFIY 226
Cdd:cd18549  230 SGMNFFTNLLNLVVLVAGGYFIIKGEITLGDLVAFLLY 267
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
 297-497 6.81e-27

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: 108.71  E-value: 6.81e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  297 LKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHDYLhskiaLVGQEPVLFA-RTIKENI 375
Cdd:TIGR01184   1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPwLTVRENI 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  376 SYGLSDVSMEM-VVQAATKANAHDFITTLPKGYDTSVGekglQLSGGQKQRVAIARALIRQPRVLILDEATSALDAESEH 454
Cdd:TIGR01184  76 ALAVDRVLPDLsKSERRAIVEEHIALVGLTEAADKRPG----QLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 961964003  455 IVQQALNSIMQEH--TVLVIAHRL-STVEKADNIIVIDRGQVAERG 497
Cdd:TIGR01184 152 NLQEELMQIWEEHrvTVLMVTHDVdEALLLSDRVVMLTNGPAANIG 197
cbiO PRK13637
energy-coupling factor transporter ATPase;
279-498 8.95e-27

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 110.14  E-value: 8.95e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 279 VEFKDVTFAY-PTRP-ETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDG-----KPVNEfqhD 351
Cdd:PRK13637   3 IKIENLTHIYmEGTPfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdKKVKL---S 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 352 YLHSKIALVGQEP--VLFARTIKENISYG-----LSDVSMEMVVQAATKANAHDfittlpkgYDTSVGEKGLQLSGGQKQ 424
Cdd:PRK13637  80 DIRKKVGLVFQYPeyQLFEETIEKDIAFGpinlgLSEEEIENRVKRAMNIVGLD--------YEDYKDKSPFELSGGQKR 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 425 RVAIARALIRQPRVLILDEATSALDAESEhivQQALNSIMQEH-----TVLVIAHRLSTVEK-ADNIIVIDRGQVAERGT 498
Cdd:PRK13637 152 RVAIAGVVAMEPKILILDEPTAGLDPKGR---DEILNKIKELHkeynmTIILVSHSMEDVAKlADRIIVMNKGKCELQGT 228
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
 279-502 1.38e-26

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: 107.59  E-value: 1.38e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 279 VEFKDVTFAYPTRPETdVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEfQHDYLHSKIA 358
Cdd:cd03263    1 LQIRNLTKTYKKGTKP-AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 359 LVGQEPVLFAR-TIKENISY-----GLSDVSMEMVVQAATKanahdfITTLPKGYDTSVGekglQLSGGQKQRVAIARAL 432
Cdd:cd03263   79 YCPQFDALFDElTVREHLRFyarlkGLPKSEIKEEVELLLR------VLGLTDKANKRAR----TLSGGMKRKLSLAIAL 148

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 961964003 433 IRQPRVLILDEATSALDAESEHIVQQALNSIMQEHTVLVIAHRLSTVEK-ADNIIVIDRGQVAERGTHSQL 502
Cdd:cd03263  149 IGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
ABC_6TM_Rv0194_D2_like cd18546
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ...
 8-254 1.53e-26

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: 109.50  E-value: 1.53e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   8 TLFFLLSSMAIGVRGGVFTLTMARLNVR----LRSRLFRTLMTQEIAFFDENHTGDILSRLSADTTQVSDLISQNVNVFL 83
Cdd:cd18546   42 AAAYLAVVLAGWVAQRAQTRLTGRTGERllydLRLRVFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLV 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  84 RSVIKGTGFIIFMFRMSWKLTLVTMMGFPFIALVSKLYGEYYKKLTKEVQTVLAEANKVAEETISGMRTVRSFANESREA 163
Cdd:cd18546  122 VSLLTLVGIAVVLLVLDPRLALVALAALPPLALATRWFRRRSSRAYRRARERIAAVNADLQETLAGIRVVQAFRRERRNA 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 164 NSYYAKLLVMFQLNKKQALAYACYM-WSSCISELALeVAVLYYGGHLVLTDQLSSGGLISFFIYMLELGECFESIASVYS 242
Cdd:cd18546  202 ERFAELSDDYRDARLRAQRLVAIYFpGVELLGNLAT-AAVLLVGAWRVAAGTLTVGVLVAFLLYLRRFFAPIQQLSQVFD 280

                        250
                 ....*....|..
gi 961964003 243 GLMQGVGAAEKV 254
Cdd:cd18546  281 SYQQARAALEKI 292
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
 258-513 3.15e-26

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: 114.27  E-value: 3.15e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   258 LDRKPKHPADGteapNSCTglveFKDVTFAYpTRPETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQ 337
Cdd:TIGR00957  624 IERRTIKPGEG----NSIT----VHNATFTW-ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGH 694

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   338 VLLDGKpvnefqhdylhskIALVGQEPVLFARTIKENISYG--LSDVSMEMVVQAAtkANAHDfITTLPKGYDTSVGEKG 415
Cdd:TIGR00957  695 VHMKGS-------------VAYVPQQAWIQNDSLRENILFGkaLNEKYYQQVLEAC--ALLPD-LEILPSGDRTEIGEKG 758

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   416 LQLSGGQKQRVAIARALIRQPRVLILDEATSALDAE-SEHIVQQALN--SIMQEHTVLVIAHRLSTVEKADNIIVIDRGQ 492
Cdd:TIGR00957  759 VNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHvGKHIFEHVIGpeGVLKNKTRILVTHGISYLPQVDVIIVMSGGK 838

                          250       260
                   ....*....|....*....|.
gi 961964003   493 VAERGTHSQLMATGGLYCKLV 513
Cdd:TIGR00957  839 ISEMGSYQELLQRDGAFAEFL 859
urea_trans_UrtE TIGR03410
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ...
 280-502 3.16e-26

urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 274567 [Multi-domain]  Cd Length: 230  Bit Score: 106.84  E-value: 3.16e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  280 EFKDVTFAYPtrpETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQ-HDYLHSKIA 358
Cdd:TIGR03410   2 EVSNLNVYYG---QSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPpHERARAGIA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  359 LVGQEPVLFAR-TIKENISYGLSdvsmemvVQAATKANAHDFITTLPKGYDTSVGEKGLQLSGGQKQRVAIARALIRQPR 437
Cdd:TIGR03410  79 YVPQGREIFPRlTVEENLLTGLA-------ALPRRSRKIPDEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPK 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 961964003  438 VLILDEATsaldaesEHI-------VQQALNSIMQEH--TVLVIAHRLS-TVEKADNIIVIDRGQVAERGTHSQL 502
Cdd:TIGR03410 152 LLLLDEPT-------EGIqpsiikdIGRVIRRLRAEGgmAILLVEQYLDfARELADRYYVMERGRVVASGAGDEL 219
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 296-507 4.89e-26

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


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 108.27  E-value: 4.89e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 296 VLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNefqhdylHSKIALVG---QEPVLFAR-TI 371
Cdd:COG4152   16 AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD-------PEDRRRIGylpEERGLYPKmKV 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 372 KENISY-----GLSdvsmemvvQAATKANAHDFITT--LPKGYDTSVGEkglqLSGGQKQRVAIARALIRQPRVLILDEA 444
Cdd:COG4152   89 GEQLVYlarlkGLS--------KAEAKRRADEWLERlgLGDRANKKVEE----LSKGNQQKVQLIAALLHDPELLILDEP 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 961964003 445 TSALDAESEHIVQQALNSIMQE-HTVLVIAHRLSTVEK-ADNIIVIDRGQVAERGTHSQLMATGG 507
Cdd:COG4152  157 FSGLDPVNVELLKDVIRELAAKgTTVIFSSHQMELVEElCDRIVIINKGRKVLSGSVDEIRRQFG 221
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
 278-504 6.45e-26

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: 106.22  E-value: 6.45e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 278 LVEFKDVTFAYPtrpETDVLKGVSFTLRPGEVTALVGPSGSGKSS---CVS-LLEnfylPQGGQVLLDGKPVNEFQ-HDY 352
Cdd:COG0410    3 MLEVENLHAGYG---GIHVLHGVSLEVEEGEIVALLGRNGAGKTTllkAISgLLP----PRSGSIRFDGEDITGLPpHRI 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 353 LHSKIALVGQEPVLFAR-TIKENISYGlsdvsmemvvqAATKANAHDFITTLPKGYDT--SVGE----KGLQLSGGQKQR 425
Cdd:COG0410   76 ARLGIGYVPEGRRIFPSlTVEENLLLG-----------AYARRDRAEVRADLERVYELfpRLKErrrqRAGTLSGGEQQM 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 426 VAIARALIRQPRVLILDEATSALdaeSEHIVQQ---ALNSIMQE-HTVLVI---AHRLSTVekADNIIVIDRGQVAERGT 498
Cdd:COG0410  145 LAIGRALMSRPKLLLLDEPSLGL---APLIVEEifeIIRRLNREgVTILLVeqnARFALEI--ADRAYVLERGRIVLEGT 219


                 ....*.
gi 961964003 499 HSQLMA 504
Cdd:COG0410  220 AAELLA 225
ABC_6TM_exporter_like cd18550
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
 17-230 6.74e-26

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: 107.57  E-value: 6.74e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  17 AIGVRGGVFTLTMARLNVR--------LRSRLFRTLMTQEIAFFDENHTGDILSRLSADTTQVSDLISQNVNVFLRSVIK 88
Cdd:cd18550   47 AVAVASALLGVVQTYLSARigqgvmydLRVQLYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVT 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  89 GTGFIIFMFRMSWKLTLVTMMGFPFIALVSKLYGEYYKKLTKEVQTVLAEANKVAEET--ISGMRTVRSFANESREANSY 166
Cdd:cd18550  127 LVATLVAMLALDWRLALLSLVLLPLFVLPTRRVGRRRRKLTREQQEKLAELNSIMQETlsVSGALLVKLFGREDDEAARF 206

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 961964003 167 YAKLLVMFQLNKKQALAYACYMWSSCISELALEVAVLYYGGHLVLTDQLSSGGLISFFIYMLEL 230
Cdd:cd18550  207 ARRSRELRDLGVRQALAGRWFFAALGLFTAIGPALVYWVGGLLVIGGGLTIGTLVAFTALLGRL 270
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
269-498 6.79e-26

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 109.27  E-value: 6.79e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 269 TEAPNSCTGLVEFKDVTFAYPTrpeTDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEF 348
Cdd:PRK09452   5 NKQPSSLSPLVELRGISKSFDG---KEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 349 --QHDYLHSkialVGQEPVLFAR-TIKENISYGLSdvsMEMVVQAATKANAHDFITTLPkgYDTSVGEKGLQLSGGQKQR 425
Cdd:PRK09452  82 paENRHVNT----VFQSYALFPHmTVFENVAFGLR---MQKTPAAEITPRVMEALRMVQ--LEEFAQRKPHQLSGGQQQR 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 961964003 426 VAIARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQEH--TVLVIAHrlsTVEKA----DNIIVIDRGQVAERGT 498
Cdd:PRK09452 153 VAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLgiTFVFVTH---DQEEAltmsDRIVVMRDGRIEQDGT 228
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
 278-504 9.15e-26

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 107.24  E-value: 9.15e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 278 LVEFKDVTFAYPTrpETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVnefqhDY----- 352
Cdd:PRK13636   5 ILKVEELNYNYSD--GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-----DYsrkgl 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 353 --LHSKIALVGQEP--VLFARTIKENISYGLSDVSM--EMVVQAATKANAHDFITTLpKGYDTSVgekglqLSGGQKQRV 426
Cdd:PRK13636  78 mkLRESVGMVFQDPdnQLFSASVYQDVSFGAVNLKLpeDEVRKRVDNALKRTGIEHL-KDKPTHC------LSFGQKKRV 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 427 AIARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQEH--TVLVIAHRLSTVE-KADNIIVIDRGQVAERGTHSQLM 503
Cdd:PRK13636 151 AIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELglTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVF 230


                 .
gi 961964003 504 A 504
Cdd:PRK13636 231 A 231
SufC COG0396
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ...
 293-515 1.08e-25

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


Pssm-ID: 440165 [Multi-domain]  Cd Length: 245  Bit Score: 105.92  E-value: 1.08e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 293 ETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENF--YLPQGGQVLLDGK-----PVNE---------FQH------ 350
Cdd:COG0396   12 GKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEdilelSPDEraragiflaFQYpveipg 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 351 ----DYLHSKIALVGQEPV---LFARTIKENisygLSDVSMemvvqaatkanAHDFIttlpkgyDTSVGEKglqLSGGQK 423
Cdd:COG0396   92 vsvsNFLRTALNARRGEELsarEFLKLLKEK----MKELGL-----------DEDFL-------DRYVNEG---FSGGEK 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 424 QRVAIARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQEHT-VLVIAH--RLSTVEKADNIIVIDRGQVAERGTHS 500
Cdd:COG0396  147 KRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRgILIITHyqRILDYIKPDFVHVLVDGRIVKSGGKE 226

                        250
                 ....*....|....*...
gi 961964003 501 ---QLMATGglYCKLVQR 515
Cdd:COG0396  227 lalELEEEG--YDWLKEE 242
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
293-528 1.12e-25

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 105.87  E-value: 1.12e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 293 ETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHDYLHSKIALVGQEPVL-FARTI 371
Cdd:PRK11231  14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTpEGITV 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 372 KENISYG----------LSDVSMEMVVQAATKANahdfITTLPkgyDTSVGEkglqLSGGQKQRVAIARALIRQPRVLIL 441
Cdd:PRK11231  94 RELVAYGrspwlslwgrLSAEDNARVNQAMEQTR----INHLA---DRRLTD----LSGGQRQRAFLAMVLAQDTPVVLL 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 442 DEATSALDaesehIVQQA-LNSIMQE-----HTVLVIAHRLSTVEK-ADNIIVIDRGQVAERGTHSQLMATGGLycklvq 514
Cdd:PRK11231 163 DEPTTYLD-----INHQVeLMRLMRElntqgKTVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPEEVMTPGLL------ 231

                        250
                 ....*....|....
gi 961964003 515 RQVLGIEtgAEVLN 528
Cdd:PRK11231 232 RTVFDVE--AEIHP 243
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
 279-497 1.48e-25

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


Pssm-ID: 213235 [Multi-domain]  Cd Length: 208  Bit Score: 104.22  E-value: 1.48e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 279 VEFKDVTFAYPTRPetdVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHDYlhSKIA 358
Cdd:cd03268    1 LKTNDLTKTYGKKR---VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAL--RRIG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 359 LVGQEPVLF-ARTIKENISYGLsdvsmemVVQAATKANAHDFITTLpkGYDTSVGEKGLQLSGGQKQRVAIARALIRQPR 437
Cdd:cd03268   76 ALIEAPGFYpNLTARENLRLLA-------RLLGIRKKRIDEVLDVV--GLKDSAKKKVKGFSLGMKQRLGIALALLGNPD 146

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 961964003 438 VLILDEATSALDAESEHIVQQALNSIMQE-HTVLVIAHRLSTVEK-ADNIIVIDRGQVAERG 497
Cdd:cd03268  147 LLILDEPTNGLDPDGIKELRELILSLRDQgITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
PLN03130 PLN03130
ABC transporter C family member; Provisional
 279-514 1.78e-25

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 111.75  E-value: 1.78e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  279 VEFKDVTFAYPTRPETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVS--LLEnfyLP--QGGQVLLDGKpvnefqhdylh 354
Cdd:PLN03130  615 ISIKNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISamLGE---LPprSDASVVIRGT----------- 680

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  355 skIALVGQEPVLFARTIKENISYGL--SDVSMEMVVQAAtkANAHDfITTLPKGYDTSVGEKGLQLSGGQKQRVAIARAL 432
Cdd:PLN03130  681 --VAYVPQVSWIFNATVRDNILFGSpfDPERYERAIDVT--ALQHD-LDLLPGGDLTEIGERGVNISGGQKQRVSMARAV 755

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  433 IRQPRVLILDEATSALDAeseHIVQQALNSIMQEH-----TVLVI--AHRLSTVekaDNIIVIDRGQVAERGTHSQLMAT 505
Cdd:PLN03130  756 YSNSDVYIFDDPLSALDA---HVGRQVFDKCIKDElrgktRVLVTnqLHFLSQV---DRIILVHEGMIKEEGTYEELSNN 829


                  ....*....
gi 961964003  506 GGLYCKLVQ 514
Cdd:PLN03130  830 GPLFQKLME 838
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
 297-476 2.60e-25

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 104.86  E-value: 2.60e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 297 LKGVSFTLRPGEVTALVGPSGSGKSSCVSLLE--NFYLPQ---GGQVLLDGKPVNEFQHDY--LHSKIALVGQEPVLFAR 369
Cdd:PRK14239  21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPEvtiTGSIVYNGHNIYSPRTDTvdLRKEIGMVFQQPNPFPM 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 370 TIKENISYGL-------SDVSMEMVVQAATKANAHDFITTlpKGYDTSVGekglqLSGGQKQRVAIARALIRQPRVLILD 442
Cdd:PRK14239 101 SIYENVVYGLrlkgikdKQVLDEAVEKSLKGASIWDEVKD--RLHDSALG-----LSGGQQQRVCIARVLATSPKIILLD 173

                        170       180       190
                 ....*....|....*....|....*....|....
gi 961964003 443 EATSALDAESEHIVQQALNSIMQEHTVLVIAHRL 476
Cdd:PRK14239 174 EPTSALDPISAGKIEETLLGLKDDYTMLLVTRSM 207
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
 271-505 3.76e-25

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 109.02  E-value: 3.76e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 271 APNSCTGLVEFKDVTFAYPTRP--------ETDVLKGVSFTLRPGEVTALVGPSGSGKSSC-VSLLEnfYLPQGGQVLLD 341
Cdd:PRK15134 268 LPEPASPLLDVEQLQVAFPIRKgilkrtvdHNVVVKNISFTLRPGETLGLVGESGSGKSTTgLALLR--LINSQGEIWFD 345

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 342 GKPVNEF---QHDYLHSKIALVGQEP--VLFAR-TIKENISYGLSdvsmemVVQAATKANAHD--FITTLPkgydtsvgE 413
Cdd:PRK15134 346 GQPLHNLnrrQLLPVRHRIQVVFQDPnsSLNPRlNVLQIIEEGLR------VHQPTLSAAQREqqVIAVME--------E 411

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 414 KGL----------QLSGGQKQRVAIARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQEHTV--LVIAHRLSTVEK 481
Cdd:PRK15134 412 VGLdpetrhrypaEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLayLFISHDLHVVRA 491

                        250       260
                 ....*....|....*....|....*
gi 961964003 482 -ADNIIVIDRGQVAERGTHSQLMAT 505
Cdd:PRK15134 492 lCHQVIVLRQGEVVEQGDCERVFAA 516
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
279-500 8.40e-25

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


Pssm-ID: 443326 [Multi-domain]  Cd Length: 242  Bit Score: 103.17  E-value: 8.40e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 279 VEFKDVTFAYPTrpeTDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDG------KPVNEFQHDY 352
Cdd:COG4161    3 IQLKNINCFYGS---HQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIRL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 353 LHSKIALVGQEPVLFA-RTIKENIS------YGLS-DVSMEMVVQAATKANAHDFITTLPkgydtsvgekgLQLSGGQKQ 424
Cdd:COG4161   80 LRQKVGMVFQQYNLWPhLTVMENLIeapckvLGLSkEQAREKAMKLLARLRLTDKADRFP-----------LHLSGGQQQ 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 425 RVAIARALIRQPRVLILDEATSALDAEsehIVQQALNSIMQ----EHTVLVIAHRLSTVEK-ADNIIVIDRGQVAERGTH 499
Cdd:COG4161  149 RVAIARALMMEPQVLLFDEPTAALDPE---ITAQVVEIIRElsqtGITQVIVTHEVEFARKvASQVVYMEKGRIIEQGDA 225


                 .
gi 961964003 500 S 500
Cdd:COG4161  226 S 226
cbiO PRK13644
energy-coupling factor transporter ATPase;
278-504 8.84e-25

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 103.91  E-value: 8.84e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 278 LVEFKDVTFAYPTrpETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQH-DYLHSK 356
Cdd:PRK13644   1 MIRLENVSYSYPD--GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKlQGIRKL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 357 IALVGQEP--VLFARTIKENISYGLSDVSMEMvvqaatkanahdfiTTLPKGYDTSVGEKGLQ---------LSGGQKQR 425
Cdd:PRK13644  79 VGIVFQNPetQFVGRTVEEDLAFGPENLCLPP--------------IEIRKRVDRALAEIGLEkyrhrspktLSGGQGQC 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 426 VAIARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQE-HTVLVIAHRLSTVEKADNIIVIDRGQVAERGTHSQLMA 504
Cdd:PRK13644 145 VALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKgKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLS 224
cbiO PRK13646
energy-coupling factor transporter ATPase;
279-506 9.15e-25

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 104.09  E-value: 9.15e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 279 VEFKDVTFAYP--TRPETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHD----Y 352
Cdd:PRK13646   3 IRFDNVSYTYQkgTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDkyirP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 353 LHSKIALVGQ--EPVLFARTIKENISYGLSDVSMEMvvqAATKANAHDFITTLpkGYDTSVGEKG-LQLSGGQKQRVAIA 429
Cdd:PRK13646  83 VRKRIGMVFQfpESQLFEDTVEREIIFGPKNFKMNL---DEVKNYAHRLLMDL--GFSRDVMSQSpFQMSGGQMRKIAIV 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 430 RALIRQPRVLILDEATSALDAESEHIVQQALNSIMQEH--TVLVIAHRLSTVEK-ADNIIVIDRGQVAERGTHSQLMATG 506
Cdd:PRK13646 158 SILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDEnkTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKELFKDK 237
PLN03232 PLN03232
ABC transporter C family member; Provisional
 279-514 9.32e-25

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 109.68  E-value: 9.32e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  279 VEFKDVTFAYPTRPETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSllenfylpqggqVLLDGKPVNEFQHDYLHSKIA 358
Cdd:PLN03232  615 ISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLIS------------AMLGELSHAETSSVVIRGSVA 682

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  359 LVGQEPVLFARTIKENISYGlSDVSMEMVVQAA-TKANAHDFitTLPKGYD-TSVGEKGLQLSGGQKQRVAIARALIRQP 436
Cdd:PLN03232  683 YVPQVSWIFNATVRENILFG-SDFESERYWRAIdVTALQHDL--DLLPGRDlTEIGERGVNISGGQKQRVSMARAVYSNS 759

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  437 RVLILDEATSALDAeseHIVQQALNSIMQEH----TVLVIAHRLSTVEKADNIIVIDRGQVAERGTHSQLMATGGLYCKL 512
Cdd:PLN03232  760 DIYIFDDPLSALDA---HVAHQVFDSCMKDElkgkTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKL 836


                  ..
gi 961964003  513 VQ 514
Cdd:PLN03232  837 ME 838
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
278-498 1.06e-24

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 104.01  E-value: 1.06e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 278 LVEFKDVTFAYPTRPETD---VLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHDY-L 353
Cdd:PRK13633   4 MIKCKNVSYKYESNEESTeklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWdI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 354 HSKIALVGQEP--VLFARTIKENISYGLSDVSM------EMVVQAATKANAHDFITTLPKgydtsvgekglQLSGGQKQR 425
Cdd:PRK13633  84 RNKAGMVFQNPdnQIVATIVEEDVAFGPENLGIppeeirERVDESLKKVGMYEYRRHAPH-----------LLSGGQKQR 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 961964003 426 VAIARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQEH--TVLVIAHRLSTVEKADNIIVIDRGQVAERGT 498
Cdd:PRK13633 153 VAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEAVEADRIIVMDSGKVVMEGT 227
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
 296-502 1.15e-24

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 107.44  E-value: 1.15e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 296 VLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHDYLHS-KIALVGQEPVLFAR-TIKE 373
Cdd:PRK15439  26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQlGIYLVPQEPLLFPNlSVKE 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 374 NISYGLSDvsmemvvQAATKANAHDFITTLPKGYDTSVGEKGLQLSggQKQRVAIARALIRQPRVLILDEATSALD-AES 452
Cdd:PRK15439 106 NILFGLPK-------RQASMQKMKQLLAALGCQLDLDSSAGSLEVA--DRQIVEILRGLMRDSRILILDEPTASLTpAET 176

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 961964003 453 EHIVQQaLNSIMQE-HTVLVIAHRLSTVEK-ADNIIVIDRGQVAERGTHSQL 502
Cdd:PRK15439 177 ERLFSR-IRELLAQgVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADL 227
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
 279-504 1.26e-24

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 103.95  E-value: 1.26e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 279 VEFKDVTFAY-PTRP-ETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPV----NEFQHDY 352
Cdd:PRK13634   3 ITFQKVEHRYqYKTPfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkKNKKLKP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 353 LHSKIALVGQ--EPVLFARTIKENISYGLSDVSmemVVQAATKANAHDFITTLpkGYDTSVGEKG-LQLSGGQKQRVAIA 429
Cdd:PRK13634  83 LRKKVGIVFQfpEHQLFEETVEKDICFGPMNFG---VSEEDAKQKAREMIELV--GLPEELLARSpFELSGGQMRRVAIA 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 961964003 430 RALIRQPRVLILDEATSALDAESEHIVQQALNSIMQEH--TVLVIAHRLSTVEK-ADNIIVIDRGQVAERGTHSQLMA 504
Cdd:PRK13634 158 GVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKglTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREIFA 235
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
 290-498 1.45e-24

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 104.55  E-value: 1.45e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 290 TRPETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQV-----LLDGKPVNEFQHDYLHSK-------- 356
Cdd:PRK13631  35 QENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdiYIGDKKNNHELITNPYSKkiknfkel 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 357 ---IALVGQEP--VLFARTIKENISYGLSDVSMEMVvQAATKANAHdfittLPK-GYDTSVGEKG-LQLSGGQKQRVAIA 429
Cdd:PRK13631 115 rrrVSMVFQFPeyQLFKDTIEKDIMFGPVALGVKKS-EAKKLAKFY-----LNKmGLDDSYLERSpFGLSGGQKRRVAIA 188

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 961964003 430 RALIRQPRVLILDEATSALDAESEH-IVQQALNSIMQEHTVLVIAHRLSTV-EKADNIIVIDRGQVAERGT 498
Cdd:PRK13631 189 GILAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVlEVADEVIVMDKGKILKTGT 259
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
 278-504 1.76e-24

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 104.28  E-value: 1.76e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 278 LVEFKDVTFAYPTR-----PETDV--LKGVSFTLRPGEVTALVGPSGSGKSSC---VSLLENfylPQGGQVLLDGKPVNE 347
Cdd:PRK11308   5 LLQAIDLKKHYPVKrglfkPERLVkaLDGVSFTLERGKTLAVVGESGCGKSTLarlLTMIET---PTGGELYYQGQDLLK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 348 FQHDY---LHSKIALVGQEPV--LFAR----TIKEN---ISYGLSdvsmemvvQAATKANAHDFITTL---PKGYDtsvg 412
Cdd:PRK11308  82 ADPEAqklLRQKIQIVFQNPYgsLNPRkkvgQILEEpllINTSLS--------AAERREKALAMMAKVglrPEHYD---- 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 413 EKGLQLSGGQKQRVAIARALIRQPRVLILDEATSALDAEsehIVQQALNSIM---QE-HTVLV-IAHRLSTVEK-ADNII 486
Cdd:PRK11308 150 RYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVS---VQAQVLNLMMdlqQElGLSYVfISHDLSVVEHiADEVM 226

                        250
                 ....*....|....*...
gi 961964003 487 VIDRGQVAERGTHSQLMA 504
Cdd:PRK11308 227 VMYLGRCVEKGTKEQIFN 244
ABC_6TM_Pgp_ABCB1 cd18558
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ...
 7-254 2.03e-24

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: 103.90  E-value: 2.03e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   7 FTLFFLLSSMAIGVRGGVFTLTMARLNVRLRSRLFRTLMTQEIAFFDENHTGDILSRLSADTTQVSDLISQNVNVFLRSV 86
Cdd:cd18558   65 YLIIGAIVLITAYIQGSFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIFQNI 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  87 IK-GTGFIIFMFRmSWKLTLVTMMGFPFIALVSKLYGEYYKKLTKEVQTVLAEANKVAEETISGMRTVRSFANESREANS 165
Cdd:cd18558  145 ATfGTGFIIGFIR-GWKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETR 223

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 166 YYAKLLVMFQLNKKQALAYACYMWSSCISELALEVAVLYYGGHLVLTDQLSSGGLISFFIYMLELGECFESIASVYSGLM 245
Cdd:cd18558  224 YAQNLEIAKRNGIKKAITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGEVLTVFFSVLIGAFSAGQQVPSIEAFA 303


                 ....*....
gi 961964003 246 QGVGAAEKV 254
Cdd:cd18558  304 NARGAAYHI 312
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
 296-492 2.83e-24

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: 101.36  E-value: 2.83e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 296 VLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLldgkpvneFQHDYlhSKIALVGQEPvlfaRTI---- 371
Cdd:COG4778   26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSIL--------VRHDG--GWVDLAQASP----REIlalr 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 372 KENISYglsdVS-----------MEMVVQ---------AATKANAHDFITTLpkgydtSVGEKGLQL-----SGGQKQRV 426
Cdd:COG4778   92 RRTIGY----VSqflrviprvsaLDVVAEpllergvdrEEARARARELLARL------NLPERLWDLppatfSGGEQQRV 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 961964003 427 AIARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQEHTVLV-IAHRLSTVEK-ADNIIVIDRGQ 492
Cdd:COG4778  162 NIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIgIFHDEEVREAvADRVVDVTPFS 229
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
 292-491 3.37e-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: 100.87  E-value: 3.37e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 292 PETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHDYLHSK----IALVGQEPVLF 367
Cdd:cd03290   12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWLL 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 368 ARTIKENISYG--LSDVSMEMVVQAATkanAHDFITTLPKGYDTSVGEKGLQLSGGQKQRVAIARALIRQPRVLILDEAT 445
Cdd:cd03290   92 NATVEENITFGspFNKQRYKAVTDACS---LQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPF 168

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 961964003 446 SALDAE-SEHIVQQALNSIMQE--HTVLVIAHRLSTVEKADNIIVIDRG 491
Cdd:cd03290  169 SALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
 291-468 3.57e-24

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: 100.13  E-value: 3.57e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  291 RPETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEfQHDYLHSKIALVGQEPVLFAR- 369
Cdd:TIGR01189  10 RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAE-QRDEPHENILYLGHLPGLKPEl 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  370 TIKENISY--GLSDVSMEMVVQAATKANAHDFiTTLPKGydtsvgekglQLSGGQKQRVAIARALIRQPRVLILDEATSA 447
Cdd:TIGR01189  89 SALENLHFwaAIHGGAQRTIEDALAAVGLTGF-EDLPAA----------QLSAGQQRRLALARLWLSRRPLWILDEPTTA 157

                         170       180
                  ....*....|....*....|.
gi 961964003  448 LDAESehivQQALNSIMQEHT 468
Cdd:TIGR01189 158 LDKAG----VALLAGLLRAHL 174
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
265-497 3.64e-24

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 104.53  E-value: 3.64e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 265 PADGTEAPNSCTGLVEFKDVTFAYPTRPETDvlkGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGkp 344
Cdd:PRK11607   6 PRPQAKTRKALTPLLEIRNLTKSFDGQHAVD---DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDG-- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 345 vnefqHDYLH-----SKIALVGQEPVLFAR-TIKENISYGLSDvsmEMVVQAATKANAHDFITTLpkGYDTSVGEKGLQL 418
Cdd:PRK11607  81 -----VDLSHvppyqRPINMMFQSYALFPHmTVEQNIAFGLKQ---DKLPKAEIASRVNEMLGLV--HMQEFAKRKPHQL 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 419 SGGQKQRVAIARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQE---HTVLVIAHRLSTVEKADNIIVIDRGQVAE 495
Cdd:PRK11607 151 SGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERvgvTCVMVTHDQEEAMTMAGRIAIMNRGKFVQ 230


                 ..
gi 961964003 496 RG 497
Cdd:PRK11607 231 IG 232
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
 291-492 5.31e-24

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: 99.87  E-value: 5.31e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 291 RPETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNeFQHDYLHSKIALVGQEPVLFAR- 369
Cdd:cd03231   10 RDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLD-FQRDSIARGLLYLGHAPGIKTTl 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 370 TIKENISYGLSDVSMEMVVQAATKANAHDFittlpkgYDTSVGekglQLSGGQKQRVAIARALIRQPRVLILDEATSALD 449
Cdd:cd03231   89 SVLENLRFWHADHSDEQVEEALARVGLNGF-------EDRPVA----QLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 961964003 450 AESEHIVQQALNSIMQEHTVLVIAHRLSTVEKADNIIVIDRGQ 492
Cdd:cd03231  158 KAGVARFAEAMAGHCARGGMVVLTTHQDLGLSEAGARELDLGF 200
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
 279-500 5.38e-24

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 100.86  E-value: 5.38e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 279 VEFKDVTFAYPTrpeTDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDG------KPVNEFQHDY 352
Cdd:PRK11124   3 IQLNGINCFYGA---HQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAIRE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 353 LHSKIALVGQEPVLFAR-TIKENIsyglsdVSMEMVVQAATKANAH-------------DFITTLPkgydtsvgekgLQL 418
Cdd:PRK11124  80 LRRNVGMVFQQYNLWPHlTVQQNL------IEAPCRVLGLSKDQALaraekllerlrlkPYADRFP-----------LHL 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 419 SGGQKQRVAIARALIRQPRVLILDEATSALDAEsehIVQQALnSIMQEH-----TVLVIAHRLSTVEK-ADNIIVIDRGQ 492
Cdd:PRK11124 143 SGGQQQRVAIARALMMEPQVLLFDEPTAALDPE---ITAQIV-SIIRELaetgiTQVIVTHEVEVARKtASRVVYMENGH 218


                 ....*...
gi 961964003 493 VAERGTHS 500
Cdd:PRK11124 219 IVEQGDAS 226
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
 278-495 5.70e-24

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: 100.59  E-value: 5.70e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 278 LVEFKDVTFAYPTRPET-DVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHDYL--- 353
Cdd:COG4181    8 IIELRGLTKTVGTGAGElTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARarl 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 354 -HSKIALVGQ-EPVLFARTIKENISyglsdVSMEMVVQAATKANAHDFITtlpkgydtSVGEKGL------QLSGGQKQR 425
Cdd:COG4181   88 rARHVGFVFQsFQLLPTLTALENVM-----LPLELAGRRDARARARALLE--------RVGLGHRldhypaQLSGGEQQR 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 961964003 426 VAIARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQEH-TVLVIA-HRLSTVEKADNIIVIDRGQVAE 495
Cdd:COG4181  155 VALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERgTTLVLVtHDPALAARCDRVLRLRAGRLVE 226
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
 281-493 6.53e-24

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 105.15  E-value: 6.53e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 281 FKDVTFAYPTRPetdVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGkpvnefqhdylHSKIALV 360
Cdd:COG0488    1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-----------GLRIGYL 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 361 GQEPVLFA-RTIKENISYGLSDV------------SMEMVVQAATK-ANAHDFITTLpKGY--DTSVGE--KGL------ 416
Cdd:COG0488   67 PQEPPLDDdLTVLDTVLDGDAELraleaeleeleaKLAEPDEDLERlAELQEEFEAL-GGWeaEARAEEilSGLgfpeed 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 417 ------QLSGGQKQRVAIARALIRQPRVLILDEATSALDAES----EHIVQQalnsimQEHTVLVIAH-R--LSTVekAD 483
Cdd:COG0488  146 ldrpvsELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESiewlEEFLKN------YPGTVLVVSHdRyfLDRV--AT 217

                        250
                 ....*....|
gi 961964003 484 NIIVIDRGQV 493
Cdd:COG0488  218 RILELDRGKL 227
SapF COG4167
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
285-504 9.31e-24

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


Pssm-ID: 443328 [Multi-domain]  Cd Length: 265  Bit Score: 100.68  E-value: 9.31e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 285 TFAYPT----RPETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHDYLHSKIALV 360
Cdd:COG4167   13 TFKYRTglfrRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKYRCKHIRMI 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 361 GQEPV--LFARTikeNISYGLsdvsmEMVVQAATKANAHD----FITTLPKgydtsVG---EKGL----QLSGGQKQRVA 427
Cdd:COG4167   93 FQDPNtsLNPRL---NIGQIL-----EEPLRLNTDLTAEEreerIFATLRL-----VGllpEHANfyphMLSSGQKQRVA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 428 IARALIRQPRVLILDEATSALDAEsehIVQQALN---SIMQEHTV--LVIAHRLSTVEK-ADNIIVIDRGQVAERGTHSQ 501
Cdd:COG4167  160 LARALILQPKIIIADEALAALDMS---VRSQIINlmlELQEKLGIsyIYVSQHLGIVKHiSDKVLVMHQGEVVEYGKTAE 236


                 ...
gi 961964003 502 LMA 504
Cdd:COG4167  237 VFA 239
nickel_nikE TIGR02769
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ...
 278-518 9.72e-24

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: 100.65  E-value: 9.72e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  278 LVEFKDVTFAYPT------RPETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEF--- 348
Cdd:TIGR02769   2 LLEVRDVTHTYRTgglfgaKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLdrk 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  349 QHDYLHSKIALVGQE---PVLFARTIKENISYGLSDvsMEMVVQAATKANAHDFITTLpkGYDTSVGEK-GLQLSGGQKQ 424
Cdd:TIGR02769  82 QRRAFRRDVQLVFQDspsAVNPRMTVRQIIGEPLRH--LTSLDESEQKARIAELLDMV--GLRSEDADKlPRQLSGGQLQ 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  425 RVAIARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQEH--TVLVIAHRLSTVEK-ADNIIVIDRGQVAERGTHSQ 501
Cdd:TIGR02769 158 RINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFgtAYLFITHDLRLVQSfCQRVAVMDKGQIVEECDVAQ 237

                         250
                  ....*....|....*..
gi 961964003  502 LMATGGLYCKLVQRQVL 518
Cdd:TIGR02769 238 LLSFKHPAGRNLQSAVL 254
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
 278-476 1.04e-23

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: 100.16  E-value: 1.04e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 278 LVEFKDVTFAYPTRPetdVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLeNFYLPQ--GGQVLLDGKP---VNEFQhdy 352
Cdd:COG1119    3 LLELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLI-TGDLPPtyGNDVRLFGERrggEDVWE--- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 353 LHSKIALVGQEpvlFARTIKENIS---------YGLSDVSMEmvVQAATKANAHDFITTLpkgydtsvgekGL------- 416
Cdd:COG1119   76 LRKRIGLVSPA---LQLRFPRDETvldvvlsgfFDSIGLYRE--PTDEQRERARELLELL-----------GLahladrp 139

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 961964003 417 --QLSGGQKQRVAIARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQEH--TVLVIAHRL 476
Cdd:COG1119  140 fgTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGapTLVLVTHHV 203
ABC_6TM_exporter_like cd18540
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
 5-254 1.04e-23

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: 101.40  E-value: 1.04e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   5 PPFTLFFLLSSMAIGVrgGVFTLTM------ARLNVRLRSRLFRTLMTQEIAFFDENHTGDILSRLSADTTQVSDLISQN 78
Cdd:cd18540   42 TGFILLYLGLILIQAL--SVFLFIRlagkieMGVSYDLRKKAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIISWG 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  79 VNVFLRSVIKGTGFIIFMFRMSWKLTLVTMMGFPFIALVS----KLYGEYYKKLTKEVQTVLAEANkvaeETISGMRTVR 154
Cdd:cd18540  120 LVDLVWGITYMIGILIVMLILNWKLALIVLAVVPVLAVVSiyfqKKILKAYRKVRKINSRITGAFN----EGITGAKTTK 195

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 155 SFANESREANSYYAKLLVMFQLNKKQALAYACYMWS-SCISELALeVAVLYYGGHLVLTDQLSSGGLISFFIYMLELGEC 233
Cdd:cd18540  196 TLVREEKNLREFKELTEEMRRASVRAARLSALFLPIvLFLGSIAT-ALVLWYGGILVLAGAITIGTLVAFISYATQFFEP 274

                        250       260
                 ....*....|....*....|.
gi 961964003 234 FESIASVYSGLMQGVGAAEKV 254
Cdd:cd18540  275 IQQLARVLAELQSAQASAERV 295
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
290-495 1.50e-23

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 100.15  E-value: 1.50e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 290 TRPETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEF---QHDYLHSKIALVGQEP-- 364
Cdd:PRK10419  21 KHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLnraQRKAFRRDIQMVFQDSis 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 365 -VLFARTIKENIS------YGLSDVSMEMVVQAATKAnahdfittlpKGYDTSVGEK-GLQLSGGQKQRVAIARALIRQP 436
Cdd:PRK10419 101 aVNPRKTVREIIReplrhlLSLDKAERLARASEMLRA----------VDLDDSVLDKrPPQLSGGQLQRVCLARALAVEP 170

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 961964003 437 RVLILDEATSALDAESEHIVQQALNSIMQEHTV--LVIAHRLSTVEK-ADNIIVIDRGQVAE 495
Cdd:PRK10419 171 KLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTacLFITHDLRLVERfCQRVMVMDNGQIVE 232
cbiO PRK13641
energy-coupling factor transporter ATPase;
279-493 1.54e-23

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 100.67  E-value: 1.54e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 279 VEFKDVTFAY-PTRP-ETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHDY---- 352
Cdd:PRK13641   3 IKFENVDYIYsPGTPmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKnlkk 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 353 LHSKIALVGQ--EPVLFARTIKENISYGLSDVSmemVVQAATKANAHDFITTLpkGYDTSVGEKG-LQLSGGQKQRVAIA 429
Cdd:PRK13641  83 LRKKVSLVFQfpEAQLFENTVLKDVEFGPKNFG---FSEDEAKEKALKWLKKV--GLSEDLISKSpFELSGGQMRRVAIA 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 961964003 430 RALIRQPRVLILDEATSALDAESEHIVQQALNSIMQE-HTVLVIAHRLSTV-EKADNIIVIDRGQV 493
Cdd:PRK13641 158 GVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAgHTVILVTHNMDDVaEYADDVLVLEHGKL 223
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
 279-493 1.54e-23

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: 98.51  E-value: 1.54e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 279 VEFKDVTFAYPTrpeTDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVnefqhDYLH-SKI 357
Cdd:cd03269    1 LEVENVTKRFGR---VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL-----DIAArNRI 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 358 ALVGQEPVLF-ARTIKENISY--GLSDVSMEmvvqaATKANAHDFITTLP-KGYDTSVGEkglQLSGGQKQRVAIARALI 433
Cdd:cd03269   73 GYLPEERGLYpKMKVIDQLVYlaQLKGLKKE-----EARRRIDEWLERLElSEYANKRVE---ELSKGNQQKVQFIAAVI 144

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 961964003 434 RQPRVLILDEATSALDAESEHIVQQALNSIM-QEHTVLVIAHRLSTVEK-ADNIIVIDRGQV 493
Cdd:cd03269  145 HDPELLILDEPFSGLDPVNVELLKDVIRELArAGKTVILSTHQMELVEElCDRVLLLNKGRA 206
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
278-505 1.55e-23

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 100.25  E-value: 1.55e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 278 LVEFKDV--TFAYPT----RPETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHD 351
Cdd:PRK15112   4 LLEVRNLskTFRYRTgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYS 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 352 YLHSKIALVGQEPVLfARTIKENISYGLsDVSMEMVVQAATKANAHDFITTLPkgydtsvgEKGL----------QLSGG 421
Cdd:PRK15112  84 YRSQRIRMIFQDPST-SLNPRQRISQIL-DFPLRLNTDLEPEQREKQIIETLR--------QVGLlpdhasyyphMLAPG 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 422 QKQRVAIARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQEHT---VLVIAHRLSTVEKADNIIVIDRGQVAERGT 498
Cdd:PRK15112 154 QKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGisyIYVTQHLGMMKHISDQVLVMHQGEVVERGS 233


                 ....*..
gi 961964003 499 HSQLMAT 505
Cdd:PRK15112 234 TADVLAS 240
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
276-505 1.64e-23

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 101.04  E-value: 1.64e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 276 TGLVEFKDVTFAYPtrpETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHdYLHS 355
Cdd:PRK13537   5 VAPIDFRNVEKRYG---DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRAR-HARQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 356 KIALVGQ----EPVLfarTIKENIS-----YGLSDVSMEMVVQAATKanahdfITTLPKGYDTSVGEkglqLSGGQKQRV 426
Cdd:PRK13537  81 RVGVVPQfdnlDPDF---TVRENLLvfgryFGLSAAAARALVPPLLE------FAKLENKADAKVGE----LSGGMKRRL 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 427 AIARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQE-HTVLVIAHRLSTVEK-ADNIIVIDRGQVAERGTHSQLMA 504
Cdd:PRK13537 148 TLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARgKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHALIE 227


                 .
gi 961964003 505 T 505
Cdd:PRK13537 228 S 228
ABC_6TM_PCAT1_LagD_like cd18570
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ...
 31-224 1.69e-23

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: 100.60  E-value: 1.69e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  31 RLNVRLRSRLFRTLMTQEIAFFDENHTGDILSRLSaDTTQVSDLISQN-VNVFLRSVIKGTGFIiFMFRMSWKLTLVTMM 109
Cdd:cd18570   72 KLDIRLILGYFKHLLKLPLSFFETRKTGEIISRFN-DANKIREAISSTtISLFLDLLMVIISGI-ILFFYNWKLFLITLL 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 110 GFPFIALVSKLYGEYYKKLTKEVQTVLAEANKVAEETISGMRTVRSFANESR---EANSYYAKLL-VMFQLNKKQALAYA 185
Cdd:cd18570  150 IIPLYILIILLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQflkKIEKKFSKLLkKSFKLGKLSNLQSS 229

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 961964003 186 cymWSSCISELaLEVAVLYYGGHLVLTDQLSSGGLISFF 224
Cdd:cd18570  230 ---IKGLISLI-GSLLILWIGSYLVIKGQLSLGQLIAFN 264
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
 280-467 1.93e-23

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


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 98.32  E-value: 1.93e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 280 EFKDVTFAYPTRPetdVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFyLPQG----GQVLLDGKPVNEFQhdYLHS 355
Cdd:COG4136    3 SLENLTITLGGRP---LLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGT-LSPAfsasGEVLLNGRRLTALP--AEQR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 356 KIALVGQEPVLFAR-TIKENISYGL-SDVSME----MVVQAATKANAHDFITTLPKgydtsvgekglQLSGGQKQRVAIA 429
Cdd:COG4136   77 RIGILFQDDLLFPHlSVGENLAFALpPTIGRAqrraRVEQALEEAGLAGFADRDPA-----------TLSGGQRARVALL 145

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 961964003 430 RALIRQPRVLILDEATSALDAES---------EHIVQQALNSIMQEH 467
Cdd:COG4136  146 RALLAEPRALLLDEPFSKLDAALraqfrefvfEQIRQRGIPALLVTH 192
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
276-493 3.34e-23

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 103.65  E-value: 3.34e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 276 TGLVEFKDVTFAYPTRPET-DVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHDYLh 354
Cdd:PRK10535   2 TALLELKDIRRSYPSGEEQvEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADAL- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 355 skiALVGQE--PVLFARTikenisYGLSDVSMEMVVQ----------AATKANAHDFITTLpkGYDTSVGEKGLQLSGGQ 422
Cdd:PRK10535  81 ---AQLRREhfGFIFQRY------HLLSHLTAAQNVEvpavyaglerKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQ 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 961964003 423 KQRVAIARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQE-HTVLVIAHRLSTVEKADNIIVIDRGQV 493
Cdd:PRK10535 150 QQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRgHTVIIVTHDPQVAAQAERVIEIRDGEI 221
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
 279-502 3.99e-23

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 98.96  E-value: 3.99e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 279 VEFKDVTFAYPTRpetDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLeNFYLPQGGQVLLDGKPvnEF--QHDY---- 352
Cdd:PRK14258   8 IKVNNLSFYYDTQ---KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNELESEVRVEGRV--EFfnQNIYerrv 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 353 ----LHSKIALVGQEPVLFARTIKENISYGLS------DVSMEMVVQAATKAnahdfiTTLPKGYDTSVGEKGLQLSGGQ 422
Cdd:PRK14258  82 nlnrLRRQVSMVHPKPNLFPMSVYDNVAYGVKivgwrpKLEIDDIVESALKD------ADLWDEIKHKIHKSALDLSGGQ 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 423 KQRVAIARALIRQPRVLILDEATSALDAES----EHIVQQAlnSIMQEHTVLVIAHRLSTVEKADNIIVIDRG------Q 492
Cdd:PRK14258 156 QQRLCIARALAVKPKVLLMDEPCFGLDPIAsmkvESLIQSL--RLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenrigQ 233

                        250
                 ....*....|
gi 961964003 493 VAERGTHSQL 502
Cdd:PRK14258 234 LVEFGLTKKI 243
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
 291-510 6.07e-23

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


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 102.82  E-value: 6.07e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  291 RPETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLEnFYLPQG----GQVLLDGKPVNEFQhdyLHSKIALVGQEPVL 366
Cdd:TIGR00955  35 RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKGvkgsGSVLLNGMPIDAKE---MRAISAYVQQDDLF 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  367 F-ARTIKENISYgLSDVSMEMVVQAATKANAHDFITT---LPKGYDTSVGEKGLQ--LSGGQKQRVAIARALIRQPRVLI 440
Cdd:TIGR00955 111 IpTLTVREHLMF-QAHLRMPRRVTKKEKRERVDEVLQalgLRKCANTRIGVPGRVkgLSGGERKRLAFASELLTDPPLLF 189

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 961964003  441 LDEATSALDAESEHIVQQALNSIMQE-HTVLVIAHRLST--VEKADNIIVIDRGQVAERGTHSQL---MATGGLYC 510
Cdd:TIGR00955 190 CDEPTSGLDSFMAYSVVQVLKGLAQKgKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQAvpfFSDLGHPC 265
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
 278-498 1.01e-22

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 97.95  E-value: 1.01e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 278 LVEFKDVTFAYptRPETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHDYLHSKI 357
Cdd:PRK13652   3 LIETRDLCYSY--SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 358 ALVGQEP--VLFARTIKENISYG-----LSDVSMEMVVQAATKA-NAHDFITTLPKgydtsvgekglQLSGGQKQRVAIA 429
Cdd:PRK13652  81 GLVFQNPddQIFSPTVEQDIAFGpinlgLDEETVAHRVSSALHMlGLEELRDRVPH-----------HLSGGEKKRVAIA 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 961964003 430 RALIRQPRVLILDEATSALDAESEHIVQQALNSIMQEH--TVLVIAHRLSTV-EKADNIIVIDRGQVAERGT 498
Cdd:PRK13652 150 GVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYgmTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGT 221
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
283-508 1.03e-22

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 98.16  E-value: 1.03e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 283 DVTFAYPTRPetdVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHDY--LHSKIALV 360
Cdd:PRK13638   6 DLWFRYQDEP---VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLlaLRQQVATV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 361 GQEP--VLFARTIKENISYGLSDVSM------EMVVQAATKANAHDFittlpkgydtsvGEKGLQ-LSGGQKQRVAIARA 431
Cdd:PRK13638  83 FQDPeqQIFYTDIDSDIAFSLRNLGVpeaeitRRVDEALTLVDAQHF------------RHQPIQcLSHGQKKRVAIAGA 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 432 LIRQPRVLILDEATSALD--------AESEHIVQQALNSIMQEHTVLVIahrlstVEKADNIIVIDRGQVAERGTHSQLM 503
Cdd:PRK13638 151 LVLQARYLLLDEPTAGLDpagrtqmiAIIRRIVAQGNHVIISSHDIDLI------YEISDAVYVLRQGQILTHGAPGEVF 224


                 ....*
gi 961964003 504 ATGGL 508
Cdd:PRK13638 225 ACTEA 229
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
 297-498 1.33e-22

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 97.55  E-value: 1.33e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 297 LKGVSFTLRPGEVTALVGPSGSGKSS---CVS----LLENFYLPqgGQVLLDGKPVNEFQHD--YLHSKIALVGQEPVLF 367
Cdd:PRK14243  26 VKNVWLDIPKNQITAFIGPSGCGKSTilrCFNrlndLIPGFRVE--GKVTFHGKNLYAPDVDpvEVRRRIGMVFQKPNPF 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 368 ARTIKENISYGLS----DVSMEMVVQAATKANAhdfittLPKGYDTSVGEKGLQLSGGQKQRVAIARALIRQPRVLILDE 443
Cdd:PRK14243 104 PKSIYDNIAYGARingyKGDMDELVERSLRQAA------LWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDE 177

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 961964003 444 ATSALDAESEHIVQQALNSIMQEHTVLVIAHRLSTVEKADNIIVIDRGQVAERGT 498
Cdd:PRK14243 178 PCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFNVELTEGGG 232
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
279-499 1.55e-22

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 98.75  E-value: 1.55e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 279 VEFKDVTFAYPTRPetdVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEfQHDYLHSKIA 358
Cdd:PRK13536  42 IDLAGVSKSYGDKA---VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIG 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 359 LVGQEPVLFAR-TIKENI-----SYGLSDVSMEMVVQAATkanahDFiTTLPKGYDTSVGEkglqLSGGQKQRVAIARAL 432
Cdd:PRK13536 118 VVPQFDNLDLEfTVRENLlvfgrYFGMSTREIEAVIPSLL-----EF-ARLESKADARVSD----LSGGMKRRLTLARAL 187

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 433 IRQPRVLILDEATSALDAESEHIVQQALNSIM-QEHTVLVIAHRLSTVEK-ADNIIVIDRG-QVAERGTH 499
Cdd:PRK13536 188 INDPQLLILDEPTTGLDPHARHLIWERLRSLLaRGKTILLTTHFMEEAERlCDRLCVLEAGrKIAEGRPH 257
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
294-502 1.75e-22

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 99.00  E-value: 1.75e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 294 TDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEfqhdyLHSKIALVG---QEPVLFAR- 369
Cdd:PRK10851  15 TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSR-----LHARDRKVGfvfQHYALFRHm 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 370 TIKENISYGLSDV------SMEMVVQAATKANAHDFITTLPKGYDTsvgekglQLSGGQKQRVAIARALIRQPRVLILDE 443
Cdd:PRK10851  90 TVFDNIAFGLTVLprrerpNAAAIKAKVTQLLEMVQLAHLADRYPA-------QLSGGQKQRVALARALAVEPQILLLDE 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 961964003 444 ATSALDAESEHIVQQALNSIMQE---HTVLVIAHRLSTVEKADNIIVIDRGQVAERGTHSQL 502
Cdd:PRK10851 163 PFGALDAQVRKELRRWLRQLHEElkfTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
 293-502 2.21e-22

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: 95.51  E-value: 2.21e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 293 ETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGkpvnefqHDylhskialVGQEPvlfaRTIK 372
Cdd:cd03265   12 DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAG-------HD--------VVREP----REVR 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 373 ENISYGLSDVSME--------MVVQAA----TKANAHDFITTLPKGYDtsVGEKGLQL----SGGQKQRVAIARALIRQP 436
Cdd:cd03265   73 RRIGIVFQDLSVDdeltgwenLYIHARlygvPGAERRERIDELLDFVG--LLEAADRLvktySGGMRRRLEIARSLVHRP 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 961964003 437 RVLILDEATSALDAESEHIVQQALNSIMQEH--TVLVIAHRLSTVEK-ADNIIVIDRGQVAERGTHSQL 502
Cdd:cd03265  151 EVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFgmTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
279-502 2.27e-22

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 98.64  E-value: 2.27e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 279 VEFKDVTFAYPTrpeTDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSL---LENfylPQGGQVLLDGKPVNEF---QHDy 352
Cdd:PRK11432   7 VVLKNITKRFGS---NTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLvagLEK---PTEGQIFIDGEDVTHRsiqQRD- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 353 lhskIALVGQEPVLFAR-TIKENISYGLS--DVSMEMVVQAATKANAhdfITTLPKGYDTSVGekglQLSGGQKQRVAIA 429
Cdd:PRK11432  80 ----ICMVFQSYALFPHmSLGENVGYGLKmlGVPKEERKQRVKEALE---LVDLAGFEDRYVD----QISGGQQQRVALA 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 430 RALIRQPRVLILDEATSALDAE-----SEHI--VQQALNSimqehTVLVIAHRLS-TVEKADNIIVIDRGQVAERGTHSQ 501
Cdd:PRK11432 149 RALILKPKVLLFDEPLSNLDANlrrsmREKIreLQQQFNI-----TSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQE 223


                 .
gi 961964003 502 L 502
Cdd:PRK11432 224 L 224
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
 278-492 3.26e-22

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 100.00  E-value: 3.26e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 278 LVEFKDVTFAYPtrpetDV--LKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYlPQG---GQVLLDGKPVnEFQH-- 350
Cdd:PRK13549   5 LLEMKNITKTFG-----GVkaLDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHGtyeGEIIFEGEEL-QASNir 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 351 DYLHSKIALVGQEPVLFAR-TIKENISYGLSDVSMEMVVQAATKANAHDFITTLpkGYDTSVGEKGLQLSGGQKQRVAIA 429
Cdd:PRK13549  78 DTERAGIAIIHQELALVKElSVLENIFLGNEITPGGIMDYDAMYLRAQKLLAQL--KLDINPATPVGNLGLGQQQLVEIA 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 961964003 430 RALIRQPRVLILDEATSALdAESEhiVQQALNSI--MQEHTV--LVIAHRLSTVEK-ADNIIVIDRGQ 492
Cdd:PRK13549 156 KALNKQARLLILDEPTASL-TESE--TAVLLDIIrdLKAHGIacIYISHKLNEVKAiSDTICVIRDGR 220
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
297-502 3.45e-22

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 99.99  E-value: 3.45e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 297 LKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNeFQH--DYLHSKIALVGQE----PVLfarT 370
Cdd:PRK11288  20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMR-FASttAALAAGVAIIYQElhlvPEM---T 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 371 IKENISYGLSDVSMEMVVQAATKANAHDFITTLpkGYDTSVGEKGLQLSGGQKQRVAIARALIRQPRVLILDEATSALDA 450
Cdd:PRK11288  96 VAENLYLGQLPHKGGIVNRRLLNYEAREQLEHL--GVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSA 173

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 961964003 451 -ESEHI--VQQALNSimQEHTVLVIAHRLSTV-EKADNIIVIDRGQVAErgTHSQL 502
Cdd:PRK11288 174 rEIEQLfrVIRELRA--EGRVILYVSHRMEEIfALCDAITVFKDGRYVA--TFDDM 225
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
294-477 3.57e-22

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 95.27  E-value: 3.57e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 294 TDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEF----QHDYLHSKIALVGQepvlFAR 369
Cdd:PRK11629  22 TDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLssaaKAELRNQKLGFIYQ----FHH 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 370 TIKENISygLSDVSMEMVVQAATKANAHDFITTLPK--GYDTSVGEKGLQLSGGQKQRVAIARALIRQPRVLILDEATSA 447
Cdd:PRK11629  98 LLPDFTA--LENVAMPLLIGKKKPAEINSRALEMLAavGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGN 175

                        170       180       190
                 ....*....|....*....|....*....|..
gi 961964003 448 LDAESEHIVQQALNSIMQEH--TVLVIAHRLS 477
Cdd:PRK11629 176 LDARNADSIFQLLGELNRLQgtAFLVVTHDLQ 207
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
293-504 4.57e-22

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 95.81  E-value: 4.57e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 293 ETDVLKGVSFTLRPGEVTALVGPSGSGKSS---CVSLLENfylPQGGQVLLDGKPVN-------------EFQHDYLHSK 356
Cdd:PRK10619  17 EHEVLKGVSLQANAGDVISIIGSSGSGKSTflrCINFLEK---PSEGSIVVNGQTINlvrdkdgqlkvadKNQLRLLRTR 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 357 IALVGQEPVLFAR-TIKENIsyglsdvsMEMVVQ--AATKANAHD-FITTLPK-GYDTSV-GEKGLQLSGGQKQRVAIAR 430
Cdd:PRK10619  94 LTMVFQHFNLWSHmTVLENV--------MEAPIQvlGLSKQEARErAVKYLAKvGIDERAqGKYPVHLSGGQQQRVSIAR 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 431 ALIRQPRVLILDEATSALDAEsehIVQQALNsIMQE-----HTVLVIAHRLSTVEKADN-IIVIDRGQVAERGTHSQLMA 504
Cdd:PRK10619 166 ALAMEPEVLLFDEPTSALDPE---LVGEVLR-IMQQlaeegKTMVVVTHEMGFARHVSShVIFLHQGKIEEEGAPEQLFG 241
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
287-488 4.90e-22

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 93.84  E-value: 4.90e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 287 AYPTRPetdVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGkpvnefqhdylHSKIALVGQ---E 363
Cdd:NF040873   1 GYGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQrseV 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 364 PVLFARTIKENISYGL---------SDVSMEMVVQAATKANAhdfITTLPKgydTSVGEkglqLSGGQKQRVAIARALIR 434
Cdd:NF040873  67 PDSLPLTVRDLVAMGRwarrglwrrLTRDDRAAVDDALERVG---LADLAG---RQLGE----LSGGQRQRALLAQGLAQ 136

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 961964003 435 QPRVLILDEATSALDAESEHIVQQALNsimQEH----TVLVIAHRLSTVEKADNIIVI 488
Cdd:NF040873 137 EADLLLLDEPTTGLDAESRERIIALLA---EEHargaTVVVVTHDLELVRRADPCVLL 191
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
 296-519 5.89e-22

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: 94.92  E-value: 5.89e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 296 VLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNefqHDYLHSK----IALVGQEPVLFAR-T 370
Cdd:cd03218   15 VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDIT---KLPMHKRarlgIGYLPQEASIFRKlT 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 371 IKENISyglsdVSMEMVV----QAATKANA--HDF-ITTLPKgydtsvgEKGLQLSGGQKQRVAIARALIRQPRVLILDE 443
Cdd:cd03218   92 VEENIL-----AVLEIRGlskkEREEKLEEllEEFhITHLRK-------SKASSLSGGERRRVEIARALATNPKFLLLDE 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 444 ATSALD----AESEHIVQQALNSIMqehTVLVIAHRLS-TVEKADNIIVIDRGQVAERGTHSQLMATgglycKLVQRQVL 518
Cdd:cd03218  160 PFAGVDpiavQDIQKIIKILKDRGI---GVLITDHNVReTLSITDRAYIIYEGKVLAEGTPEEIAAN-----ELVRKVYL 231


                 .
gi 961964003 519 G 519
Cdd:cd03218  232 G 232
ABC_6TM_CyaB_HlyB_like cd18588
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ...
 19-223 9.67e-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: 95.64  E-value: 9.67e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  19 GVRGGVFTLTMARLNVRLRSRLFRTLMTQEIAFFDENHTGDILSRL-----------SADTTQVSDLisqnvnVFlrSVI 87
Cdd:cd18588   60 GLRTYLFSHTTNRIDAELGARLFRHLLRLPLSYFESRQVGDTVARVrelesirqfltGSALTLVLDL------VF--SVV 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  88 kgtgFIIFMFRMSWKLTLVTMMGFPFIALVSKLYGEYYKKLTKEVQTVLAEANKVAEETISGMRTVRSFANESREANSYY 167
Cdd:cd18588  132 ----FLAVMFYYSPTLTLIVLASLPLYALLSLLVTPILRRRLEEKFQRGAENQSFLVETVTGIETVKSLAVEPQFQRRWE 207

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 961964003 168 AkllvmfQLNKKQALAYACYMWSSCISELA------LEVAVLYYGGHLVLTDQLSSGGLISF 223
Cdd:cd18588  208 E------LLARYVKASFKTANLSNLASQIVqliqklTTLAILWFGAYLVMDGELTIGQLIAF 263
CeuD COG4604
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ...
 279-503 1.06e-21

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


Pssm-ID: 443654 [Multi-domain]  Cd Length: 252  Bit Score: 94.38  E-value: 1.06e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 279 VEFKDVTFAYPTRPetdVLKGVSFTLRPGEVTALVGPSGSGKS---SCVS-LLEnfylPQGGQVLLDGKPVNEFQHDYLH 354
Cdd:COG4604    2 IEIKNVSKRYGGKV---VLDDVSLTIPKGGITALIGPNGAGKStllSMISrLLP----PDSGEVLVDGLDVATTPSRELA 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 355 SKIALVGQEPVLFAR-TIKENISYG--------LSDVSMEMVVQAATKAN----AHDFITtlpkgydtsvgekglQLSGG 421
Cdd:COG4604   75 KRLAILRQENHINSRlTVRELVAFGrfpyskgrLTAEDREIIDEAIAYLDledlADRYLD---------------ELSGG 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 422 QKQRVAIARALIRQPRVLILDEATSALDAesEHIVQ--QALNSIMQEH--TVLVIAHRLSTVEK-ADNIIVIDRGQVAER 496
Cdd:COG4604  140 QRQRAFIAMVLAQDTDYVLLDEPLNNLDM--KHSVQmmKLLRRLADELgkTVVIVLHDINFASCyADHIVAMKDGRVVAQ 217


                 ....*..
gi 961964003 497 GTHSQLM 503
Cdd:COG4604  218 GTPEEII 224
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
 293-497 1.12e-21

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 94.59  E-value: 1.12e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 293 ETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVS----LLENFYLPQ-GGQVLLDGKPVNEFQHDYLHSKIALVGQEPVLF 367
Cdd:PRK14247  15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRvfnrLIELYPEARvSGEVYLDGQDIFKMDVIELRRRVQMVFQIPNPI 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 368 AR-TIKENISYGLSDVSM--------EMVVQAATKANAHDFITTlpkgydtSVGEKGLQLSGGQKQRVAIARALIRQPRV 438
Cdd:PRK14247  95 PNlSIFENVALGLKLNRLvkskkelqERVRWALEKAQLWDEVKD-------RLDAPAGKLSGGQQQRLCIARALAFQPEV 167

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 439 LILDEATSALDAESEHIVQQALNSIMQEHTVLVIAHRLSTVEK-ADNIIVIDRGQVAERG 497
Cdd:PRK14247 168 LLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARiSDYVAFLYKGQIVEWG 227
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
 294-504 1.36e-21

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: 99.60  E-value: 1.36e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   294 TDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKpvnefqhdylhskIALVGQEPVLFARTIKE 373
Cdd:TIGR01271  439 TPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQTSWIMPGTIKD 505

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   374 NISYGLS--DVSMEMVVQAAtkaNAHDFITTLPKGYDTSVGEKGLQLSGGQKQRVAIARALIRQPRVLILDEATSALDAE 451
Cdd:TIGR01271  506 NIIFGLSydEYRYTSVIKAC---QLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVV 582

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 961964003   452 SE-HIVQQALNSIMQEHTVLVIAHRLSTVEKADNIIVIDRGQVAERGTHSQLMA 504
Cdd:TIGR01271  583 TEkEIFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQA 636
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
 288-497 1.65e-21

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 94.00  E-value: 1.65e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 288 YPTRPetdVLKGVSFTLRPGEVTALVGPSGSGKS-SCVSLLEnfYLPQG-----GQVLLDGKPVNEfqHDYLHSKIALVG 361
Cdd:PRK10418  13 QAAQP---LVHGVSLTLQRGRVLALVGGSGSGKSlTCAAALG--ILPAGvrqtaGRVLLDGKPVAP--CALRGRKIATIM 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 362 QEP-VLF--ARTIKENISYGL-------SDVSMEMVVQAATKANAHDFITTLPkgydtsvgekgLQLSGGQKQRVAIARA 431
Cdd:PRK10418  86 QNPrSAFnpLHTMHTHARETClalgkpaDDATLTAALEAVGLENAARVLKLYP-----------FEMSGGMLQRMMIALA 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 961964003 432 LIRQPRVLILDEATSALDAESEHIVQQALNSIMQEHT--VLVIAHRLSTVEK-ADNIIVIDRGQVAERG 497
Cdd:PRK10418 155 LLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVARlADDVAVMSHGRIVEQG 223
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
 290-467 2.32e-21

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 92.24  E-value: 2.32e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 290 TRPETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHD----YLHSKIALvgqEPV 365
Cdd:PRK13539  11 VRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAeachYLGHRNAM---KPA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 366 LfarTIKENIS-----YGLSDVSmemvVQAATKANAHDFITTLPKGYdtsvgekglqLSGGQKQRVAIARALIRQPRVLI 440
Cdd:PRK13539  88 L---TVAENLEfwaafLGGEELD----IAAALEAVGLAPLAHLPFGY----------LSAGQKRRVALARLLVSNRPIWI 150

                        170       180
                 ....*....|....*....|....*..
gi 961964003 441 LDEATSALDAESehivQQALNSIMQEH 467
Cdd:PRK13539 151 LDEPTAALDAAA----VALFAELIRAH 173
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 284-493 6.53e-21

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


Pssm-ID: 440718 [Multi-domain]  Cd Length: 264  Bit Score: 92.46  E-value: 6.53e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 284 VTFAYPTRPETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNeFQHDYLHSK-IALVGQ 362
Cdd:COG1101    9 KTFNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVT-KLPEYKRAKyIGRVFQ 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 363 EPVL--FAR-TIKENIS--------YGLSdvsmemvvQAATKANAHDF---ITTLPKGY----DTSVGekglQLSGGQKQ 424
Cdd:COG1101   88 DPMMgtAPSmTIEENLAlayrrgkrRGLR--------RGLTKKRRELFrelLATLGLGLenrlDTKVG----LLSGGQRQ 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 961964003 425 RVAIARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQEH--TVLVIAHRLS-TVEKADNIIVIDRGQV 493
Cdd:COG1101  156 ALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENnlTTLMVTHNMEqALDYGNRLIMMHEGRI 227
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
 299-491 7.11e-21

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


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 92.36  E-value: 7.11e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 299 GVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKP--------------VNEFQHDYLHSKIALVgqEP 364
Cdd:PRK11300  23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHieglpghqiarmgvVRTFQHVRLFREMTVI--EN 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 365 VLFA--RTIKENISYGL------SDVSMEMVVQAAT---KANAHDFITTlpkgydtsvgEKGlQLSGGQKQRVAIARALI 433
Cdd:PRK11300 101 LLVAqhQQLKTGLFSGLlktpafRRAESEALDRAATwleRVGLLEHANR----------QAG-NLAYGQQRRLEIARCMV 169

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 961964003 434 RQPRVLILDEATSALDAESEHIVQQALNSIMQEH--TVLVIAHRLSTV-EKADNIIVIDRG 491
Cdd:PRK11300 170 TQPEILMLDEPAAGLNPKETKELDELIAELRNEHnvTVLLIEHDMKLVmGISDRIYVVNQG 230
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
279-498 7.58e-21

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


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 94.14  E-value: 7.58e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 279 VEFKDVTFAYPTRpeTDVLKGVSFTLRPGEVTALVGPSGSGKSSC---VSLLENFylpQGGQVLLDGKPVNEfqhdyLHS 355
Cdd:PRK11650   4 LKLQAVRKSYDGK--TQVIKGIDLDVADGEFIVLVGPSGCGKSTLlrmVAGLERI---TSGEIWIGGRVVNE-----LEP 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 356 K---IALVGQEPVLFAR-TIKENISYGLSDVSM------EMVVQAATKANAHDFITTLPKgydtsvgekglQLSGGQKQR 425
Cdd:PRK11650  74 AdrdIAMVFQNYALYPHmSVRENMAYGLKIRGMpkaeieERVAEAARILELEPLLDRKPR-----------ELSGGQRQR 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 426 VAIARALIRQPRVLILDEATSALDAESEhiVQQALnSIMQEHtvlviaHRLST---------VEK---ADNIIVIDRGQV 493
Cdd:PRK11650 143 VAMGRAIVREPAVFLFDEPLSNLDAKLR--VQMRL-EIQRLH------RRLKTtslyvthdqVEAmtlADRVVVMNGGVA 213


                 ....*
gi 961964003 494 AERGT 498
Cdd:PRK11650 214 EQIGT 218
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
 295-493 7.71e-21

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: 90.18  E-value: 7.71e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 295 DVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQ-HDYLHSKIALV----GQEPVLFAR 369
Cdd:cd03215   14 GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSpRDAIRAGIAYVpedrKREGLVLDL 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 370 TIKENIsyglsdvsmemvvqaatkanahdfitTLPkgydtsvgekgLQLSGGQKQRVAIARALIRQPRVLILDEATSALD 449
Cdd:cd03215   94 SVAENI--------------------------ALS-----------SLLSGGNQQKVVLARWLARDPRVLILDEPTRGVD 136

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 961964003 450 AESEHIVQQALNSIMQE-HTVLVIAHRLSTV-EKADNIIVIDRGQV 493
Cdd:cd03215  137 VGAKAEIYRLIRELADAgKAVLLISSELDELlGLCDRILVMYEGRI 182
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
 279-489 1.02e-20

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: 89.14  E-value: 1.02e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 279 VEFKDVTFAYPTrpETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVlldGKPVnefqhdylHSKIA 358
Cdd:cd03223    1 IELENLSLATPD--GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI---GMPE--------GEDLL 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 359 LVGQEPVLFARTIKENISYGLSDVsmemvvqaatkanahdfittlpkgydtsvgekglqLSGGQKQRVAIARALIRQPRV 438
Cdd:cd03223   68 FLPQRPYLPLGTLREQLIYPWDDV-----------------------------------LSGGEQQRLAFARLLLHKPKF 112

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 961964003 439 LILDEATSALDAESEhivqQALNSIMQEH--TVLVIAHRlSTVEK-ADNIIVID 489
Cdd:cd03223  113 VFLDEATSALDEESE----DRLYQLLKELgiTVISVGHR-PSLWKfHDRVLDLD 161
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
 295-494 1.13e-20

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: 90.79  E-value: 1.13e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 295 DVLKGVSFTLRPGEVTALVGPSGSGKSSCVSL----LENFYLpQGGQVLLDGKPVN--EF--------QHDYLHSKIalv 360
Cdd:cd03234   21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAisgrVEGGGT-TSGQILFNGQPRKpdQFqkcvayvrQDDILLPGL--- 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 361 gqepvlfarTIKENISYGL---------SDVSMEMVVQAATKANAHdfittlpkgydTSVGEKGLQ-LSGGQKQRVAIAR 430
Cdd:cd03234   97 ---------TVRETLTYTAilrlprkssDAIRKKRVEDVLLRDLAL-----------TRIGGNLVKgISGGERRRVSIAV 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 961964003 431 ALIRQPRVLILDEATSALDAESEHIVQQALNSIMQEH-TVLVIAH--RLSTVEKADNIIVIDRGQVA 494
Cdd:cd03234  157 QLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNrIVILTIHqpRSDLFRLFDRILLLSSGEIV 223
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
278-475 1.17e-20

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 90.70  E-value: 1.17e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 278 LVEFKDVTFAYPTRPETdvLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHD---YLH 354
Cdd:PRK10908   1 MIRFEHVSKAYLGGRQA--LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNRevpFLR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 355 SKIALVGQEP-VLFARTIKENisyglsdVSMEMVVQAATKAN-------AHDFITTLPKGYDTSVgekglQLSGGQKQRV 426
Cdd:PRK10908  79 RQIGMIFQDHhLLMDRTVYDN-------VAIPLIIAGASGDDirrrvsaALDKVGLLDKAKNFPI-----QLSGGEQQRV 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 961964003 427 AIARALIRQPRVLILDEATSALD-AESEHIVQ--QALNSI-----MQEHTVLVIAHR 475
Cdd:PRK10908 147 GIARAVVNKPAVLLADEPTGNLDdALSEGILRlfEEFNRVgvtvlMATHDIGLISRR 203
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
 294-502 1.56e-20

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: 91.84  E-value: 1.56e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 294 TDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKpvnefqhdylhskIALVGQEPVLFARTIKE 373
Cdd:cd03291   50 APVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQFSWIMPGTIKE 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 374 NISYGLS--DVSMEMVVQAAtkaNAHDFITTLPKGYDTSVGEKGLQLSGGQKQRVAIARALIRQPRVLILDEATSALDAE 451
Cdd:cd03291  117 NIIFGVSydEYRYKSVVKAC---QLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVF 193

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 961964003 452 SE-HIVQQALNSIMQEHTVLVIAHRLSTVEKADNIIVIDRGQVAERGTHSQL 502
Cdd:cd03291  194 TEkEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
BtuD COG4138
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ...
 297-503 1.75e-20

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


Pssm-ID: 443313 [Multi-domain]  Cd Length: 248  Bit Score: 91.06  E-value: 1.75e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 297 LKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFyLPQGGQVLLDGKPVNEFQHDYLHSKIA-LVGQEPVLFARTIKENI 375
Cdd:COG4138   12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSAAELARHRAyLSQQQSPPFAMPVFQYL 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 376 SYGLSDVSMEMVVQAATKANAHDFitTLPKGYDTSVGekglQLSGGQKQRVAIARALIR-------QPRVLILDEATSAL 448
Cdd:COG4138   91 ALHQPAGASSEAVEQLLAQLAEAL--GLEDKLSRPLT----QLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSL 164

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 961964003 449 DaesehIVQQ-ALNSIMQEH-----TVLVIAHRLS-TVEKADNIIVIDRGQVAERGTHSQLM 503
Cdd:COG4138  165 D-----VAQQaALDRLLRELcqqgiTVVMSSHDLNhTLRHADRVWLLKQGKLVASGETAEVM 221
ABC_6TM_CvaB_RaxB_like cd18567
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ...
 7-226 1.80e-20

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: 91.75  E-value: 1.80e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   7 FTLFFLLSSMAIGVRGGVFTLTMARLNVRLRSRLFRTLMTQEIAFFDENHTGDILSRLSAdTTQVSDLISQNvnvFLRSV 86
Cdd:cd18567   48 FGLLLLLQALLSALRSWLVLYLSTSLNLQWTSNLFRHLLRLPLSYFEKRHLGDIVSRFGS-LDEIQQTLTTG---FVEAL 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  87 IKG---TGFIIFMFRMSWKLTLVTMMGFPFIALVSKLYGEYYKKLTKEVQTVLAEANKVAEETISGMRTVRSFANES-RE 162
Cdd:cd18567  124 LDGlmaILTLVMMFLYSPKLALIVLAAVALYALLRLALYPPLRRATEEQIVASAKEQSHFLETIRGIQTIKLFGREAeRE 203

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 163 A---NSYYAKLLVMFQLNKKQalayacyMWSSCISEL--ALE-VAVLYYGGHLVLTDQLSSGGLISFFIY 226
Cdd:cd18567  204 ArwlNLLVDAINADIRLQRLQ-------ILFSAANGLlfGLEnILVIYLGALLVLDGEFTVGMLFAFLAY 266
cbiO PRK13649
energy-coupling factor transporter ATPase;
279-502 1.89e-20

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 91.73  E-value: 1.89e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 279 VEFKDVTFAYP--TRPETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHD----Y 352
Cdd:PRK13649   3 INLQNVSYTYQagTPFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNkdikQ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 353 LHSKIALVGQ--EPVLFARTIKENISYGLSD--VSMEMVVQAATKANAHdfittlpKGYDTSVGEKG-LQLSGGQKQRVA 427
Cdd:PRK13649  83 IRKKVGLVFQfpESQLFEETVLKDVAFGPQNfgVSQEEAEALAREKLAL-------VGISESLFEKNpFELSGGQMRRVA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 428 IARALIRQPRVLILDEATSALDAESehivQQALNSIMQE-H----TVLVIAHRLSTV-EKADNIIVIDRGQVAERGTHSQ 501
Cdd:PRK13649 156 IAGILAMEPKILVLDEPTAGLDPKG----RKELMTLFKKlHqsgmTIVLVTHLMDDVaNYADFVYVLEKGKLVLSGKPKD 231


                 .
gi 961964003 502 L 502
Cdd:PRK13649 232 I 232
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
 14-519 2.24e-20

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: 95.75  E-value: 2.24e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003    14 SSMAIGV-RGGVFTLTMARLNVRLRSRLFRTLMTQEIAFFDENHTGDILSRLSADTTQVSDLISQNVNVFLRSVIKGTGf 92
Cdd:TIGR01271  937 SVLALGFfRGLPLVHTLLTVSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLG- 1015

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003    93 IIFMFRMSWKLTLVTMMGFPFIALVSKLY----GEYYKKLTKEVQTVLAEANKVaeeTISGMRTVRSFANESreansyYA 168
Cdd:TIGR01271 1016 AIFVVSVLQPYIFIAAIPVAVIFIMLRAYflrtSQQLKQLESEARSPIFSHLIT---SLKGLWTIRAFGRQS------YF 1086

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   169 KLLVMFQLNKKQA---LAYACYMWSSCISELaleVAVLYYGGHL---VLTDQLSSGGL-ISFFIYMLELGECFESIASVY 241
Cdd:TIGR01271 1087 ETLFHKALNLHTAnwfLYLSTLRWFQMRIDI---IFVFFFIAVTfiaIGTNQDGEGEVgIILTLAMNILSTLQWAVNSSI 1163

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   242 S--GLMQGVgaaEKVFEYLDRKPK--HPADGTEAPNSCTGLV-EFKDVTFAYPTRPETDV--------------LKGVSF 302
Cdd:TIGR01271 1164 DvdGLMRSV---SRVFKFIDLPQEepRPSGGGGKYQLSTVLViENPHAQKCWPSGGQMDVqgltakyteagravLQDLSF 1240

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   303 TLRPGEVTALVGPSGSGKSSCVSLLENFyLPQGGQVLLDGKPVNEFQHDYLHSKIALVGQEPVLFARTIKENISyGLSDV 382
Cdd:TIGR01271 1241 SVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLD-PYEQW 1318

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   383 SMEMVVQAATKANAHDFITTLPKGYDTSVGEKGLQLSGGQKQRVAIARALIRQPRVLILDEATSALDAESEHIVQQALNS 462
Cdd:TIGR01271 1319 SDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQ 1398

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 961964003   463 IMQEHTVLVIAHRLSTVEKADNIIVIDRGQVAERGTHSQLMATGGLYcklvqRQVLG 519
Cdd:TIGR01271 1399 SFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLF-----KQAMS 1450
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
 278-495 2.52e-20

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 94.36  E-value: 2.52e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 278 LVEFKDVTFAYPTRPetdVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLdGKPVNE--F--QHDYL 353
Cdd:COG0488  315 VLELEGLSKSYGDKT---LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVKIgyFdqHQEEL 390

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 354 HSKialvgqepvlfaRTIKENISYGLSDvsmemvvqaATKANAHDFITT-LPKGYD--TSVGEkglqLSGGQKQRVAIAR 430
Cdd:COG0488  391 DPD------------KTVLDELRDGAPG---------GTEQEVRGYLGRfLFSGDDafKPVGV----LSGGEKARLALAK 445

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 961964003 431 ALIRQPRVLILDEATSALDAESEHIVQQALNSImqEHTVLVIAH-R--LSTVekADNIIVIDRGQVAE 495
Cdd:COG0488  446 LLLSPPNVLLLDEPTNHLDIETLEALEEALDDF--PGTVLLVSHdRyfLDRV--ATRILEFEDGGVRE 509
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
 279-492 2.74e-20

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: 87.12  E-value: 2.74e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 279 VEFKDVTFAYPTRPetdVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKpvnefqhdylhskia 358
Cdd:cd03221    1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST--------------- 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 359 lvgqepvlfartikENISYglsdvsmemvvqaatkanahdfittLPkgydtsvgekglQLSGGQKQRVAIARALIRQPRV 438
Cdd:cd03221   63 --------------VKIGY-------------------------FE------------QLSGGEKMRLALAKLLLENPNL 91

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 961964003 439 LILDEATSALDAESEHIVQQALNSimQEHTVLVIAH-R--LSTVekADNIIVIDRGQ 492
Cdd:cd03221   92 LLLDEPTNHLDLESIEALEEALKE--YPGTVILVSHdRyfLDQV--ATKIIELEDGK 144
ABC_6TM_Tm287_like cd18548
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ...
 36-227 2.89e-20

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: 91.31  E-value: 2.89e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  36 LRSRLFRTLMTQEIAFFDENHTGDILSRLSADTTQVSDLISQNVNVFLRSVIKGTGFIIFMFRMSWKLTLVTMMGFPFIA 115
Cdd:cd18548   74 LRKDLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPILA 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 116 LV----SKLYGEYYKKltkeVQTVLAEANKVAEETISGMRTVRSFANESRE------ANSYYAKLlvMFQLNKKQALAYA 185
Cdd:cd18548  154 LVvfliMKKAIPLFKK----VQKKLDRLNRVVRENLTGIRVIRAFNREDYEeerfdkANDDLTDT--SLKAGRLMALLNP 227

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 961964003 186 CYMwssCISELALeVAVLYYGGHLVLTDQLSSGGLISFFIYM 227
Cdd:cd18548  228 LMM---LIMNLAI-VAILWFGGHLINAGSLQVGDLVAFINYL 265
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
 296-505 3.19e-20

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 94.00  E-value: 3.19e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 296 VLKGVSFTLRPGEVTALVGPSGSGKS-SCVSLLEnfYLPQ------GGQVLLDGKPVnefqhdyLHS-----------KI 357
Cdd:PRK15134  24 VVNDVSLQIEAGETLALVGESGSGKSvTALSILR--LLPSppvvypSGDIRFHGESL-------LHAseqtlrgvrgnKI 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 358 ALVGQEPVLFARTIkENISYGLSDV-----SM-------EMVV--------QAATKANahDFittlPKgydtsvgekglQ 417
Cdd:PRK15134  95 AMIFQEPMVSLNPL-HTLEKQLYEVlslhrGMrreaargEILNcldrvgirQAAKRLT--DY----PH-----------Q 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 418 LSGGQKQRVAIARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQE--HTVLVIAHRLSTVEK-ADNIIVIDRGQVA 494
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElnMGLLFITHNLSIVRKlADRVAVMQNGRCV 236

                        250
                 ....*....|.
gi 961964003 495 ERGTHSQLMAT 505
Cdd:PRK15134 237 EQNRAATLFSA 247
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
282-523 4.57e-20

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 90.23  E-value: 4.57e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 282 KDVTFAYPTRPetdVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHDYLHSKIALVG 361
Cdd:PRK10575  15 RNVSFRVPGRT---LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLP 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 362 QE-PVLFARTIKENIS------------YGLSDvsMEMVVQAAT----KANAHDFITTlpkgydtsvgekglqLSGGQKQ 424
Cdd:PRK10575  92 QQlPAAEGMTVRELVAigrypwhgalgrFGAAD--REKVEEAISlvglKPLAHRLVDS---------------LSGGERQ 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 425 RVAIARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQEHTVLVIA--HRLSTVEK-ADNIIVIDRGQVAERGTHSQ 501
Cdd:PRK10575 155 RAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAvlHDINMAARyCDYLVALRGGEMIAQGTPAE 234

                        250       260
                 ....*....|....*....|..
gi 961964003 502 LMatgglyCKLVQRQVLGIETG 523
Cdd:PRK10575 235 LM------RGETLEQIYGIPMG 250
PTZ00243 PTZ00243
ABC transporter; Provisional
 265-505 4.75e-20

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 94.85  E-value: 4.75e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  265 PADGTEAPNSCTGLVEFKDVTFAYPTRPETDVLKGVSFTLRPGEVTALVGPSGSGKSSCV-SLLENFYLpQGGQVLLDgk 343
Cdd:PTZ00243  644 GGGHEATPTSERSAKTPKMKTDDFFELEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLqSLLSQFEI-SEGRVWAE-- 720

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  344 pvnefqhdylhSKIALVGQEPVLFARTIKENISY-------GLSDVSMEMVVQAAtkanahdfITTLPKGYDTSVGEKGL 416
Cdd:PTZ00243  721 -----------RSIAYVPQQAWIMNATVRGNILFfdeedaaRLADAVRVSQLEAD--------LAQLGGGLETEIGEKGV 781

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  417 QLSGGQKQRVAIARALIRQPRVLILDEATSALDAE-SEHIVQQALNSIMQEHTVLVIAHRLSTVEKADNIIVIDRGQVAE 495
Cdd:PTZ00243  782 NLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHvGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEF 861

                         250
                  ....*....|
gi 961964003  496 RGTHSQLMAT 505
Cdd:PTZ00243  862 SGSSADFMRT 871
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
297-503 8.32e-20

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


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 91.63  E-value: 8.32e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 297 LKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHDYLHS----KIALVGQEPVLFAR-TI 371
Cdd:PRK10070  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFALMPHmTV 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 372 KENISYG--LSDVSMEMVVQAATKANAHDFITTLPKGYDTsvgekglQLSGGQKQRVAIARALIRQPRVLILDEATSALD 449
Cdd:PRK10070 124 LDNTAFGmeLAGINAEERREKALDALRQVGLENYAHSYPD-------ELSGGMRQRVGLARALAINPDILLMDEAFSALD 196

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 961964003 450 AESEHIVQQALNSIMQEH--TVLVIAHRLSTVEK-ADNIIVIDRGQVAERGTHSQLM 503
Cdd:PRK10070 197 PLIRTEMQDELVKLQAKHqrTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEIL 253
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
 288-443 8.85e-20

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


Pssm-ID: 440752 [Multi-domain]  Cd Length: 240  Bit Score: 88.55  E-value: 8.85e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 288 YPTRPetdVLKGVSFTLRPGEVTALVGPSGSGKSSCvsllenFYL------PQGGQVLLDGKPVNefqHDYLHsKIALVG 361
Cdd:COG1137   13 YGKRT---VVKDVSLEVNQGEIVGLLGPNGAGKTTT------FYMivglvkPDSGRIFLDGEDIT---HLPMH-KRARLG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 362 -----QEPVLFAR-TIKENISyglsdVSMEMVV----QAATKANA--HDF-ITTLPKgydtsvgEKGLQLSGGQKQRVAI 428
Cdd:COG1137   80 igylpQEASIFRKlTVEDNIL-----AVLELRKlskkEREERLEEllEEFgITHLRK-------SKAYSLSGGERRRVEI 147

                        170
                 ....*....|....*
gi 961964003 429 ARALIRQPRVLILDE 443
Cdd:COG1137  148 ARALATNPKFILLDE 162
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 297-513 2.70e-19

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


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 88.99  E-value: 2.70e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 297 LKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGK-PVNEfQHDYLHsKIALV-GQE-------PVL- 366
Cdd:COG4586   38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYvPFKR-RKEFAR-RIGVVfGQRsqlwwdlPAId 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 367 -FaRTIKEnIsYGLSDvsmemvvqAATKANAHDFITTLpkgydtSVGEKgL-----QLSGGQKQRVAIARALIRQPRVLI 440
Cdd:COG4586  116 sF-RLLKA-I-YRIPD--------AEYKKRLDELVELL------DLGEL-LdtpvrQLSLGQRMRCELAAALLHRPKILF 177

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 961964003 441 LDEATSALDAESEHIVQQALNSIMQEH--TVLVIAHRLSTVEK-ADNIIVIDRGQVAERGTHSQLMATGGLYCKLV 513
Cdd:COG4586  178 LDEPTIGLDVVSKEAIREFLKEYNRERgtTILLTSHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKERFGPYKTIV 253
PRK10522 PRK10522
multidrug transporter membrane component/ATP-binding component; Provisional
 279-495 4.33e-19

multidrug transporter membrane component/ATP-binding component; Provisional


Pssm-ID: 236707 [Multi-domain]  Cd Length: 547  Bit Score: 90.42  E-value: 4.33e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 279 VEFKDVTFAYPTrpETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHDYLHSKIA 358
Cdd:PRK10522 323 LELRNVTFAYQD--NGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFS 400

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 359 LVGQEPVLFARTI-KENisyglsdvsmemvvQAATKANAHDFITTLPKGYDTSVGE---KGLQLSGGQKQRVAIARALIR 434
Cdd:PRK10522 401 AVFTDFHLFDQLLgPEG--------------KPANPALVEKWLERLKMAHKLELEDgriSNLKLSKGQKKRLALLLALAE 466

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 961964003 435 QPRVLILDEATSALDAESEHIVQQALNSIMQE--HTVLVIAHRLSTVEKADNIIVIDRGQVAE 495
Cdd:PRK10522 467 ERDILLLDEWAADQDPHFRREFYQVLLPLLQEmgKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
cbiO PRK13645
energy-coupling factor transporter ATPase;
285-512 4.71e-19

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 87.76  E-value: 4.71e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 285 TFAYPTRPETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDG-------KPVNEFQHdyLHSKI 357
Cdd:PRK13645  15 TYAKKTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipanlKKIKEVKR--LRKEI 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 358 ALVGQEP--VLFARTIKENISYGLSDVSmEMVVQAATKANAHDFITTLPKGYdtsVGEKGLQLSGGQKQRVAIARALIRQ 435
Cdd:PRK13645  93 GLVFQFPeyQLFQETIEKDIAFGPVNLG-ENKQEAYKKVPELLKLVQLPEDY---VKRSPFELSGGQKRRVALAGIIAMD 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 436 PRVLILDEATSALDAESEHIVQQALNSIMQEHT--VLVIAHRLSTVEK-ADNIIVIDRGQVAERGTHSQLMATGGLYCKL 512
Cdd:PRK13645 169 GNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKkrIIMVTHNMDQVLRiADEVIVMHEGKVISIGSPFEIFSNQELLTKI 248
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
282-507 4.84e-19

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 90.08  E-value: 4.84e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 282 KDVTFAYPTRPETD--------------VLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNe 347
Cdd:COG1129  239 RELEDLFPKRAAAPgevvleveglsvggVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVR- 317

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 348 fqhdyLHS-------KIALV----GQEPVLFARTIKENISYG-LSDVSMEMVV-QAATKANAHDFITTL---PKGYDTSV 411
Cdd:COG1129  318 -----IRSprdairaGIAYVpedrKGEGLVLDLSIRENITLAsLDRLSRGGLLdRRRERALAEEYIKRLrikTPSPEQPV 392

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 412 GekglQLSGGQKQRVAIARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQE-HTVLVIahrlST-----VEKADNI 485
Cdd:COG1129  393 G----NLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEgKAVIVI----SSelpelLGLSDRI 464

                        250       260
                 ....*....|....*....|....*....
gi 961964003 486 IVIDRGQVA-----ERGTHSQLM--ATGG 507
Cdd:COG1129  465 LVMREGRIVgeldrEEATEEAIMaaATGG 493
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
 296-505 5.63e-19

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 86.64  E-value: 5.63e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 296 VLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFY------LPQGGQVLLDGKPVNEFQHDYLHSKIALVGQEPVLFAR 369
Cdd:PRK14246  25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIeiydskIKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNPFPH 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 370 -TIKENISYGLSDVSMEMVVQAATKANAHDFITTLPKGYDTSVGEKGLQLSGGQKQRVAIARALIRQPRVLILDEATSAL 448
Cdd:PRK14246 105 lSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMI 184

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 961964003 449 DAESEHIVQQALNSIMQEHTVLVIAHRLSTVEK-ADNIIVIDRGQVAERGTHSQLMAT 505
Cdd:PRK14246 185 DIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIFTS 242
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
 286-493 8.25e-19

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: 85.85  E-value: 8.25e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 286 FAYPTRPETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHDYLHsKIALV-GQE- 363
Cdd:cd03267   26 LFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLR-RIGVVfGQKt 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 364 ------PVLFARTIKENIsYGLSDvsmemvvqAATKANAHDFITTLPKG--YDTSVgekgLQLSGGQKQRVAIARALIRQ 435
Cdd:cd03267  105 qlwwdlPVIDSFYLLAAI-YDLPP--------ARFKKRLDELSELLDLEelLDTPV----RQLSLGQRMRAEIAAALLHE 171

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 961964003 436 PRVLILDEATSALDAESEHIVQQALNSIMQEH--TVLVIAHRLSTVEK-ADNIIVIDRGQV 493
Cdd:cd03267  172 PEILFLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEAlARRVLVIDKGRL 232
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
 296-497 1.39e-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: 84.12  E-value: 1.39e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 296 VLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENF--YLPQGGQVLLDGK-----PVNEfqhdylhskIALVG-----QE 363
Cdd:cd03217   15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEditdlPPEE---------RARLGiflafQY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 364 PVLFartikenisyglSDVSMEmvvqaatkanahDFITTLPKGydtsvgekglqLSGGQKQRVAIARALIRQPRVLILDE 443
Cdd:cd03217   86 PPEI------------PGVKNA------------DFLRYVNEG-----------FSGGEKKRNEILQLLLLEPDLAILDE 130

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 961964003 444 ATSALDAESEHIVQQALNSIMQEHT-VLVIAH--RLSTVEKADNIIVIDRGQVAERG 497
Cdd:cd03217  131 PDSGLDIDALRLVAEVINKLREEGKsVLIITHyqRLLDYIKPDRVHVLYDGRIVKSG 187
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
 279-502 2.22e-18

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 85.91  E-value: 2.22e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 279 VEFKDVTFAY----PTrpETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQV---LLDGKP------V 345
Cdd:PRK13651   3 IKVKNIVKIFnkklPT--ELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewiFKDEKNkkktkeK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 346 NEFQHDYLHSK---------------IALVGQ--EPVLFARTIKENISYGlsDVSMEMVVQAAtKANAHDFITTLpkGYD 408
Cdd:PRK13651  81 EKVLEKLVIQKtrfkkikkikeirrrVGVVFQfaEYQLFEQTIEKDIIFG--PVSMGVSKEEA-KKRAAKYIELV--GLD 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 409 TSVGEKG-LQLSGGQKQRVAIARALIRQPRVLILDEATSALDAESehiVQQALNSIMQEH----TVLVIAHRLSTV-EKA 482
Cdd:PRK13651 156 ESYLQRSpFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQG---VKEILEIFDNLNkqgkTIILVTHDLDNVlEWT 232

                        250       260
                 ....*....|....*....|.
gi 961964003 483 DNIIVIDRGQVAERG-THSQL 502
Cdd:PRK13651 233 KRTIFFKDGKIIKDGdTYDIL 253
cbiO PRK13643
energy-coupling factor transporter ATPase;
278-502 3.63e-18

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 85.17  E-value: 3.63e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 278 LVEFKDVTFAY-PTRP-ETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHDY--- 352
Cdd:PRK13643   1 MIKFEKVNYTYqPNSPfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeik 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 353 -LHSKIALVGQEP--VLFARTIKENISYGLSDVSMEMVVQAATKANAHDFIttlpkGYDTSVGEKG-LQLSGGQKQRVAI 428
Cdd:PRK13643  81 pVRKKVGVVFQFPesQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMV-----GLADEFWEKSpFELSGGQMRRVAI 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 961964003 429 ARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQE-HTVLVIAHRLSTV-EKADNIIVIDRGQVAERGTHSQL 502
Cdd:PRK13643 156 AGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSgQTVVLVTHLMDDVaDYADYVYLLEKGHIISCGTPSDV 231
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
 283-449 8.00e-18

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 85.66  E-value: 8.00e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 283 DVTFAyptrpETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHDYLHSKIALVGQ 362
Cdd:PRK09536  10 SVEFG-----DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQ 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 363 EPVL-FARTIKENISYG----------LSDVSMEMVVQAATKANAHDFIttlpkgyDTSVGEkglqLSGGQKQRVAIARA 431
Cdd:PRK09536  85 DTSLsFEFDVRQVVEMGrtphrsrfdtWTETDRAAVERAMERTGVAQFA-------DRPVTS----LSGGERQRVLLARA 153

                        170
                 ....*....|....*...
gi 961964003 432 LIRQPRVLILDEATSALD 449
Cdd:PRK09536 154 LAQATPVLLLDEPTASLD 171
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
 277-493 8.52e-18

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: 83.75  E-value: 8.52e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 277 GLVEFKDVTFAYpTRPETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFyLPQGGQVLLDGKPVNEFQHDYLHSK 356
Cdd:cd03289    1 GQMTVKDLTAKY-TEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL-LNTEGDIQIDGVSWNSVPLQKWRKA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 357 IALVGQEPVLFARTIKENIS-YG-LSDvsmEMVVQAATKANAHDFITTLPKGYDTSVGEKGLQLSGGQKQRVAIARALIR 434
Cdd:cd03289   79 FGVIPQKVFIFSGTFRKNLDpYGkWSD---EEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLS 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 961964003 435 QPRVLILDEATSALDAESEHIVQQALNSIMQEHTVLVIAHRLSTVEKADNIIVIDRGQV 493
Cdd:cd03289  156 KAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKV 214
ABC_6TM_exporter_like cd18565
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
 36-230 1.21e-17

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: 83.77  E-value: 1.21e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  36 LRSRLFRTLMTQEIAFFDENHTGDILSRLSADTTQVSDLISQNVNVFLRSVIKGTGFIIFMFRMSWKLTLVTMMGFPFIA 115
Cdd:cd18565   89 LRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNWQLALVALLPVPLII 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 116 LVSKLY----GEYYKKLTKEVqtvlAEANKVAEETISGMRTVRSFANESREA-------NSYY------AKLLVMFqlnk 178
Cdd:cd18565  169 AGTYWFqrriEPRYRAVREAV----GDLNARLENNLSGIAVIKAFTAEDFERervadasEEYRdanwraIRLRAAF---- 240

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 961964003 179 kQALAYAcymwsscISELALeVAVLYYGGHLVL------TDQLSSGGLISFFIYMLEL 230
Cdd:cd18565  241 -FPVIRL-------VAGAGF-VATFVVGGYWVLdgpplfTGTLTVGTLVTFLFYTQRL 289
PvdE COG4615
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...
 4-443 1.28e-17

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


Pssm-ID: 443659 [Multi-domain]  Cd Length: 547  Bit Score: 86.01  E-value: 1.28e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   4 APPFTLFFLLSSMAIGVRGGVFTLTMARLN---VRLRSRLFRTLMTQEIAFFDENHTGDILSRLSADTTQVSDLISQNVN 80
Cdd:COG4615   48 ARLLLLFAGLLVLLLLSRLASQLLLTRLGQhavARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQAFVRLPE 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  81 vFLRSVIKGTGFIIFMFRMSWKL---TLVTMM--GFPFIALVSKLYG-------------EYYKKLT---KEVQTVLAEA 139
Cdd:COG4615  128 -LLQSVALVLGCLAYLAWLSPPLfllTLVLLGlgVAGYRLLVRRARRhlrrareaedrlfKHFRALLegfKELKLNRRRR 206

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 140 NKVAEETISgmRTVRSFANESREANSYYAkllvmfqlnkkqaLAYAcymWSSCISeLALEVAVLYYGGHLVLTDQLSSGG 219
Cdd:COG4615  207 RAFFDEDLQ--PTAERYRDLRIRADTIFA-------------LANN---WGNLLF-FALIGLILFLLPALGWADPAVLSG 267

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 220 LISFFIYM---LElgecfeSIASVYSGLMQGVGAAEKVfEYLDRKP------KHPADGTEAPNSCTGLvEFKDVTFAYPT 290
Cdd:COG4615  268 FVLVLLFLrgpLS------QLVGALPTLSRANVALRKI-EELELALaaaepaAADAAAPPAPADFQTL-ELRGVTYRYPG 339

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 291 RPETD--VLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHDYLHSKIALVGQEPVLFA 368
Cdd:COG4615  340 EDGDEgfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFD 419

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 369 RTikenisYGLSDVSMEMVVQA---------ATKANAHDFITTlpkgydtsvgekglQLSGGQKQRVAIARALIRQPRVL 439
Cdd:COG4615  420 RL------LGLDGEADPARAREllerleldhKVSVEDGRFSTT--------------DLSQGQRKRLALLVALLEDRPIL 479


                 ....
gi 961964003 440 ILDE 443
Cdd:COG4615  480 VFDE 483
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
 296-505 1.55e-17

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 82.84  E-value: 1.55e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 296 VLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFY-----LPQGGQVLLDGKPVNEFQhDYLH--SKIALVGQEPVLFA 368
Cdd:PRK14271  36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNdkvsgYRYSGDVLLGGRSIFNYR-DVLEfrRRVGMLFQRPNPFP 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 369 RTIKENISYGLSdvSMEMVVQAATKANAHDFITT--LPKGYDTSVGEKGLQLSGGQKQRVAIARALIRQPRVLILDEATS 446
Cdd:PRK14271 115 MSIMDNVLAGVR--AHKLVPRKEFRGVAQARLTEvgLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTS 192

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 447 ALDAESEHIVQQALNSIMQEHTVLVIAHRLSTVEK-ADNIIVIDRGQVAERGTHSQLMAT 505
Cdd:PRK14271 193 ALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLFSS 252
ABC_6TM_Sav1866_like cd18554
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ...
 36-254 2.36e-17

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: 82.85  E-value: 2.36e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  36 LRSRLFRTLMTQEIAFFDENHTGDILSRLSADTTQVSDLISQNVNVFLRSVIKGTGFIIFMFRMSWKLTLVTMMGFPFIA 115
Cdd:cd18554   81 IRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLVIFPFYI 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 116 LVSKLYGEYYKKLTKEVQTVLAEANKVAEETISGMRTVRSFANESREANSYYAKLLVMFQLNKKQAlAYACYMWSS--CI 193
Cdd:cd18554  161 LAVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRALKHT-RWNAKTFSAvnTI 239

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 961964003 194 SELAlEVAVLYYGGHLVLTDQLSSGGLISFFIYMLELGECFESIASVYSGLMQGVGAAEKV 254
Cdd:cd18554  240 TDLA-PLLVIGFAAYLVIEGNLTVGTLVAFVGYMERMYSPLRRLVNSFTTLTQSFASMDRV 299
ABC_6TM_HetC_like cd18568
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ...
 7-223 3.32e-17

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: 82.22  E-value: 3.32e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   7 FTLFFLLSSMAIGVRGGVFTLTMARLNVRLRSRLFRTLMTQEIAFFDENHTGDILSRLSaDTTQVSDLISQN-VNVFLRS 85
Cdd:cd18568   48 LLIVGIFQILLSAVRQYLLDYFANRIDLSLLSDFYKHLLSLPLSFFASRKVGDIITRFQ-ENQKIRRFLTRSaLTTILDL 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  86 VikgTGFI--IFMFRMSWKLTLVTMMGFPFIALVSKLYGEYYKKLTKEVQTVLAEANKVAEETISGMRTVRSFANE---- 159
Cdd:cd18568  127 L---MVFIylGLMFYYNLQLTLIVLAFIPLYVLLTLLSSPKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAErpir 203

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 961964003 160 SREANSYYAKLLVMFqlnKKQALAYACYMWSSCISELALeVAVLYYGGHLVLTDQLSSGGLISF 223
Cdd:cd18568  204 WRWENKFAKALNTRF---RGQKLSIVLQLISSLINHLGT-IAVLWYGAYLVISGQLTIGQLVAF 263
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
 286-493 5.28e-17

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: 79.61  E-value: 5.28e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 286 FAYPTRPETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLEN---FYLPQGGQVLLDGKPVNEFQHDYlHSKIALVGQ 362
Cdd:cd03233   12 TTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANrteGNVSVEGDIHYNGIPYKEFAEKY-PGEIIYVSE 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 363 EPVLFAR-TIKENISYglsdvsmemvvqaATKANAHDFIttlpKGydtsvgekglqLSGGQKQRVAIARALIRQPRVLIL 441
Cdd:cd03233   91 EDVHFPTlTVRETLDF-------------ALRCKGNEFV----RG-----------ISGGERKRVSIAEALVSRASVLCW 142

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 961964003 442 DEATSALDAESEHIVQQALNSIMQEH--TVLVIAHRLS--TVEKADNIIVIDRGQV 493
Cdd:cd03233  143 DNSTRGLDSSTALEILKCIRTMADVLktTTFVSLYQASdeIYDLFDKVLVLYEGRQ 198
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
297-502 5.44e-17

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 81.21  E-value: 5.44e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 297 LKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFY----LPQ------GGQVLLDGKPVNEFQHDYLHSkiALVGQEPVL 366
Cdd:PRK09984  20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdkSAGshiellGRTVQREGRLARDIRKSRANT--GYIFQQFNL 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 367 FAR-TIKENISYG--------------LSDVSMEMVVQAATKAN----AHDFITTlpkgydtsvgekglqLSGGQKQRVA 427
Cdd:PRK09984  98 VNRlSVLENVLIGalgstpfwrtcfswFTREQKQRALQALTRVGmvhfAHQRVST---------------LSGGQQQRVA 162

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 961964003 428 IARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQEH--TVLVIAHRLS-TVEKADNIIVIDRGQVAERGTHSQL 502
Cdd:PRK09984 163 IARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDgiTVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQF 240
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
 285-497 5.65e-17

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: 80.27  E-value: 5.65e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 285 TFAYPTRPETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVnefqhdylhSKIAL-VGQE 363
Cdd:cd03220   26 LGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVS---------SLLGLgGGFN 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 364 PVLFARtikENIS-----YGLSDVSMEMVVqaatkanahDFI---TTLPKGYDTSVGEkglqLSGGQKQRVAIARALIRQ 435
Cdd:cd03220   97 PELTGR---ENIYlngrlLGLSRKEIDEKI---------DEIiefSELGDFIDLPVKT----YSSGMKARLAFAIATALE 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 961964003 436 PRVLILDEATSALDAESEHIVQQALNSIMQEHTVLVIA-HRLSTVEK-ADNIIVIDRGQVAERG 497
Cdd:cd03220  161 PDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVsHDPSSIKRlCDRALVLEKGKIRFDG 224
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
279-497 6.77e-17

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 82.38  E-value: 6.77e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 279 VEFKDVTFAYPtrpETDVLKGVSFTLRPGEVTALVGPSGSGKSS---CVSLLENFylpQGGQVLLDGKPVNefqhDYLHS 355
Cdd:PRK11000   4 VTLRNVTKAYG---DVVISKDINLDIHEGEFVVFVGPSGCGKSTllrMIAGLEDI---TSGDLFIGEKRMN----DVPPA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 356 K--IALVGQEPVLFAR-TIKENISYGLSDVSMEM------VVQAATKANAHDFITTLPKGydtsvgekglqLSGGQKQRV 426
Cdd:PRK11000  74 ErgVGMVFQSYALYPHlSVAENMSFGLKLAGAKKeeinqrVNQVAEVLQLAHLLDRKPKA-----------LSGGQRQRV 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 427 AIARALIRQPRVLILDEATSALDAESEhiVQ---------QALNSIMqehtVLVIAHRLSTVEKADNIIVIDRGQVAERG 497
Cdd:PRK11000 143 AIGRTLVAEPSVFLLDEPLSNLDAALR--VQmrieisrlhKRLGRTM----IYVTHDQVEAMTLADKIVVLDAGRVAQVG 216
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
 297-492 9.28e-17

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: 82.95  E-value: 9.28e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  297 LKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYlPQG---GQVLLDGKPVNEfQH--DYLHSKIALVGQEPVLFAR-T 370
Cdd:TIGR02633  17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHGtwdGEIYWSGSPLKA-SNirDTERAGIVIIHQELTLVPElS 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  371 IKENISYGlSDVSME--MVVQAATKANAHDFITTLpKGYDTSVGEKGLQLSGGQKQRVAIARALIRQPRVLILDEATSAL 448
Cdd:TIGR02633  95 VAENIFLG-NEITLPggRMAYNAMYLRAKNLLREL-QLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSL 172

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 961964003  449 DAESEHIVqqaLNSI--MQEHTV--LVIAHRLSTVEK-ADNIIVIDRGQ 492
Cdd:TIGR02633 173 TEKETEIL---LDIIrdLKAHGVacVYISHKLNEVKAvCDTICVIRDGQ 218
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
 297-504 1.48e-16

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 82.36  E-value: 1.48e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 297 LKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPV-NEFQHDYLHSKIALVGQEP----VLFARTI 371
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVvTRSPQDGLANGIVYISEDRkrdgLVLGMSV 347

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 372 KENISY-GLSDVSMEMVV--QAATKANAHDFITTL----PkGYDTSVGEkglqLSGGQKQRVAIARALIRQPRVLILDEA 444
Cdd:PRK10762 348 KENMSLtALRYFSRAGGSlkHADEQQAVSDFIRLFniktP-SMEQAIGL----LSGGNQQKVAIARGLMTRPKVLILDEP 422

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 961964003 445 TSALDAESEHIVQQALNSIMQE--HTVLVIAHRLSTVEKADNIIVIDRGQV-----AERGTHSQLMA 504
Cdd:PRK10762 423 TRGVDVGAKKEIYQLINQFKAEglSIILVSSEMPEVLGMSDRILVMHEGRIsgeftREQATQEKLMA 489
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
299-467 2.18e-16

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 77.92  E-value: 2.18e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 299 GVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHDYlHSKIALVGQEPvlfarTIK------ 372
Cdd:PRK13538  19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEY-HQDLLYLGHQP-----GIKteltal 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 373 ENISYGLS---DVSMEMVVQAATKANAHDFittlpkgYDTSVGekglQLSGGQKQRVAIARALIRQPRVLILDEATSALD 449
Cdd:PRK13538  93 ENLRFYQRlhgPGDDEALWEALAQVGLAGF-------EDVPVR----QLSAGQQRRVALARLWLTRAPLWILDEPFTAID 161

                        170
                 ....*....|....*...
gi 961964003 450 AESehiVQQaLNSIMQEH 467
Cdd:PRK13538 162 KQG---VAR-LEALLAQH 175
ABC_6TM_T1SS_like cd18555
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ...
 1-223 2.25e-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: 79.86  E-value: 2.25e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   1 MSVAPPFTLFFLLSSMAIGVRGGVFTLTMARLNVRLRSRLFRTLMTQEI--------AFFDENHTGDILSRLSaDTTQVS 72
Cdd:cd18555   34 VPGNLNLLNVLGIGILILFLLYGLFSFLRGYIIIKLQTKLDKSLMSDFFehllklpySFFENRSSGDLLFRAN-SNVYIR 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  73 DLISQNVNVFLRSVIKGTGFIIFMFRMSWKLTLVTMMGFPFIALVSKLYGEYYKKLTKEVQTVLAEANKVAEETISGMRT 152
Cdd:cd18555  113 QILSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLLLLLTRKKIKKLNQEEIVAQTKVQSYLTETLYGIET 192

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 961964003 153 VRSFANESR---EANSYYAKLLVMFQlnKKQALAyacyMWSSCISE---LALEVAVLYYGGHLVLTDQLSSGGLISF 223
Cdd:cd18555  193 IKSLGSEKNiykKWENLFKKQLKAFK--KKERLS----NILNSISSsiqFIAPLLILWIGAYLVINGELTLGELIAF 263
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
 291-502 2.29e-16

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 82.21  E-value: 2.29e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 291 RPETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGK----------PVNEFQHDYLH----SK 356
Cdd:PRK10261  26 QQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMllrrrsrqviELSEQSAAQMRhvrgAD 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 357 IALVGQEPV-----LFarTIKENISYGL---SDVSMEMVVQAATK-------ANAHDFITTLPKgydtsvgekglQLSGG 421
Cdd:PRK10261 106 MAMIFQEPMtslnpVF--TVGEQIAESIrlhQGASREEAMVEAKRmldqvriPEAQTILSRYPH-----------QLSGG 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 422 QKQRVAIARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQEHT--VLVIAHRLSTV-EKADNIIVIDRGQVAERGT 498
Cdd:PRK10261 173 MRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVaEIADRVLVMYQGEAVETGS 252


                 ....
gi 961964003 499 HSQL 502
Cdd:PRK10261 253 VEQI 256
GguA NF040905
sugar ABC transporter ATP-binding protein;
297-495 2.35e-16

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 81.76  E-value: 2.35e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 297 LKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYlPQG---GQVLLDGKPVnEFQ--HDYLHSKIALVGQE----PVLf 367
Cdd:NF040905  17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHGsyeGEILFDGEVC-RFKdiRDSEALGIVIIHQElaliPYL- 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 368 arTIKENI-------SYGLSDvsmemvvQAATKANAHDFITT--LPKGYDTSVGEKGLqlsgGQKQRVAIARALIRQPRV 438
Cdd:NF040905  94 --SIAENIflgneraKRGVID-------WNETNRRARELLAKvgLDESPDTLVTDIGV----GKQQLVEIAKALSKDVKL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 961964003 439 LILDEATSAL-DAESEHIV-------QQALNSIMqehtvlvIAHRLSTVEK-ADNIIVIDRGQVAE 495
Cdd:NF040905 161 LILDEPTAALnEEDSAALLdlllelkAQGITSII-------ISHKLNEIRRvADSITVLRDGRTIE 219
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
276-498 5.09e-16

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 80.98  E-value: 5.09e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 276 TGLVEFKDVTFAYPTrpeTDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQH-DYLH 354
Cdd:PRK09700   3 TPYISMAGIGKSFGP---VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHkLAAQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 355 SKIALVGQE-PVLFARTIKENISYG-----------LSDVSmEMVVQAAtkanahdfITTLPKGYDTSVGEKGLQLSGGQ 422
Cdd:PRK09700  80 LGIGIIYQElSVIDELTVLENLYIGrhltkkvcgvnIIDWR-EMRVRAA--------MMLLRVGLKVDLDEKVANLSISH 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 961964003 423 KQRVAIARALIRQPRVLILDEATSAL-DAESEHIVqQALNSIMQEHTVLV-IAHRLSTVEKadniiVIDRGQVAERGT 498
Cdd:PRK09700 151 KQMLEIAKTLMLDAKVIIMDEPTSSLtNKEVDYLF-LIMNQLRKEGTAIVyISHKLAEIRR-----ICDRYTVMKDGS 222
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
 279-504 5.77e-16

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: 80.62  E-value: 5.77e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  279 VEFKDVTFAYPtrpETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENF--YLPQGGQVL----------------L 340
Cdd:TIGR03269   1 IEVKNLTKKFD---GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyverpsK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  341 DGKP-------VNEFQHDY----------LHSKIALVGQEPvlFA----RTIKENISYGLSDV------SMEMVVQAATK 393
Cdd:TIGR03269  78 VGEPcpvcggtLEPEEVDFwnlsdklrrrIRKRIAIMLQRT--FAlygdDTVLDNVLEALEEIgyegkeAVGRAVDLIEM 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  394 ANAHDFITTLPKgydtsvgekglQLSGGQKQRVAIARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQEH--TVLV 471
Cdd:TIGR03269 156 VQLSHRITHIAR-----------DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgiSMVL 224

                         250       260       270
                  ....*....|....*....|....*....|....
gi 961964003  472 IAHRLSTVEK-ADNIIVIDRGQVAERGTHSQLMA 504
Cdd:TIGR03269 225 TSHWPEVIEDlSDKAIWLENGEIKEEGTPDEVVA 258
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
278-504 1.44e-15

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


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 76.46  E-value: 1.44e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 278 LVEFKDVTFAYPtrpETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQ-HDYLHSK 356
Cdd:PRK11614   5 MLSFDKVSAHYG---KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQtAKIMREA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 357 IALVGQEPVLFAR-TIKENISYGLSDVSMEMVVQAATKANAhdfitTLPKGYDTSVGEKGlQLSGGQKQRVAIARALIRQ 435
Cdd:PRK11614  82 VAIVPEGRRVFSRmTVEENLAMGGFFAERDQFQERIKWVYE-----LFPRLHERRIQRAG-TMSGGEQQMLAIGRALMSQ 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 961964003 436 PRVLILDEATSALdaeSEHIVQQALNSIMQEH----TVLVIAHRLSTVEK-ADNIIVIDRGQVAERGTHSQLMA 504
Cdd:PRK11614 156 PRLLLLDEPSLGL---APIIIQQIFDTIEQLReqgmTIFLVEQNANQALKlADRGYVLENGHVVLEDTGDALLA 226
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
309-503 1.65e-15

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 77.99  E-value: 1.65e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 309 VTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEfqhdyLHSKIAL---------VGQEPVLFAR-TIKENISYG 378
Cdd:PRK11144  26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFD-----AEKGICLppekrrigyVFQDARLFPHyKVRGNLRYG 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 379 LSDVSMEM---VVQAATkanahdfITTLPKGYDTSvgekglqLSGGQKQRVAIARALIRQPRVLILDEATSALDAESEHI 455
Cdd:PRK11144 101 MAKSMVAQfdkIVALLG-------IEPLLDRYPGS-------LSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRE 166

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 961964003 456 VQQALNSIMQEHT--VLVIAHRLSTVEK-ADNIIVIDRGQVAERGT-----HSQLM 503
Cdd:PRK11144 167 LLPYLERLAREINipILYVSHSLDEILRlADRVVVLEQGKVKAFGPleevwASSAM 222
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
 296-497 2.10e-15

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 76.03  E-value: 2.10e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 296 VLKGVSFTLRPGEVTALVGPSGSGKSSCVS----LLE-NFYLPQGGQVLLDGKPVNEFQHDYLH--SKIALVGQEPVLFA 368
Cdd:PRK14267  19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRtfnrLLElNEEARVEGEVRLFGRNIYSPDVDPIEvrREVGMVFQYPNPFP 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 369 R-TIKENISYGL-------SDVSMEMVVQAATKANAhdfittLPKGYDTSVGEKGLQLSGGQKQRVAIARALIRQPRVLI 440
Cdd:PRK14267  99 HlTIYDNVAIGVklnglvkSKKELDERVEWALKKAA------LWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILL 172

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 961964003 441 LDEATSALDAESEHIVQQALNSIMQEHTVLVIAHRLSTVEK-ADNIIVIDRGQVAERG 497
Cdd:PRK14267 173 MDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARvSDYVAFLYLGKLIEVG 230
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
 293-474 3.00e-15

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 75.20  E-value: 3.00e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 293 ETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPV---NEFQHDYLHSK-IALVGQE----P 364
Cdd:PRK10584  22 ELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLhqmDEEARAKLRAKhVGFVFQSfmliP 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 365 VLFARtikENISY-----GLSDvsmemvvqAATKANAHDFITTLpkGYDTSVGEKGLQLSGGQKQRVAIARALIRQPRVL 439
Cdd:PRK10584 102 TLNAL---ENVELpallrGESS--------RQSRNGAKALLEQL--GLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVL 168

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 961964003 440 ILDEATSALDAESEHIVQQALNSIMQEH--TVLVIAH 474
Cdd:PRK10584 169 FADEPTGNLDRQTGDKIADLLFSLNREHgtTLILVTH 205
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
 298-502 3.09e-15

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 77.05  E-value: 3.09e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 298 KGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHDYLH---SKIALVGQEPV--LFAR-TI 371
Cdd:PRK15079  38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRavrSDIQMIFQDPLasLNPRmTI 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 372 KENIsyglsdvsmemvvqaatkanAHDFITTLPKGYDTSVGEK--------GL----------QLSGGQKQRVAIARALI 433
Cdd:PRK15079 118 GEII--------------------AEPLRTYHPKLSRQEVKDRvkammlkvGLlpnlinryphEFSGGQCQRIGIARALI 177

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 961964003 434 RQPRVLILDEATSALDAESEHIVQQALNSIMQEH--TVLVIAHRLSTVEK-ADNIIVIDRGQVAERGTHSQL 502
Cdd:PRK15079 178 LEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMglSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV 249
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
296-519 4.72e-15

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 75.41  E-value: 4.72e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 296 VLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHDYLHSKIALVGQEPV---------- 365
Cdd:PRK10253  22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATtpgditvqel 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 366 ----------LFARTIKENisyglsdvsmEMVVQAATKANAhdfITTLP-KGYDTsvgekglqLSGGQKQRVAIARALIR 434
Cdd:PRK10253 102 vargryphqpLFTRWRKED----------EEAVTKAMQATG---ITHLAdQSVDT--------LSGGQRQRAWIAMVLAQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 435 QPRVLILDEATSALDAESEHIVQQALNSIMQE--HTVLVIAHRLSTVEK-ADNIIVIDRGQVAERGTHSQLMATG----- 506
Cdd:PRK10253 161 ETAIMLLDEPTTWLDISHQIDLLELLSELNREkgYTLAAVLHDLNQACRyASHLIALREGKIVAQGAPKEIVTAElieri 240

                        250
                 ....*....|....
gi 961964003 507 -GLYCKLVQRQVLG 519
Cdd:PRK10253 241 yGLRCMIIDDPVAG 254
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
 299-497 5.07e-15

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 74.96  E-value: 5.07e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 299 GVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKpvnefqHDYLHSKIALVGQEPVLFART----IKEN 374
Cdd:PRK11701  24 DVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMR------DGQLRDLYALSEAERRRLLRTewgfVHQH 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 375 ISYGL-SDVSM-----E--MVVQA----ATKANAHDF----------ITTLPKGYdtsvgekglqlSGGQKQRVAIARAL 432
Cdd:PRK11701  98 PRDGLrMQVSAggnigErlMAVGArhygDIRATAGDWlerveidaarIDDLPTTF-----------SGGMQQRLQIARNL 166

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 961964003 433 IRQPRVLILDEATSALDAEsehiVQQALNSIMQEHT------VLVIAHRLSTVE-KADNIIVIDRGQVAERG 497
Cdd:PRK11701 167 VTHPRLVFMDEPTGGLDVS----VQARLLDLLRGLVrelglaVVIVTHDLAVARlLAHRLLVMKQGRVVESG 234
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
 293-495 5.70e-15

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


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 74.22  E-value: 5.70e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 293 ETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLenfylpQGGQVLLDGKPVNEFQHDYLHSKIALVgqEPVLFARTIK 372
Cdd:COG2401   42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLL------AGALKGTPVAGCVDVPDNQFGREASLI--DAIGRKGDFK 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 373 ENISY----GLSDVSMemvvqaatkanahdfittlpkgYDTSVGEkglqLSGGQKQRVAIARALIRQPRVLILDEATSAL 448
Cdd:COG2401  114 DAVELlnavGLSDAVL----------------------WLRRFKE----LSTGQKFRFRLALLLAERPKLLVIDEFCSHL 167

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 961964003 449 DAESEHIVQQALNSIMQEH--TVLVIAHRlSTVEKA---DNIIVIDRGQVAE 495
Cdd:COG2401  168 DRQTAKRVARNLQKLARRAgiTLVVATHH-YDVIDDlqpDLLIFVGYGGVPE 218
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
 276-490 6.62e-15

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 74.77  E-value: 6.62e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 276 TGLVEFKDVTFAYPTRpetDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKpvneFQHDYLHS 355
Cdd:PRK09544   2 TSLVSLENVSVSFGQR---RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK----LRIGYVPQ 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 356 KIALVGQEPVlfartikenisyglsDVSMEMVVQAATKANahDFITTLPKGYDTSVGEKGLQ-LSGGQKQRVAIARALIR 434
Cdd:PRK09544  75 KLYLDTTLPL---------------TVNRFLRLRPGTKKE--DILPALKRVQAGHLIDAPMQkLSGGETQRVLLARALLN 137

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 961964003 435 QPRVLILDEATSALDAESEHIVQQALNSIMQE--HTVLVIAHRLSTV-EKADNIIVIDR 490
Cdd:PRK09544 138 RPQLLVLDEPTQGVDVNGQVALYDLIDQLRREldCAVLMVSHDLHLVmAKTDEVLCLNH 196
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
 278-498 7.64e-15

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 75.92  E-value: 7.64e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 278 LVEFKD--VTFAYPTRPETDVlKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQG---GQVLLDGKPV---NEFQ 349
Cdd:PRK09473  12 LLDVKDlrVTFSTPDGDVTAV-NDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREIlnlPEKE 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 350 HDYLHS-KIALVGQEPVlfartIKENISYGLSDVSME--MVVQAATKANAhdfittlpkgYDTSV----------GEKGL 416
Cdd:PRK09473  91 LNKLRAeQISMIFQDPM-----TSLNPYMRVGEQLMEvlMLHKGMSKAEA----------FEESVrmldavkmpeARKRM 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 417 QL-----SGGQKQRVAIARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQEH--TVLVIAHRLSTVEK-ADNIIVI 488
Cdd:PRK09473 156 KMyphefSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFntAIIMITHDLGVVAGiCDKVLVM 235

                        250
                 ....*....|
gi 961964003 489 DRGQVAERGT 498
Cdd:PRK09473 236 YAGRTMEYGN 245
hmuV PRK13547
heme ABC transporter ATP-binding protein;
296-503 1.28e-14

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 74.09  E-value: 1.28e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 296 VLKGVSFTLRPGEVTALVGPSGSGKSscvSLLENF-------YLPQG----GQVLLDGKPVNEFQHDYLHSKIALVGQ-- 362
Cdd:PRK13547  16 ILRDLSLRIEPGRVTALLGRNGAGKS---TLLKALagdltggGAPRGarvtGDVTLNGEPLAAIDAPRLARLRAVLPQaa 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 363 EPVlFARTIKENISYG----------LSDVSMEMVVQAATKANAhdfittlpkgyDTSVGEKGLQLSGGQKQRVAIARAL 432
Cdd:PRK13547  93 QPA-FAFSAREIVLLGrypharragaLTHRDGEIAWQALALAGA-----------TALVGRDVTTLSGGELARVQFARVL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 433 ---------IRQPRVLILDEATSALDAESEHIVQQALNSIMQEHT--VLVIAHRLSTVEK-ADNIIVIDRGQVAERGTHS 500
Cdd:PRK13547 161 aqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNlgVLAIVHDPNLAARhADRIAMLADGAIVAHGAPA 240


                 ...
gi 961964003 501 QLM 503
Cdd:PRK13547 241 DVL 243
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
 296-498 1.45e-14

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


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 73.58  E-value: 1.45e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 296 VLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKpvnefqhdyLHSKIAL-VGQEPVLFARtikEN 374
Cdd:COG1134   41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR---------VSALLELgAGFHPELTGR---EN 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 375 IS-----YGLSDVSMEMVVQAATK-ANAHDFIttlpkgyDTSVGekglQLSGGQKQRVAIARALIRQPRVLILDEATSAL 448
Cdd:COG1134  109 IYlngrlLGLSRKEIDEKFDEIVEfAELGDFI-------DQPVK----TYSSGMRARLAFAVATAVDPDILLVDEVLAVG 177

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 961964003 449 DAESEHIVQQALNSIMQEH-TVLVIAHRLSTVEK-ADNIIVIDRGQVAERGT 498
Cdd:COG1134  178 DAAFQKKCLARIRELRESGrTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGD 229
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
 280-504 1.69e-14

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 76.12  E-value: 1.69e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 280 EFKDVTFAYPTRPETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYlpQG---GQVLLDGKPVN-EFQHDYLHS 355
Cdd:PRK13549 261 EVRNLTAWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAY--PGrweGEIFIDGKPVKiRNPQQAIAQ 338

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 356 KIALV-------GQEPVLfarTIKENISYG-LSDVSMEMVVQAATKAN-AHDFITTL------PkgyDTSVGekglQLSG 420
Cdd:PRK13549 339 GIAMVpedrkrdGIVPVM---GVGKNITLAaLDRFTGGSRIDDAAELKtILESIQRLkvktasP---ELAIA----RLSG 408

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 421 GQKQRVAIARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQEH-TVLVIAHRLSTV-EKADNIIVIDRGQ-----V 493
Cdd:PRK13549 409 GNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGvAIIVISSELPEVlGLSDRVLVMHEGKlkgdlI 488

                        250
                 ....*....|.
gi 961964003 494 AERGTHSQLMA 504
Cdd:PRK13549 489 NHNLTQEQVME 499
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
 278-505 2.04e-14

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


Pssm-ID: 131681 [Multi-domain]  Cd Length: 500  Bit Score: 75.63  E-value: 2.04e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  278 LVEFKDVTFAYPTRPETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQ-GGQVLLDGKPVN-EFQHDYLHS 355
Cdd:TIGR02633 257 ILEARNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDiRNPAQAIRA 336

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  356 KIALVGQE-------PVLfarTIKENISYG-LSDVSMEMVVQAATKANAHD----------FITTLPKGydtsvgekglQ 417
Cdd:TIGR02633 337 GIAMVPEDrkrhgivPIL---GVGKNITLSvLKSFCFKMRIDAAAELQIIGsaiqrlkvktASPFLPIG----------R 403

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  418 LSGGQKQRVAIARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQEH-TVLVIAHRLSTVEK-ADNIIVIDRGQ--- 492
Cdd:TIGR02633 404 LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGvAIIVVSSELAEVLGlSDRVLVIGEGKlkg 483

                         250
                  ....*....|....*
gi 961964003  493 --VAERGTHSQLMAT 505
Cdd:TIGR02633 484 dfVNHALTQEQVLAA 498
SapD COG4170
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
296-505 2.28e-14

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


Pssm-ID: 443330 [Multi-domain]  Cd Length: 331  Bit Score: 74.17  E-value: 2.28e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 296 VLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQ----------GGQVLLDGKPvnEFQHDYLHSKIALVGQEP- 364
Cdd:COG4170   22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNwhvtadrfrwNGIDLLKLSP--RERRKIIGREIAMIFQEPs 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 365 ------VLFARTIKENI-SYGLSDVSMEMVVQAATKAnahdfITTLPKgydtsVGEKG---------LQLSGGQKQRVAI 428
Cdd:COG4170  100 scldpsAKIGDQLIEAIpSWTFKGKWWQRFKWRKKRA-----IELLHR-----VGIKDhkdimnsypHELTEGECQKVMI 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 429 ARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQEH--TVLVIAHRLSTVEK-ADNIIVIDRGQVAERGTHSQLMAT 505
Cdd:COG4170  170 AMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQgtSILLISHDLESISQwADTITVLYCGQTVESGPTEQILKS 249
PLN03211 PLN03211
ABC transporter G-25; Provisional
 293-504 2.60e-14

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 75.69  E-value: 2.60e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 293 ETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQG--GQVLL-DGKPVNEfqhdyLHSKIALVGQEPVLFAR 369
Cdd:PLN03211  80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILAnNRKPTKQ-----ILKRTGFVTQDDILYPH 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 370 -TIKENISY-GLSDVSMEMVVQAATKAnAHDFITTL--PKGYDTSVGEKGLQ-LSGGQKQRVAIARALIRQPRVLILDEA 444
Cdd:PLN03211 155 lTVRETLVFcSLLRLPKSLTKQEKILV-AESVISELglTKCENTIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDEP 233

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 961964003 445 TSALDAESEHIVQQALNSIMQE-HTVLVIAHRLST--VEKADNIIVIDRGQVAERGTHSQLMA 504
Cdd:PLN03211 234 TSGLDATAAYRLVLTLGSLAQKgKTIVTSMHQPSSrvYQMFDSVLVLSEGRCLFFGKGSDAMA 296
ABC_6TM_PrtD_LapB_HlyB_like cd18783
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ...
 30-228 3.26e-14

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: 73.32  E-value: 3.26e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  30 ARLNVRLRSRLFRTLMTQEIAFFDENHTGDILSRLSAdTTQVSDLISQNVnvfLRSVIKGTGFIIF---MFRMSWKLTLV 106
Cdd:cd18783   71 TRIDARLALRTFDRLLSLPIDFFERTPAGVLTKHMQQ-IERIRQFLTGQL---FGTLLDATSLLVFlpvLFFYSPTLALV 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 107 TMMGFPFIALVSKLYGEYYKKLTKEVqtVLAEANKVAE--ETISGMRTVRSFANESREANSYYAKLLVMFQLNKKQALAY 184
Cdd:cd18783  147 VLAFSALIALIILAFLPPFRRRLQAL--YRAEGERQAFlvETVHGIRTVKSLALEPRQRREWDERVARAIRARFAVGRLS 224

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 961964003 185 AcymWSSCIS---ELALEVAVLYYGGHLVLTDQLSSGGLISFfiYML 228
Cdd:cd18783  225 N---WPQTLTgplEKLMTVGVIWVGAYLVFAGSLTVGALIAF--NML 266
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
 282-492 3.78e-14

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: 74.97  E-value: 3.78e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  282 KDVTFAYPtrPETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLdgkpvnefQHDYlhsKIALVG 361
Cdd:TIGR03719   8 NRVSKVVP--PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARP--------QPGI---KVGYLP 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  362 QEPVL-FARTIKENISYGLSD----------VSM-------EMVVQAATKA---------NAHDFITTL---------PK 405
Cdd:TIGR03719  75 QEPQLdPTKTVRENVEEGVAEikdaldrfneISAkyaepdaDFDKLAAEQAelqeiidaaDAWDLDSQLeiamdalrcPP 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  406 GyDTSVGEkglqLSGGQKQRVAIARALIRQPRVLILDEATSALDAESEHIVQQALnsimQEH--TVLVIAH-R--LSTVe 480
Cdd:TIGR03719 155 W-DADVTK----LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHL----QEYpgTVVAVTHdRyfLDNV- 224

                         250
                  ....*....|..
gi 961964003  481 kADNIIVIDRGQ 492
Cdd:TIGR03719 225 -AGWILELDRGR 235
ABCG_PDR_domain2 cd03232
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...
 281-491 3.86e-14

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: 71.12  E-value: 3.86e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 281 FKDVTFAYPTRPET-DVLKGVSFTLRPGEVTALVGPSGSGKSScvsLLEnfYLPQ-------GGQVLLDGKPVNEfqhdY 352
Cdd:cd03232    6 WKNLNYTVPVKGGKrQLLNNISGYVKPGTLTALMGESGAGKTT---LLD--VLAGrktagviTGEILINGRPLDK----N 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 353 LHSKIALVGQEPVLFAR-TIKENISYglsdvsmemvvqaatkanahdfittlpkgydtSVGEKGLQLSggQKQRVAIARA 431
Cdd:cd03232   77 FQRSTGYVEQQDVHSPNlTVREALRF--------------------------------SALLRGLSVE--QRKRLTIGVE 122

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 961964003 432 LIRQPRVLILDEATSALDAESEHIVQQALNSI-MQEHTVLVIAHRLSTV--EKADNIIVIDRG 491
Cdd:cd03232  123 LAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLaDSGQAILCTIHQPSASifEKFDRLLLLKRG 185
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
 197-479 4.53e-14

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: 74.84  E-value: 4.53e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  197 ALEVAVLYYGGHLVLTDQLSS--GGLISFFIYmLELGECFE--SIASVYSGLMQGVGAAEKVFEYLDRKPkhpadgteap 272
Cdd:TIGR03269 210 ALEEAVKASGISMVLTSHWPEviEDLSDKAIW-LENGEIKEegTPDEVVAVFMEGVSEVEKECEVEVGEP---------- 278

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  273 nsctgLVEFKDVTFAYPT--RPETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQV-------LLDGK 343
Cdd:TIGR03269 279 -----IIKVRNVSKRYISvdRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdeWVDMT 353

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  344 PVNEFQHDYLHSKIALVGQEPVLFA-RTIKENISYGLS-DVSMEMVVQAATkanahdfITTLPKGYDTSVGEKGL----- 416
Cdd:TIGR03269 354 KPGPDGRGRAKRYIGILHQEYDLYPhRTVLDNLTEAIGlELPDELARMKAV-------ITLKMVGFDEEKAEEILdkypd 426

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 961964003  417 QLSGGQKQRVAIARALIRQPRVLILDEATSALDAESEHIVQqalNSIMQ-----EHTVLVIAHRLSTV 479
Cdd:TIGR03269 427 ELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVT---HSILKareemEQTFIIVSHDMDFV 491
ycf16 CHL00131
sulfate ABC transporter protein; Validated
 293-498 4.59e-14

sulfate ABC transporter protein; Validated


Pssm-ID: 214372 [Multi-domain]  Cd Length: 252  Bit Score: 72.37  E-value: 4.59e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 293 ETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENF--YLPQGGQVLLDGKPVNEFQHDYL-HSKIALVGQEPVL--- 366
Cdd:CHL00131  19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEPEERaHLGIFLAFQYPIEipg 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 367 -----FARTI--KENISYGLSDVS----MEMVVQAATKANAHdfittlPKGYDTSVGEKglqLSGGQKQRVAIARALIRQ 435
Cdd:CHL00131  99 vsnadFLRLAynSKRKFQGLPELDplefLEIINEKLKLVGMD------PSFLSRNVNEG---FSGGEKKRNEILQMALLD 169

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 961964003 436 PRVLILDEATSALDAESEHIVQQALNSIM-QEHTVLVIAH--RLSTVEKADNIIVIDRGQVAERGT 498
Cdd:CHL00131 170 SELAILDETDSGLDIDALKIIAEGINKLMtSENSIILITHyqRLLDYIKPDYVHVMQNGKIIKTGD 235
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
 282-492 5.17e-14

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 74.77  E-value: 5.17e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 282 KDVTFAYPtrPETDVLKGVSFTLRPGEVTALVGPSGSGKSScvsllenfylpqggqVL-----LDgkpvNEFQHDYLHSK 356
Cdd:PRK11819  10 NRVSKVVP--PKKQILKDISLSFFPGAKIGVLGLNGAGKST---------------LLrimagVD----KEFEGEARPAP 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 357 IALVG---QEPVL-FARTIKENISYGLSD----------VSMEM---------------VVQAATKA-NAHDFITTL--- 403
Cdd:PRK11819  69 GIKVGylpQEPQLdPEKTVRENVEEGVAEvkaaldrfneIYAAYaepdadfdalaaeqgELQEIIDAaDAWDLDSQLeia 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 404 ------PKGyDTSVGekglQLSGGQKQRVAIARALIRQPRVLILDEATSALDAESEHIVQQALnsimQEH--TVLVIAH- 474
Cdd:PRK11819 149 mdalrcPPW-DAKVT----KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFL----HDYpgTVVAVTHd 219

                        250       260
                 ....*....|....*....|
gi 961964003 475 R--LSTVekADNIIVIDRGQ 492
Cdd:PRK11819 220 RyfLDNV--AGWILELDRGR 237
ABC_6TM_PrtD_LapB_HlyB_like cd18782
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ...
 12-225 5.70e-14

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: 72.63  E-value: 5.70e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  12 LLSSMAIGVRGGVFTLTMARLNVRLRSRLFRTLMTQEIAFFDENHTGDILSRLSaDTTQVSDLISQNVNVFLRSVIKGTG 91
Cdd:cd18782   53 LLEAVLTALRTYLFTDTANRIDLELGGTIIDHLLRLPLGFFDKRPVGELSTRIS-ELDTIRGFLTGTALTTLLDVLFSVI 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  92 FIIFMFRMSWKLTLVTMMGFPFIALVSKLYGEYYKKLTKEVQTVLAEANKVAEETISGMRTVRSFANES----REANSYY 167
Cdd:cd18782  132 YIAVLFSYSPLLTLVVLATVPLQLLLTFLFGPILRRQIRRRAEASAKTQSYLVESLTGIQTVKAQNAELkarwRWQNRYA 211

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 961964003 168 AKLLVMFQLNKKQALAYACymwSSCISELAlEVAVLYYGGHLVLTDQLSSGGLISFFI 225
Cdd:cd18782  212 RSLGEGFKLTVLGTTSGSL---SQFLNKLS-SLLVLWVGAYLVLRGELTLGQLIAFRI 265
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
 300-502 6.49e-14

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 72.85  E-value: 6.49e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 300 VSFTLRPGEVTALVGPSGSGKS-SCVSLLENFYLPqgGQVLLDGKPVNefQHDYLH-----------SKIALVGQEPVlf 367
Cdd:PRK11022  26 ISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYP--GRVMAEKLEFN--GQDLQRisekerrnlvgAEVAMIFQDPM-- 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 368 artIKENISYGLSDVSMEM--VVQAATKANAHDFITTLPkgydTSVG----EKGL-----QLSGGQKQRVAIARALIRQP 436
Cdd:PRK11022 100 ---TSLNPCYTVGFQIMEAikVHQGGNKKTRRQRAIDLL----NQVGipdpASRLdvyphQLSGGMSQRVMIAMAIACRP 172

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 961964003 437 RVLILDEATSALDAESE-HIVQQALNSIMQEHTVLV-IAHRLSTV-EKADNIIVIDRGQVAERGTHSQL 502
Cdd:PRK11022 173 KLLIADEPTTALDVTIQaQIIELLLELQQKENMALVlITHDLALVaEAAHKIIVMYAGQVVETGKAHDI 241
ABC_6TM_ABCC_D2 cd18580
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ...
 7-257 6.96e-14

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: 72.54  E-value: 6.96e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   7 FTLFFLLSSMAIGVRGGVFTLTMARLNVRLRSRLFRTLMTQEIAFFDENHTGDILSRLSADTTQVSDLISQNVNVFLRSV 86
Cdd:cd18580   45 AALLVLASVLLVLLRWLLFVLAGLRASRRLHDKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSL 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  87 IKGTGFIIFMFRMSWKLTLVtmmgFPFIALVSKLYGEYYKKLTKEVQTVLAEA-----NKVAeETISGMRTVRSFANESR 161
Cdd:cd18580  125 FSVLGSLIVIAIVSPYFLIV----LPPLLVVYYLLQRYYLRTSRQLRRLESESrsplySHFS-ETLSGLSTIRAFGWQER 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 162 eansyyakllVMFQLNKKQALAYACYMWSSCISE---LALE---------VAVLyygghLVLTDQLSSGGLISF-FIYML 228
Cdd:cd18580  200 ----------FIEENLRLLDASQRAFYLLLAVQRwlgLRLDllgallalvVALL-----AVLLRSSISAGLVGLaLTYAL 264

                        250       260
                 ....*....|....*....|....*....
gi 961964003 229 ELGECFESIASVYSGLMQGVGAAEKVFEY 257
Cdd:cd18580  265 SLTGSLQWLVRQWTELETSMVSVERILEY 293
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
 297-496 7.41e-14

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 73.88  E-value: 7.41e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 297 LKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNeFQ--HDYLHSKIALVGQEPVLFAR-TIKE 373
Cdd:PRK10762  20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVT-FNgpKSSQEAGIGIIHQELNLIPQlTIAE 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 374 NISYGLSDVSM-------EMVVQAA---TKANahdfittLPKGYDTSVGEkglqLSGGQKQRVAIARALIRQPRVLILDE 443
Cdd:PRK10762  99 NIFLGREFVNRfgridwkKMYAEADkllARLN-------LRFSSDKLVGE----LSIGEQQMVEIAKVLSFESKVIIMDE 167

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 961964003 444 ATSAL-DAESEhivqqALNSIMQE-----HTVLVIAHRLSTV-EKADNIIVIDRGQ-VAER 496
Cdd:PRK10762 168 PTDALtDTETE-----SLFRVIRElksqgRGIVYISHRLKEIfEICDDVTVFRDGQfIAER 223
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
 293-497 1.14e-13

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 73.74  E-value: 1.14e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 293 ETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHDYLHS---KIALVGQEPV--LF 367
Cdd:PRK10261 336 EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQAlrrDIQFIFQDPYasLD 415

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 368 AR-TIKENISYGLSdVSMEMVVQAATKANAH--DFITTLPKgydtSVGEKGLQLSGGQKQRVAIARALIRQPRVLILDEA 444
Cdd:PRK10261 416 PRqTVGDSIMEPLR-VHGLLPGKAAAARVAWllERVGLLPE----HAWRYPHEFSGGQRQRICIARALALNPKVIIADEA 490

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 961964003 445 TSALDAEsehIVQQALNSIMQEH-----TVLVIAHRLSTVEK-ADNIIVIDRGQVAERG 497
Cdd:PRK10261 491 VSALDVS---IRGQIINLLLDLQrdfgiAYLFISHDMAVVERiSHRVAVMYLGQIVEIG 546
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
 300-503 2.21e-13

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 69.96  E-value: 2.21e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 300 VSFTLRPGEVTALVGPSGSGKSSCVSLLENFyLPQGGQVLLDGKPVNefqhDYLHSKIA-----LVGQEPVLFARTIKEN 374
Cdd:PRK03695  15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLE----AWSAAELArhrayLSQQQTPPFAMPVFQY 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 375 ISYGLSDvsmemVVQAATKANAHDFITTLPKGYD---TSVGekglQLSGGQKQRVAIArALIRQ------P--RVLILDE 443
Cdd:PRK03695  90 LTLHQPD-----KTRTEAVASALNEVAEALGLDDklgRSVN----QLSGGEWQRVRLA-AVVLQvwpdinPagQLLLLDE 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 961964003 444 ATSALDaesehIVQQ-ALNSIMQEH-----TVLVIAHRLS-TVEKADNIIVIDRGQVAERGTHSQLM 503
Cdd:PRK03695 160 PMNSLD-----VAQQaALDRLLSELcqqgiAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVL 221
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
 291-515 3.29e-13

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: 73.12  E-value: 3.29e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   291 RPETDVLkgvSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVnEFQHDYLHSKIALVGQEPVLFAR- 369
Cdd:TIGR01257  943 RPAVDRL---NITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHl 1018

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   370 TIKENISY--GLSDVSMEMVvQAATKANAHDfittlpKGYDTSVGEKGLQLSGGQKQRVAIARALIRQPRVLILDEATSA 447
Cdd:TIGR01257 1019 TVAEHILFyaQLKGRSWEEA-QLEMEAMLED------TGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSG 1091

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 961964003   448 LDAESEHIVQQALNSIMQEHTVLVIAHRLSTVE-KADNIIVIDRGQVAERGTHSQLMAT--GGLYCKLVQR 515
Cdd:TIGR01257 1092 VDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADlLGDRIAIISQGRLYCSGTPLFLKNCfgTGFYLTLVRK 1162
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
 296-521 6.96e-13

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 68.38  E-value: 6.96e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 296 VLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQ-HDYLHSKIALVGQEPVLFAR-TIKE 373
Cdd:PRK10895  18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlHARARRGIGYLPQEASIFRRlSVYD 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 374 NISYGLS---DVSMEMVVQAATKANAHDFITTLPKGYdtsvgekGLQLSGGQKQRVAIARALIRQPRVLILDEATSALDA 450
Cdd:PRK10895  98 NLMAVLQirdDLSAEQREDRANELMEEFHIEHLRDSM-------GQSLSGGERRRVEIARALAANPKFILLDEPFAGVDP 170

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 961964003 451 ES--------EHIVQQALNSIMQEHTVlviAHRLSTVEKAdniIVIDRGQVAERGTHSQLMATgglycKLVQRQVLGIE 521
Cdd:PRK10895 171 ISvidikriiEHLRDSGLGVLITDHNV---RETLAVCERA---YIVSQGHLIAHGTPTEILQD-----EHVKRVYLGED 238
sufC PRK09580
cysteine desulfurase ATPase component; Reviewed
 293-500 1.51e-12

cysteine desulfurase ATPase component; Reviewed


Pssm-ID: 181965 [Multi-domain]  Cd Length: 248  Bit Score: 67.51  E-value: 1.51e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 293 ETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLL--ENFYLPQGGQVLLDGKPVNEFQ-HDYLHSKIALVGQEPVlfar 369
Cdd:PRK09580  13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSpEDRAGEGIFMAFQYPV---- 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 370 tikenisyGLSDVSMEMVVQAATKA----------NAHDF-------ITTLPKGYDTSVGEKGLQLSGGQKQRVAIARAL 432
Cdd:PRK09580  89 --------EIPGVSNQFFLQTALNAvrsyrgqeplDRFDFqdlmeekIALLKMPEDLLTRSVNVGFSGGEKKRNDILQMA 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 961964003 433 IRQPRVLILDEATSALDAESEHIVQQALNSIMQEHTVLVIA---HRLSTVEKADNIIVIDRGQVAERGTHS 500
Cdd:PRK09580 161 VLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVthyQRILDYIKPDYVHVLYQGRIVKSGDFT 231
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
283-497 2.30e-12

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 67.60  E-value: 2.30e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 283 DVTFAYptRPETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHDYLhskIALVGQ 362
Cdd:PRK15056  11 DVTVTW--RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VAYVPQ 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 363 EpvlfartikENISYGLSdVSMEMVVQAATKAnaHDFITTLPKGYDTSVGEKGL--------------QLSGGQKQRVAI 428
Cdd:PRK15056  86 S---------EEVDWSFP-VLVEDVVMMGRYG--HMGWLRRAKKRDRQIVTAALarvdmvefrhrqigELSGGQKKRVFL 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 429 ARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQE-HTVLVIAHRLSTVEKADNIIVIDRGQVAERG 497
Cdd:PRK15056 154 ARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEgKTMLVSTHNLGSVTEFCDYTVMVKGTVLASG 223
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
 303-506 2.97e-12

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: 66.66  E-value: 2.97e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 303 TLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDG-----KPvNEFQHDY-------LHSKIALVGQEPvlfart 370
Cdd:cd03237   21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELdtvsyKP-QYIKADYegtvrdlLSSITKDFYTHP------ 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 371 ikenisYGLSDVSMEMvvqaatkanahdfitTLPKGYDTSVGEkglqLSGGQKQRVAIARALIRQPRVLILDEATSALDA 450
Cdd:cd03237   94 ------YFKTEIAKPL---------------QIEQILDREVPE----LSGGELQRVAIAACLSKDADIYLLDEPSAYLDV 148

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 961964003 451 ESEHIVQQALNSIMQEH--TVLVIAHRLSTVEK-ADNIIVIDrGQVAERGTHS--QLMATG 506
Cdd:cd03237  149 EQRLMASKVIRRFAENNekTAFVVEHDIIMIDYlADRLIVFE-GEPSVNGVANppQSLRSG 208
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
 244-504 3.35e-12

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 68.90  E-value: 3.35e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 244 LMqgVGaaEKVFEYLDRKPKHPADgteaPnsctgLVEFKDVTfaYPTRPETDVLKGVSFTLRPGEVTALVGPSGSGKSSC 323
Cdd:COG3845  236 LM--VG--REVLLRVEKAPAEPGE----V-----VLEVENLS--VRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSEL 300

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 324 VSLLENFYLPQGGQVLLDGKPV-NEFQHDYLHSKIALVGQEP-----VLfARTIKENI---SYGLSDVS-MEMVVQAATK 393
Cdd:COG3845  301 AEALAGLRPPASGSIRLDGEDItGLSPRERRRLGVAYIPEDRlgrglVP-DMSVAENLilgRYRRPPFSrGGFLDRKAIR 379

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 394 ANAHDFITTL---PKGYDTSVGekglQLSGGQKQRVAIARALIRQPRVLILDEATSALDAES-EHIVQQalnsIMQE--- 466
Cdd:COG3845  380 AFAEELIEEFdvrTPGPDTPAR----SLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAiEFIHQR----LLELrda 451

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 961964003 467 -HTVLVIAHRLSTV-EKADNIIVIDRGQ-VAERGTHS-------QLMA 504
Cdd:COG3845  452 gAAVLLISEDLDEIlALSDRIAVMYEGRiVGEVPAAEatreeigLLMA 499
ABC_6TM_PrtD_LapB_HlyB_like cd18566
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ...
 19-225 3.39e-12

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: 67.22  E-value: 3.39e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  19 GVRGGVFTLTMARLNVRLRSRLFRTLMTQEIAFFDENHTGDILSRLsADTTQVSD-LISQNVNVFLR---SVIkgtgFII 94
Cdd:cd18566   60 LLRSYILAWIGARFDHRLSNAAFEHLLSLPLSFFEREPSGAHLERL-NSLEQIREfLTGQALLALLDlpfVLI----FLG 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  95 FMFRMSWKLTLVTMMGFPFIALVSKLYGEYYKKLTKEVQTVLAEANKVAEETISGMRTVRSFANESREANSY---YAKLL 171
Cdd:cd18566  135 LIWYLGGKLVLVPLVLLGLFVLVAILLGPILRRALKERSRADERRQNFLIETLTGIHTIKAMAMEPQMLRRYerlQANAA 214

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 961964003 172 VM-FQLNKKQALAYACymwSSCISELALeVAVLYYGGHLVLTDQLSSGGLISFFI 225
Cdd:cd18566  215 YAgFKVAKINAVAQTL---GQLFSQVSM-VAVVAFGALLVINGDLTVGALIACTM 265
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
276-504 1.03e-11

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 65.56  E-value: 1.03e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 276 TGLVEFKDVTFaypTRPETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHDYLHS 355
Cdd:PRK11831   5 ANLVDMRGVSF---TRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 356 ---KIALVGQEPVLFAR-TIKENISYGLSDvsmemvvqaatkanaHdfiTTLPKGYDTS--------VGEKGL------Q 417
Cdd:PRK11831  82 vrkRMSMLFQSGALFTDmNVFDNVAYPLRE---------------H---TQLPAPLLHStvmmkleaVGLRGAaklmpsE 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 418 LSGGQKQRVAIARALIRQPRVLILDEATSALDAesehIVQQALNSIMQE--H----TVLVIAHRLSTV-EKADNIIVIDR 490
Cdd:PRK11831 144 LSGGMARRAALARAIALEPDLIMFDEPFVGQDP----ITMGVLVKLISElnSalgvTCVVVSHDVPEVlSIADHAYIVAD 219

                        250
                 ....*....|....
gi 961964003 491 GQVAERGTHSQLMA 504
Cdd:PRK11831 220 KKIVAHGSAQALQA 233
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 306-490 1.25e-11

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 62.78  E-value: 1.25e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   306 PGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLdgkpvnefqhdylhskialvgqepvlfartikenisyglsdVSME 385
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY-----------------------------------------IDGE 39

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   386 MVVQAATKANAHdfittlpkgydTSVGEKGLQLSGGQKQRVAIARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQ 465
Cdd:smart00382  40 DILEEVLDQLLL-----------IIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLL 108

                          170       180       190
                   ....*....|....*....|....*....|..
gi 961964003   466 EH-------TVLVIAHRLSTVEKADNIIVIDR 490
Cdd:smart00382 109 LLlkseknlTVILTTNDEKDLGPALLRRRFDR 140
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
278-498 1.91e-11

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 66.76  E-value: 1.91e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 278 LVEFKDVTFAYPTRpETDVLKGvsfTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLD----GKPvnefQhdYL 353
Cdd:PRK13409 340 LVEYPDLTKKLGDF-SLEVEGG---EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPElkisYKP----Q--YI 409

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 354 HSKIalvgQEPV-LFARTIKENI--SYGLSDVSMEMvvqaatkanahdfitTLPKGYDTSVGEkglqLSGGQKQRVAIAR 430
Cdd:PRK13409 410 KPDY----DGTVeDLLRSITDDLgsSYYKSEIIKPL---------------QLERLLDKNVKD----LSGGELQRVAIAA 466

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 961964003 431 ALIRQPRVLILDEATSALDAESEHIVQQALNSIMQEH--TVLVIAHRLSTVEK-ADNIIVIDrGQVAERGT 498
Cdd:PRK13409 467 CLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEReaTALVVDHDIYMIDYiSDRLMVFE-GEPGKHGH 536
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
 283-483 2.88e-11

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127 [Multi-domain]  Cd Length: 200  Bit Score: 63.05  E-value: 2.88e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 283 DVTFAYPTRPetdVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHDYlHSKIALVGQ 362
Cdd:PRK13540   6 ELDFDYHDQP---LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTY-QKQLCFVGH 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 363 E----PVLfarTIKENISYGLSDVSMEMVVQAATKANAHDFITTLPKGYdtsvgekglqLSGGQKQRVAIARALIRQPRV 438
Cdd:PRK13540  82 RsginPYL---TLRENCLYDIHFSPGAVGITELCRLFSLEHLIDYPCGL----------LSSGQKRQVALLRLWMSKAKL 148

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 961964003 439 LILDEATSALDaesehivQQALNSIM---QEH-----TVLVIAHRLSTVEKAD 483
Cdd:PRK13540 149 WLLDEPLVALD-------ELSLLTIItkiQEHrakggAVLLTSHQDLPLNKAD 194
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
 292-536 4.10e-11

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


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 65.90  E-value: 4.10e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   292 PETDVLKGVSFTLRPGEVTALVGPSGSGKS----SCVSLLENFYLPQGGQVLLDGKPVNEFQHDYlHSKIALVGQEPVLF 367
Cdd:TIGR00956   72 KTFDILKPMDGLIKPGELTVVLGRPGSGCStllkTIASNTDGFHIGVEGVITYDGITPEEIKKHY-RGDVVYNAETDVHF 150

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   368 AR-TIKEnisyglsdvSMEMVVQAATKANAHDFITT----------------LPKGYDTSVGEKGLQ-LSGGQKQRVAIA 429
Cdd:TIGR00956  151 PHlTVGE---------TLDFAARCKTPQNRPDGVSReeyakhiadvymatygLSHTRNTKVGNDFVRgVSGGERKRVSIA 221

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   430 RALIRQPRVLILDEATSALDAESEHIVQQALNSIMQE--HTVLVIAHRLS--TVEKADNIIVIDRGQVAERGTHS---QL 502
Cdd:TIGR00956  222 EASLGGAKIQCWDNATRGLDSATALEFIRALKTSANIldTTPLVAIYQCSqdAYELFDKVIVLYEGYQIYFGPADkakQY 301

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 961964003   503 MATGGLYCKlvQRQvlgieTGAEVL----NPSETVRWK 536
Cdd:TIGR00956  302 FEKMGFKCP--DRQ-----TTADFLtsltSPAERQIKP 332
GguA NF040905
sugar ABC transporter ATP-binding protein;
259-449 5.86e-11

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 64.81  E-value: 5.86e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 259 DRKPKH-PADGTEapnsctgLVEFKDVTFAYPTRPETDVLKGVSFTLRPGEVTALVGPSGSGKSS-CVSLLENFYlpqG- 335
Cdd:NF040905 244 DRYPERtPKIGEV-------VFEVKNWTVYHPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTElAMSVFGRSY---Gr 313

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 336 ---GQVLLDGKPVnEFQ--HDYLHSKIALVGQEpvlfaR---------TIKENISY-GLSDVSMEMVV--QAATKAnAHD 398
Cdd:NF040905 314 nisGTVFKDGKEV-DVStvSDAIDAGLAYVTED-----RkgyglnlidDIKRNITLaNLGKVSRRGVIdeNEEIKV-AEE 386

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 961964003 399 FITTL----PkgydtSVGEKGLQLSGGQKQRVAIARALIRQPRVLILDEATSALD 449
Cdd:NF040905 387 YRKKMniktP-----SVFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGID 436
3a01203 TIGR00954
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...
 292-477 6.99e-11

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: 64.77  E-value: 6.99e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  292 PETDVL-KGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKpvnefqhdylhSKIALVGQEPVLFART 370
Cdd:TIGR00954 462 PNGDVLiESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAK-----------GKLFYVPQRPYMTLGT 530

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  371 IKENISY----------GLSDVSMEMVVQaatkaNAH-DFITTLPKGYDtSVGEKGLQLSGGQKQRVAIARALIRQPRVL 439
Cdd:TIGR00954 531 LRDQIIYpdssedmkrrGLSDKDLEQILD-----NVQlTHILEREGGWS-AVQDWMDVLSGGEKQRIAMARLFYHKPQFA 604

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 961964003  440 ILDEATSALDAEsehiVQQALNSIMQEH--TVLVIAHRLS 477
Cdd:TIGR00954 605 ILDECTSAVSVD----VEGYMYRLCREFgiTLFSVSHRKS 640
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
 278-479 8.09e-11

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 64.27  E-value: 8.09e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 278 LVEFKDVTFAYPTRPetdVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYlPQGgqvlldgkpvneFQHDYlhski 357
Cdd:PRK10938 260 RIVLNNGVVSYNDRP---ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDH-PQG------------YSNDL----- 318

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 358 alvgqepVLFART---------IKENISYGLSDVSMEMVV-------------------QAATKAN---AHDFITTLpkG 406
Cdd:PRK10938 319 -------TLFGRRrgsgetiwdIKKHIGYVSSSLHLDYRVstsvrnvilsgffdsigiyQAVSDRQqklAQQWLDIL--G 389

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 407 YDTSVGEKGLQ-LSGGQKQRVAIARALIRQPRVLILDEATSALDAESEHIVQQALNS-IMQEHTVLV------------I 472
Cdd:PRK10938 390 IDKRTADAPFHsLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVlISEGETQLLfvshhaedapacI 469


                 ....*..
gi 961964003 473 AHRLSTV 479
Cdd:PRK10938 470 THRLEFV 476
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
 300-494 1.08e-10

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 63.92  E-value: 1.08e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 300 VSFTLRPGEVTALVGPSGSGKSScvsLLENFY---LPQGGQVLLDGKPVNEFQ-------------HD------YLHSKI 357
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTE---LAETLYglrPARGGRIMLNGKEINALStaqrlarglvylpEDrqssglYLDAPL 358

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 358 -----ALVGQEPVLFARTIKENisyglsdvsmemvvqaATKANAHDFITTLPKGYDTSVGekglQLSGGQKQRVAIARAL 432
Cdd:PRK15439 359 awnvcALTHNRRGFWIKPAREN----------------AVLERYRRALNIKFNHAEQAAR----TLSGGNQQKVLIAKCL 418

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 961964003 433 IRQPRVLILDEATSALDAESEHIVQQALNSIMQEHT-VLVIAHRLSTVEK-ADNIIVIDRGQVA 494
Cdd:PRK15439 419 EASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVaVLFISSDLEEIEQmADRVLVMHQGEIS 482
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
300-501 1.53e-10

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 63.39  E-value: 1.53e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 300 VSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVN-EFQHDYLHSKIALV----GQEPVLFARTIKEN 374
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDiRSPRDAIRAGIMLCpedrKAEGIIPVHSVADN 351

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 375 --ISYGLSDVSMEMVVQAATKA-NAHDFITTL----PKGyDTSVGekglQLSGGQKQRVAIARALIRQPRVLILDEATSA 447
Cdd:PRK11288 352 inISARRHHLRAGCLINNRWEAeNADRFIRSLniktPSR-EQLIM----NLSGGNQQKAILGRWLSEDMKVILLDEPTRG 426

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 961964003 448 LD--AESEhIVQQALNSIMQEHTVLVIAHRLSTVEK-ADNIIVIDRGQVAERGTHSQ 501
Cdd:PRK11288 427 IDvgAKHE-IYNVIYELAAQGVAVLFVSSDLPEVLGvADRIVVMREGRIAGELAREQ 482
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
 292-455 2.22e-10

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 63.21  E-value: 2.22e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 292 PETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVN-EFQHDYLHSKIALVGQE-PVLFAR 369
Cdd:PRK10982   9 PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQElNLVLQR 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 370 TIKENISYGLSDVSMEMVVQAATKANAHDFITTLpkGYDTSVGEKGLQLSGGQKQRVAIARALIRQPRVLILDEATSAL- 448
Cdd:PRK10982  89 SVMDNMWLGRYPTKGMFVDQDKMYRDTKAIFDEL--DIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLt 166


                 ....*..
gi 961964003 449 DAESEHI 455
Cdd:PRK10982 167 EKEVNHL 173
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
 301-504 2.62e-10

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 62.72  E-value: 2.62e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 301 SFTLRPGEVTALVGPSGSGKSSCVSLLEnfylpqGGQVLLDGKPVNEFQHDYLHS-----KiaLVGQEpvlFARTIKENI 375
Cdd:PRK10938  23 SLTLNAGDSWAFVGANGSGKSALARALA------GELPLLSGERQSQFSHITRLSfeqlqK--LVSDE---WQRNNTDML 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 376 SYGLSDV--SMEMVVQAATKANAhdfittLPKGYDTSVGEKGL------QLSGGQKQRVAIARALIRQPRVLILDEATSA 447
Cdd:PRK10938  92 SPGEDDTgrTTAEIIQDEVKDPA------RCEQLAQQFGITALldrrfkYLSTGETRKTLLCQALMSEPDLLILDEPFDG 165

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 961964003 448 LDAESEHIVQQALNSIMQEHTVLV-IAHRLSTV-EKADNIIVIDRGQVAERGTHSQLMA 504
Cdd:PRK10938 166 LDVASRQQLAELLASLHQSGITLVlVLNRFDEIpDFVQFAGVLADCTLAETGEREEILQ 224
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 278-498 2.68e-10

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: 62.88  E-value: 2.68e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 278 LVEFKDVTFAYPtrpetdvlkgvSFTL-------RPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKpvnefqh 350
Cdd:COG1245  341 LVEYPDLTKSYG-----------GFSLeveggeiREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLK------- 402

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 351 dylhskialvgqepvlfartikenISYGLSDVS--MEMVVQAATKANAHDFITT------------LPKGYDTSVGEkgl 416
Cdd:COG1245  403 ------------------------ISYKPQYISpdYDGTVEEFLRSANTDDFGSsyykteiikplgLEKLLDKNVKD--- 455

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 417 qLSGGQKQRVAIARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQEH--TVLVIAHRLSTVEK-ADNIIVIDrGQV 493
Cdd:COG1245  456 -LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRgkTAMVVDHDIYLIDYiSDRLMVFE-GEP 533


                 ....*
gi 961964003 494 AERGT 498
Cdd:COG1245  534 GVHGH 538
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
 280-503 3.12e-10

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


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 63.20  E-value: 3.12e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   280 EFKDVTFAYPTRPETDV-LKGVSFTLRPGEVTALVGPSGSGKSS---CVSLLENFYLPQGGQVLLDGKPVNE-F------ 348
Cdd:TIGR00956  761 HWRNLTYEVKIKKEKRViLNNVDGWVKPGTLTALMGASGAGKTTllnVLAERVTTGVITGGDRLVNGRPLDSsFqrsigy 840

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   349 --QHDyLHSKIALVgQEPVLFAR--------TIKENISYglsdvsMEMVVQaatkanahdfITTLPKGYDTSVGEKGLQL 418
Cdd:TIGR00956  841 vqQQD-LHLPTSTV-RESLRFSAylrqpksvSKSEKMEY------VEEVIK----------LLEMESYADAVVGVPGEGL 902

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   419 SGGQKQRVAIARALIRQPRVLI-LDEATSALDAESEHIVQQALNSIMQE-HTVLVIAHRLSTV--EKADNIIVIDRG-QV 493
Cdd:TIGR00956  903 NVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADHgQAILCTIHQPSAIlfEEFDRLLLLQKGgQT 982

                          250
                   ....*....|...
gi 961964003   494 A---ERGTHSQLM 503
Cdd:TIGR00956  983 VyfgDLGENSHTI 995
PRK15093 PRK15093
peptide ABC transporter ATP-binding protein SapD;
417-505 4.81e-10

peptide ABC transporter ATP-binding protein SapD;


Pssm-ID: 185049 [Multi-domain]  Cd Length: 330  Bit Score: 61.36  E-value: 4.81e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 417 QLSGGQKQRVAIARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQEH--TVLVIAHRLSTVEK-ADNIIVIDRGQV 493
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNntTILLISHDLQMLSQwADKINVLYCGQT 237

                         90
                 ....*....|..
gi 961964003 494 AERGTHSQLMAT 505
Cdd:PRK15093 238 VETAPSKELVTT 249
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
 297-492 5.86e-10

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: 58.49  E-value: 5.86e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 297 LKGVSFTLRPGEVTALVGPSGSGKSSCVslLENFYlPQGGQVLLDGKPVNEfqhdylHSKIALVGQepvlFARTIKENIS 376
Cdd:cd03238   11 LQNLDVSIPLNVLVVVTGVSGSGKSTLV--NEGLY-ASGKARLISFLPKFS------RNKLIFIDQ----LQFLIDVGLG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 377 YglsdvsmemvvqaatkanahdfittLPKGYDTSVgekglqLSGGQKQRVAIARALIRQPR--VLILDEATSALDAESEH 454
Cdd:cd03238   78 Y-------------------------LTLGQKLST------LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDIN 126

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 961964003 455 IVQQALNSIMQE-HTVLVIAHRLSTVEKADNIIVIDRGQ 492
Cdd:cd03238  127 QLLEVIKGLIDLgNTVILIEHNLDVLSSADWIIDFGPGS 165
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
 305-485 7.17e-10

The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.


Pssm-ID: 213203 [Multi-domain]  Cd Length: 255  Bit Score: 59.69  E-value: 7.17e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 305 RPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQvlLDGKP-----VNEFQ----HDYLHS----------KIALVGQEPV 365
Cdd:cd03236   24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGK--FDDPPdwdeiLDEFRgselQNYFTKllegdvkvivKPQYVDLIPK 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 366 LFARTIKENIsyglsdvsmemvvqaaTKANAHDFITTLPKGYD-TSVGEKGL-QLSGGQKQRVAIARALIRQPRVLILDE 443
Cdd:cd03236  102 AVKGKVGELL----------------KKKDERGKLDELVDQLElRHVLDRNIdQLSGGELQRVAIAAALARDADFYFFDE 165

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 961964003 444 ATSALDAESEHIVQQALNSIMQE-HTVLVIAHRLSTVEK-ADNI 485
Cdd:cd03236  166 PSSYLDIKQRLNAARLIRELAEDdNYVLVVEHDLAVLDYlSDYI 209
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
 279-478 8.66e-10

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: 61.10  E-value: 8.66e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  279 VEFKDVTFAYPTRPetdVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLdGKPVnefqhdylhsKIA 358
Cdd:TIGR03719 323 IEAENLTKAFGDKL---LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV----------KLA 388

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  359 LVGQ--EPVLFARTIKENISYGLsDVSMEMVVQAATKA--NAHDFittlpKGYDTS--VGekglQLSGGQKQRVAIARAL 432
Cdd:TIGR03719 389 YVDQsrDALDPNKTVWEEISGGL-DIIKLGKREIPSRAyvGRFNF-----KGSDQQkkVG----QLSGGERNRVHLAKTL 458

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 961964003  433 IRQPRVLILDEATSALDAESehivQQALNSIMQEH--TVLVIAH------RLST 478
Cdd:TIGR03719 459 KSGGNVLLLDEPTNDLDVET----LRALEEALLNFagCAVVISHdrwfldRIAT 508
PLN03140 PLN03140
ABC transporter G family member; Provisional
 296-498 1.29e-09

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 61.40  E-value: 1.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  296 VLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENF----YLPqgGQVLLDGKPVNE--F--------QHDyLHSKIALVG 361
Cdd:PLN03140  895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRktggYIE--GDIRISGFPKKQetFarisgyceQND-IHSPQVTVR 971

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  362 QEPVL--FARTIKENISYG---LSDVSMEMVvqaaTKANAHDFITTLPkgydtsvGEKGLqlSGGQKQRVAIARALIRQP 436
Cdd:PLN03140  972 ESLIYsaFLRLPKEVSKEEkmmFVDEVMELV----ELDNLKDAIVGLP-------GVTGL--STEQRKRLTIAVELVANP 1038

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 961964003  437 RVLILDEATSALDAESEHIVQQAL-NSIMQEHTVLVIAHRLS--TVEKADNIIVIDR-GQVAERGT 498
Cdd:PLN03140 1039 SIIFMDEPTSGLDARAAAIVMRTVrNTVDTGRTVVCTIHQPSidIFEAFDELLLMKRgGQVIYSGP 1104
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
 297-494 1.32e-09

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 60.51  E-value: 1.32e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 297 LKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPV-NEFQHDYLHSKIALVGQE----------PV 365
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKInNHNANEAINHGFALVTEErrstgiyaylDI 343

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 366 LFARTIKENISYG-----LSDVSMEMVVQAATkanahDFITTLPKGYDTSVGekglQLSGGQKQRVAIARALIRQPRVLI 440
Cdd:PRK10982 344 GFNSLISNIRNYKnkvglLDNSRMKSDTQWVI-----DSMRVKTPGHRTQIG----SLSGGNQQKVIIGRWLLTQPEILM 414

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 961964003 441 LDEATSALDAESEHIVQQALNSIMQEHT-VLVIAHRL-STVEKADNIIVIDRGQVA 494
Cdd:PRK10982 415 LDEPTRGIDVGAKFEIYQLIAELAKKDKgIIIISSEMpELLGITDRILVMSNGLVA 470
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
 297-506 1.76e-09

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: 58.78  E-value: 1.76e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 297 LKGVSFTLRPGEVTALVGPSGSGKSScvslLENFYLPQGGQVLLDGKPVNEFQHDYLH-----SKIALVGQEPVlfARTI 371
Cdd:cd03271   11 LKNIDVDIPLGVLTCVTGVSGSGKSS----LINDTLYPALARRLHLKKEQPGNHDRIEglehiDKVIVIDQSPI--GRTP 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 372 KEN------------------------------ISY---GLSDVsMEMVVQAAtkanaHDFITTLPK------------- 405
Cdd:cd03271   85 RSNpatytgvfdeirelfcevckgkrynretleVRYkgkSIADV-LDMTVEEA-----LEFFENIPKiarklqtlcdvgl 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 406 GYDTsVGEKGLQLSGGQKQRVAIARALIRQPR---VLILDEATSALDAESEHIVQQALNSIM-QEHTVLVIAHRLSTVEK 481
Cdd:cd03271  159 GYIK-LGQPATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQRLVdKGNTVVVIEHNLDVIKC 237

                        250       260
                 ....*....|....*....|....*.
gi 961964003 482 ADNIivIDRG-QVAERGthSQLMATG 506
Cdd:cd03271  238 ADWI--IDLGpEGGDGG--GQVVASG 259
ABC_6TM_MRP7_D2_like cd18605
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ...
 7-170 1.76e-09

Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).


Pssm-ID: 350049 [Multi-domain]  Cd Length: 300  Bit Score: 59.08  E-value: 1.76e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   7 FTLFFLLSSMAIGVRGGVFTLTMARLNV--------RLRSRLFRTLMTQEIAFFDENHTGDILSRLSADTTQVSDLISQN 78
Cdd:cd18605   40 SFNFFLTVYGFLAGLNSLFTLLRAFLFAygglraarRLHNKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFI 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  79 VNVFLRSVIKGTGFIIfmfrmswkltlVTMMGFPFIALV----SKLY---GEYYKKLTKEVQTVLAEAN-KVAE---ETI 147
Cdd:cd18605  120 LNILLAQLFGLLGYLV-----------VICYQLPWLLLLllplAFIYyriQRYYRATSRELKRLNSVNLsPLYThfsETL 188

                        170       180
                 ....*....|....*....|...
gi 961964003 148 SGMRTVRSFANESREANSYYAKL 170
Cdd:cd18605  189 KGLVTIRAFRKQERFLKEYLEKL 211
PRK13543 PRK13543
heme ABC exporter ATP-binding protein CcmA;
269-467 3.37e-09

heme ABC exporter ATP-binding protein CcmA;


Pssm-ID: 184129 [Multi-domain]  Cd Length: 214  Bit Score: 57.17  E-value: 3.37e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 269 TEAPNSCTGLVEFKDVTFAyptRPETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEF 348
Cdd:PRK13543   2 IEPLHTAPPLLAAHALAFS---RNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 349 QHDylhSKIALVGQEPVLFAR-TIKENISY--GLSDV-SMEMVVQAATKANAHDFITTLPKgydtsvgekglQLSGGQKQ 424
Cdd:PRK13543  79 DRS---RFMAYLGHLPGLKADlSTLENLHFlcGLHGRrAKQMPGSALAIVGLAGYEDTLVR-----------QLSAGQKK 144

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 961964003 425 RVAIARALIRQPRVLILDEATSALDAESEHIVqqalNSIMQEH 467
Cdd:PRK13543 145 RLALARLWLSPAPLWLLDEPYANLDLEGITLV----NRMISAH 183
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
303-488 4.09e-09

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 59.05  E-value: 4.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 303 TLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVllDGKPvnefqhdylhskialvGQEPVL--FARTIKENISYGLS 380
Cdd:PRK13409  95 IPKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDY--EEEP----------------SWDEVLkrFRGTELQNYFKKLY 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 381 DVSmemvVQAATKANAHDFIttlPKGYDTSVG-------EKGL-------------------QLSGGQKQRVAIARALIR 434
Cdd:PRK13409 157 NGE----IKVVHKPQYVDLI---PKVFKGKVRellkkvdERGKldevverlglenildrdisELSGGELQRVAIAAALLR 229

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 961964003 435 QPRVLILDEATSALDAESEHIVQQALNSIMQEHTVLVIAHRLSTVEK-ADNIIVI 488
Cdd:PRK13409 230 DADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDLAVLDYlADNVHIA 284
ABC_6TM_T1SS_like cd18779
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ...
 7-223 8.07e-09

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: 57.17  E-value: 8.07e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   7 FTLFFLLSSMaigVRGGVFTLTMARLNVRLRSRLFRTLMTQEIAFFDENHTGDILSRLSADTTqVSDLISQNVnvfLRSV 86
Cdd:cd18779   51 LVLTQLLAGL---LRSHLLLRLRTRLDTQLTLGFLEHLLRLPYRFFQQRSTGDLLMRLSSNAT-IRELLTSQT---LSAL 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  87 IKGT---GFIIFMFRMSWKLTLVTM-MGFPFIALVSKLYGEYyKKLTKEVQTVLAEANKVAEETISGMRTVRSFANESRE 162
Cdd:cd18779  124 LDGTlvlGYLALLFAQSPLLGLVVLgLAALQVALLLATRRRV-RELMARELAAQAEAQSYLVEALSGIETLKASGAEDRA 202

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 961964003 163 ----ANSYYAKLLVMFQLNKKQALAYACymwSSCISELAlEVAVLYYGGHLVLTDQLSSGGLISF 223
Cdd:cd18779  203 ldrwSNLFVDQLNASLRRGRLDALVDAL---LATLRLAA-PLVLLWVGAWQVLDGQLSLGTMLAL 263
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
 280-474 1.94e-08

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 57.27  E-value: 1.94e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 280 EFKDVTFAYPTRpetDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGK-PVNEF-QHdylhsKI 357
Cdd:PRK11147 321 EMENVNYQIDGK---QLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKlEVAYFdQH-----RA 392

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 358 ALvgqEPvlfARTIKENISYGLSDVsmeMVvqaatkaNA---H------DFITTlPKGYDTSVGekglQLSGGQKQRVAI 428
Cdd:PRK11147 393 EL---DP---EKTVMDNLAEGKQEV---MV-------NGrprHvlgylqDFLFH-PKRAMTPVK----ALSGGERNRLLL 451

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 961964003 429 ARALIRQPRVLILDEATSALDAESEHIVQQALNSImqEHTVLVIAH 474
Cdd:PRK11147 452 ARLFLKPSNLLILDEPTNDLDVETLELLEELLDSY--QGTVLLVSH 495
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
238-495 2.93e-08

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 56.33  E-value: 2.93e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 238 ASVYSGLMQGVGAAEKVFEYLDR--KPKHPADGTEAPNSCTGLV-EFKDVTfayptRPETDVLKGVSFTLRPGEVTALVG 314
Cdd:PRK09700 222 SSVCSGMVSDVSNDDIVRLMVGRelQNRFNAMKENVSNLAHETVfEVRNVT-----SRDRKKVRDISFSVCRGEILGFAG 296

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 315 PSGSGKSSCVSLLENFYLPQGGQVLLDGKPVN-EFQHDYLHSKIALVGQ---EPVLFAR-TIKENIS------------- 376
Cdd:PRK09700 297 LVGSGRTELMNCLFGVDKRAGGEIRLNGKDISpRSPLDAVKKGMAYITEsrrDNGFFPNfSIAQNMAisrslkdggykga 376

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 377 YGLSDVSMEmvvqAATKANAHDFITTLPKGYDTSVGEkglqLSGGQKQRVAIARALIRQPRVLILDEATSALDAESEHIV 456
Cdd:PRK09700 377 MGLFHEVDE----QRTAENQRELLALKCHSVNQNITE----LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEI 448

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 961964003 457 QQALNSIMQE-HTVLVIAHRLSTV-EKADNIIVIDRGQVAE 495
Cdd:PRK09700 449 YKVMRQLADDgKVILMVSSELPEIiTVCDRIAVFCEGRLTQ 489
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 303-488 3.03e-08

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: 56.33  E-value: 3.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 303 TLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVllDGKP-----VNEFQ----HDYLHS----------KIALVGQE 363
Cdd:COG1245   95 VPKKGKVTGILGPNGIGKSTALKILSGELKPNLGDY--DEEPswdevLKRFRgtelQDYFKKlangeikvahKPQYVDLI 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 364 PVLFARTIKENisygLSDVSMEMVV-QAATKANahdfittLPKGYDTSVGEkglqLSGGQKQRVAIARALIRQPRVLILD 442
Cdd:COG1245  173 PKVFKGTVREL----LEKVDERGKLdELAEKLG-------LENILDRDISE----LSGGELQRVAIAAALLRDADFYFFD 237

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 961964003 443 EATSALDaesehiVQQALN--SIMQE-----HTVLVIAHRLSTVEK-ADNIIVI 488
Cdd:COG1245  238 EPSSYLD------IYQRLNvaRLIRElaeegKYVLVVEHDLAILDYlADYVHIL 285
PLN03140 PLN03140
ABC transporter G family member; Provisional
 296-510 6.38e-08

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 55.62  E-value: 6.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  296 VLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQ---GGQVLLDGKPVNEF----------QHDyLHSKIALVgQ 362
Cdd:PLN03140  180 ILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSlkvSGEITYNGYRLNEFvprktsayisQND-VHVGVMTV-K 257

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  363 EPVLF-----------------ARTIKENISYGLSDVSMEMVVQAATKANAHDF------ITTLPKGYDTSVGEKGLQ-L 418
Cdd:PLN03140  258 ETLDFsarcqgvgtrydllselARREKDAGIFPEAEVDLFMKATAMEGVKSSLItdytlkILGLDICKDTIVGDEMIRgI 337

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  419 SGGQKQRVAIARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQ--EHTVLV--IAHRLSTVEKADNIIVIDRGQVA 494
Cdd:PLN03140  338 SGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHltEATVLMslLQPAPETFDLFDDIILLSEGQIV 417

                         250
                  ....*....|....*....
gi 961964003  495 ERGTHSQLMA---TGGLYC 510
Cdd:PLN03140  418 YQGPRDHILEffeSCGFKC 436
PLN03073 PLN03073
ABC transporter F family; Provisional
 265-494 9.18e-08

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 54.87  E-value: 9.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 265 PADGTEAPnsctgLVEFKDVTFAYPTRPEtdVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKp 344
Cdd:PLN03073 500 PDDRPGPP-----IISFSDASFGYPGGPL--LFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAK- 571

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 345 vnefqhdylhSKIALVGQEPVlfartikenisYGLSDVSMEMVVQA-------ATKANAHdfittlpKGYDTSVGEKGLQ 417
Cdd:PLN03073 572 ----------VRMAVFSQHHV-----------DGLDLSSNPLLYMMrcfpgvpEQKLRAH-------LGSFGVTGNLALQ 623

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 418 ----LSGGQKQRVAIARALIRQPRVLILDEATSALDAESEHIVQQALnsIMQEHTVLVIAHRLSTVE-KADNIIVIDRGQ 492
Cdd:PLN03073 624 pmytLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGL--VLFQGGVLMVSHDEHLISgSVDELWVVSEGK 701


                 ..
gi 961964003 493 VA 494
Cdd:PLN03073 702 VT 703
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
 302-493 1.06e-07

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 54.57  E-value: 1.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 302 FTLRPGEVTALVGPSGSGKSSCVSLLenfylpqGGQVLLDGKPVNeFQHDYlhsKIALVGQEPvlfARTIKEN----ISY 377
Cdd:PRK11147  24 LHIEDNERVCLVGRNGAGKSTLMKIL-------NGEVLLDDGRII-YEQDL---IVARLQQDP---PRNVEGTvydfVAE 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 378 GL------------------SDVSMEMVVQAAT------KANA-------HDFITTLPKGYDTSVGEkglqLSGGQKQRV 426
Cdd:PRK11147  90 GIeeqaeylkryhdishlveTDPSEKNLNELAKlqeqldHHNLwqlenriNEVLAQLGLDPDAALSS----LSGGWLRKA 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 961964003 427 AIARALIRQPRVLILDEATSALDAESEHIVQQALNSImqEHTVLVIAHRLSTVEK-ADNIIVIDRGQV 493
Cdd:PRK11147 166 ALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTF--QGSIIFISHDRSFIRNmATRIVDLDRGKL 231
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
 303-490 1.72e-07

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: 51.21  E-value: 1.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 303 TLRPGEVTALVGPSGSGKSScvsllenfylpqggqvlldgkpvnefqhdYLHSKIALVGQEPVLFARTIKENISYGLSDV 382
Cdd:cd03227   17 TFGEGSLTIITGPNGSGKST-----------------------------ILDAIGLALGGAQSATRRRSGVKAGCIVAAV 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 383 SMEmvvqaatkanahdFITTLPkgydtsvgekglQLSGGQKQRVAIARALI---RQPRVL-ILDEATSALDAESEHIVQQ 458
Cdd:cd03227   68 SAE-------------LIFTRL------------QLSGGEKELSALALILAlasLKPRPLyILDEIDRGLDPRDGQALAE 122

                        170       180       190
                 ....*....|....*....|....*....|...
gi 961964003 459 ALNSIMQEH-TVLVIAHRLSTVEKADNIIVIDR 490
Cdd:cd03227  123 AILEHLVKGaQVIVITHLPELAELADKLIHIKK 155
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
410-507 2.21e-07

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 53.20  E-value: 2.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 410 SVGEKGLQLSGGQKQRVAIARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQE-HTVLVIAHRLSTVEK-ADNIIV 487
Cdd:NF000106 137 AAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDgATVLLTTQYMEEAEQlAHELTV 216

                         90       100
                 ....*....|....*....|
gi 961964003 488 IDRGQVAERGTHSQLMATGG 507
Cdd:NF000106 217 IDRGRVIADGKVDELKTKVG 236
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
 416-501 2.31e-07

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


Pssm-ID: 213189 [Multi-domain]  Cd Length: 177  Bit Score: 51.03  E-value: 2.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 416 LQLSGGQKQRVAIARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQE--HTVLVIAHRLSTVEKADNIIVIDRGQV 493
Cdd:cd03222   70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEgkKTALVVEHDLAVLDYLSDRIHVFEGEP 149


                 ....*...
gi 961964003 494 AERGTHSQ 501
Cdd:cd03222  150 GVYGIASQ 157
PRK13541 PRK13541
cytochrome c biogenesis protein CcmA; Provisional
 293-482 4.74e-07

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184128 [Multi-domain]  Cd Length: 195  Bit Score: 50.26  E-value: 4.74e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 293 ETDVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHDYLhskiALVGQEPVL-FARTI 371
Cdd:PRK13541  12 EQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYC----TYIGHNLGLkLEMTV 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 372 KENISYgLSDV--SMEMVVQAATKANAHDFITtlpkgydtsvgEKGLQLSGGQKQRVAIARALIRQPRVLILDEATSALD 449
Cdd:PRK13541  88 FENLKF-WSEIynSAETLYAAIHYFKLHDLLD-----------EKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLS 155

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 961964003 450 AESEHIvqqaLNSIMQEHT-----VLVIAHRLSTVEKA 482
Cdd:PRK13541 156 KENRDL----LNNLIVMKAnsggiVLLSSHLESSIKSA 189
ABC_6TM_SUR1_D2_like cd18602
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ...
 7-161 5.16e-07

Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group represents the six-transmembrane domain 2 (TMD2) of the sulphonylurea receptors SUR1/2 (ABCC8), which function as a modulator of ATP-sensitive potassium channels and insulin release, and belong to the ABCC subfamily. The ATP-sensitive (K-ATP) channel is an octameric complex of four pore-forming Kir6.2 subunits and four regulatory SUR subunits. Thus, in contrast to other ABC transporters, the SUR serves as the regulatory subunit of an ion channel. Mutations and deficiencies in the SUR proteins have been observed in patients with hyperinsulinemic hypoglycemia of infancy, an autosomal recessive disorder of unregulated and high insulin secretion. Mutations have also been associated with non-insulin-dependent diabetes mellitus type 2, an autosomal dominant disease of defective insulin secretion.


Pssm-ID: 350046 [Multi-domain]  Cd Length: 307  Bit Score: 51.45  E-value: 5.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   7 FTLFFLLSSMAI---GVRGGVFTLTMARLNVRLRSRLFRTLMTQEIAFFDENHTGDILSRLSADTTQVSDLISQNVNVFL 83
Cdd:cd18602   53 ISVYAGLSLGAVilsLVTNLAGELAGLRAARRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLL 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  84 RSVIK-GTGFIIFMFRMSWKLTLVtmmgFPfIALVSKLYGEYYKKLTKEVQ--------TVLAEANkvaeETISGMRTVR 154
Cdd:cd18602  133 RFLLLcLSAIIVNAIVTPYFLIAL----IP-IIIVYYFLQKFYRASSRELQrldnitksPVFSHFS----ETLGGLTTIR 203


                 ....*..
gi 961964003 155 SFANESR 161
Cdd:cd18602  204 AFRQQAR 210
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
 279-451 1.16e-06

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 51.27  E-value: 1.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 279 VEFKDVTFAYPTRpetdVL-KGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLdGKPVnefqhdylhsKI 357
Cdd:PRK11819 325 IEAENLSKSFGDR----LLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV----------KL 389

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 358 ALVGQ-----EPvlfARTIKENISYGLsDVSMEMVVQAATKA--NAHDFittlpKGYDTS--VGekglQLSGGQKQRVAI 428
Cdd:PRK11819 390 AYVDQsrdalDP---NKTVWEEISGGL-DIIKVGNREIPSRAyvGRFNF-----KGGDQQkkVG----VLSGGERNRLHL 456

                        170       180
                 ....*....|....*....|...
gi 961964003 429 ARALIRQPRVLILDEATSALDAE 451
Cdd:PRK11819 457 AKTLKQGGNVLLLDEPTNDLDVE 479
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
 297-486 1.28e-06

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: 51.55  E-value: 1.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  297 LKGVSFTLRPGEVTALVGPSGSGKSSCVS-----LLENFyLPQGGQVLLDGKPVNEFQHdylHSKIALVGQEPV------ 365
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTLINdtlypALANR-LNGAKTVPGRYTSIEGLEH---LDKVIHIDQSPIgrtprs 699

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  366 --------------LFARTiKE-------------NISYG-----------------LSDVSMEMVVQAATKAN------ 395
Cdd:TIGR00630 700 npatytgvfdeireLFAET-PEakvrgytpgrfsfNVKGGrceacqgdgvikiemhfLPDVYVPCEVCKGKRYNretlev 778

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  396 -----------------AHDFITTLPK-------------GYdTSVGEKGLQLSGGQKQRVAIARALIRQ---PRVLILD 442
Cdd:TIGR00630 779 kykgkniadvldmtveeAYEFFEAVPSisrklqtlcdvglGY-IRLGQPATTLSGGEAQRIKLAKELSKRstgRTLYILD 857

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 961964003  443 EATSALDAESehiVQQALNSIM----QEHTVLVIAHRLSTVEKADNII 486
Cdd:TIGR00630 858 EPTTGLHFDD---IKKLLEVLQrlvdKGNTVVVIEHNLDVIKTADYII 902
ABC_6TM_NHLM_bacteriocin cd18569
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; ...
 9-223 3.08e-06

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: 49.01  E-value: 3.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   9 LFFLLSSMAI--GVRGGVFTL---TMARLNVRL----RSRLFRTLMTQEIAFFDENHTGDILSRLSAdTTQVSDLISQNV 79
Cdd:cd18569   41 LRPLLLGMALtaLLQGLLTWLqqyYLLRLETKLalssSSRFFWHVLRLPVEFFSQRYAGDIASRVQS-NDRVANLLSGQL 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  80 NVFLRSVIKGTGFIIFMFRMSWKLTLVTMmgfpFIALVSKLYGEYY-KKLTKEVQTVLAEANKVAEETISGMR---TVRS 155
Cdd:cd18569  120 ATTVLNLVMAVFYALLMLQYDVPLTLIGI----AIALLNLLVLRLVsRKRVDLNRRLLQDSGKLTGTTMSGLQmieTLKA 195

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 961964003 156 FANES----REAnSYYAKLlvmfqLNKKQALAyacyMWSSCISEL-----AL-EVAVLYYGGHLVLTDQLSSGGLISF 223
Cdd:cd18569  196 SGAESdffsRWA-GYQAKV-----LNAQQELG----RTNQLLGALptllsALtNAAILGLGGLLVMDGALTIGMLVAF 263
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
 418-486 3.26e-06

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 50.21  E-value: 3.26e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 961964003  418 LSGGQKQRVAIARALI---RQPRVLILDEATSALDAESEHIVQQALNSIM-QEHTVLVIAHRLSTVEKADNII 486
Cdd:PRK00635  810 LSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLHTHDIKALIYVLQSLThQGHTVVIIEHNMHVVKVADYVL 882
ABC_6TM_YOR1_D2_like cd18606
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ...
 7-161 3.98e-06

Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.


Pssm-ID: 350050 [Multi-domain]  Cd Length: 290  Bit Score: 48.63  E-value: 3.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   7 FTLFFLLSSMAIGVRGGvftltmARLNVRLRSRLFRTLMtqeiAFFDENHTGDILSRLSADTTQVSDLISQNVNVFLRSV 86
Cdd:cd18606   51 FLFLFGLLLAYLGIRAS------KRLHNKALKRVLRAPM----SFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTL 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  87 IKGTGFIIfmfrmswkLTLVTM----MGFPFIALVSKLYGEYYKKLTKEVQ--------TVLAEANkvaeETISGMRTVR 154
Cdd:cd18606  121 SSIIGTFI--------LIIIYLpwfaIALPPLLVLYYFIANYYRASSRELKrlesilrsFVYANFS----ESLSGLSTIR 188


                 ....*..
gi 961964003 155 SFANESR 161
Cdd:cd18606  189 AYGAQDR 195
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
 276-480 6.84e-06

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


Pssm-ID: 130324 [Multi-domain]  Cd Length: 2272  Bit Score: 49.24  E-value: 6.84e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   276 TGLVEFKDVTFAYP--TRPETDVLkgvSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQHDyL 353
Cdd:TIGR01257 1935 TDILRLNELTKVYSgtSSPAVDRL---CVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISD-V 2010

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   354 HSKIA-----------LVGQEPV-LFARtikenisygLSDVSMEMVVQAATKAnahdfITTLpkGYDTSVGEKGLQLSGG 421
Cdd:TIGR01257 2011 HQNMGycpqfdaiddlLTGREHLyLYAR---------LRGVPAEEIEKVANWS-----IQSL--GLSLYADRLAGTYSGG 2074

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   422 QKQRVAIARALIRQPRVLILDEATSALDAESEHIVQQALNSIMQE-HTVLVIAHRLSTVE 480
Cdd:TIGR01257 2075 NKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREgRAVVLTSHSMEECE 2134
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
 279-508 1.58e-05

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 47.58  E-value: 1.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 279 VEFKDVTFAYPTRPetdVLKGVSFTLRPGEVTALVGPSGSGKSSCVSLLenfylpqggqvlldgkpVNEFQHDylhskia 358
Cdd:PRK15064 320 LEVENLTKGFDNGP---LFKNLNLLLEAGERLAIIGENGVGKTTLLRTL-----------------VGELEPD------- 372

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 359 lvgqepvlfARTIK--EN--ISYGLSDVSMEMvvqaATKANAHDFIT--TLPKGYDTSV--------------GEKGLQL 418
Cdd:PRK15064 373 ---------SGTVKwsENanIGYYAQDHAYDF----ENDLTLFDWMSqwRQEGDDEQAVrgtlgrllfsqddiKKSVKVL 439

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 419 SGGQKQRVAIARALIRQPRVLILDEATSALDAESEHIVQQALNsiMQEHTVLVIAHRLSTVEK-ADNIIVI-DRGQVAER 496
Cdd:PRK15064 440 SGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALE--KYEGTLIFVSHDREFVSSlATRIIEItPDGVVDFS 517

                        250
                 ....*....|..
gi 961964003 497 GTHSQLMATGGL 508
Cdd:PRK15064 518 GTYEEYLRSQGI 529
ABC_6TM_peptidase_like cd18571
Six-transmembrane helical domain (6-TMD) of an uncharacterized peptidase ABC transporter and ...
 9-110 2.06e-05

Six-transmembrane helical domain (6-TMD) of an uncharacterized peptidase ABC transporter and similar proteins; This group includes the 6-TMD of an uncharacterized peptidase-containing ABC transporter of T1SS (type 1 secretion systems), similar to heterocyst differentiation protein HetC. HetC 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: 350015 [Multi-domain]  Cd Length: 294  Bit Score: 46.67  E-value: 2.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   9 LFFLLSSMAIG-VRGGVFTLTMARLNVRLRSRLFRTLMTQEIAFFDENHTGDILSRLSaDTTQVSDLISQNVNVFLRSVI 87
Cdd:cd18571   49 LVLFLGSTSIEfIRSWILLHISSRINISIISDFLIKLMRLPISFFDTKMTGDILQRIN-DHSRIESFLTSSSLSILFSLL 127

                         90       100
                 ....*....|....*....|....*.
gi 961964003  88 kgtGFIIF---MFRMSWKLTLVTMMG 110
Cdd:cd18571  128 ---NLIVFsivLAYYNLTIFLIFLIG 150
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
297-506 4.20e-05

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 46.66  E-value: 4.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 297 LKGVSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEFQH-DYLHSKIALVGQ------EPVLfar 369
Cdd:NF033858  17 LDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHrRAVCPRIAYMPQglgknlYPTL--- 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 370 TIKENIS-----YGLSDVSMEMVVQAATKAnahdfiTTL------PKGydtsvgekglQLSGGQKQRVAIARALIRQPRV 438
Cdd:NF033858  94 SVFENLDffgrlFGQDAAERRRRIDELLRA------TGLapfadrPAG----------KLSGGMKQKLGLCCALIHDPDL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 439 LILDEATSALDAES-----EHIvqqalNSIMQEH---TVLViahrlST--VEKA---DNIIVIDRGQVAERGTHSQLMA- 504
Cdd:NF033858 158 LILDEPTTGVDPLSrrqfwELI-----DRIRAERpgmSVLV-----ATayMEEAerfDWLVAMDAGRVLATGTPAELLAr 227


                 ..
gi 961964003 505 TG 506
Cdd:NF033858 228 TG 229
ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 cd18560
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ...
 7-248 5.62e-05

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: 45.29  E-value: 5.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   7 FTLFFLLSSMAIGVRGGVFTLTMARLNVRLRSRLFRTLMTQEIAFFDENHTGDILSRLSADTTQVSDLISQNV-NVFLRS 85
Cdd:cd18560   44 YALLRFSSKLLKELRSLLYRRVQQNAYRELSLKTFAHLHSLSLDWHLSKKTGEVVRIMDRGTESANTLLSYLVfYLVPTL 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  86 VIKGTGFIIFMFRMSWKLTLVTmmgfpFIALVskLYGEYYKKLT-------KEVQTVLAEANKVAEETISGMRTVRSFAN 158
Cdd:cd18560  124 LELIVVSVVFAFHFGAWLALIV-----FLSVL--LYGVFTIKVTewrtkfrRAANKKDNEAHDIAVDSLLNFETVKYFTN 196

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 159 ESREANSYYAKLLVMFQLNKKQALAYACYMWS-SCISELALeVAVLYYGGHLVLTDQLSSGGLISFFIYMLELGECFESI 237
Cdd:cd18560  197 EKYEVDRYGEAVKEYQKSSVKVQASLSLLNVGqQLIIQLGL-TLGLLLAGYRVVDGGLSVGDFVAVNTYIFQLFQPLNFL 275

                        250
                 ....*....|.
gi 961964003 238 ASVYSGLMQGV 248
Cdd:cd18560  276 GTIYRMIIQSL 286
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
 388-491 6.26e-05

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 45.98  E-value: 6.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  388 VQAATKANAHDFITTLPKGYDTSvgekglQLSGGQKQRVAIARALI---RQPRVLILDEATSALDAESEHIVQQALNS-I 463
Cdd:PRK00635 1676 IQKPLQALIDNGLGYLPLGQNLS------SLSLSEKIAIKIAKFLYlppKHPTLFLLDEIATSLDNQQKSALLVQLRTlV 1749

                          90       100
                  ....*....|....*....|....*...
gi 961964003  464 MQEHTVLVIAHRLSTVEKADNIIVIDRG 491
Cdd:PRK00635 1750 SLGHSVIYIDHDPALLKQADYLIEMGPG 1777
ABC_6TM_HMT1 cd18583
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents ...
 35-246 6.49e-05

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: 44.83  E-value: 6.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  35 RLRSRLFRTLMTQEIAFFDENHTGDILSRLSAdttqvsdliSQNVNVFLRSVI---------KGTGFIIFMFRMSWKLTL 105
Cdd:cd18583   71 ALSTAAFNHVMNLSMDFHDSKKSGEVLKAIEQ---------GSSINDLLEQILfqivpmiidLVIAIVYLYYLFDPYMGL 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 106 -VTMMGFPFIALVSKLyGEYYKKLTKEVQTVLAEANKVAEETISGMRTVRSFANESREaNSYYAKLLVMFQLNKKQalay 184
Cdd:cd18583  142 iVAVVMVLYVWSTIKL-TSWRTKLRRDMIDADREERSILTESLLNWETVKYFNREPYE-KERYREAVKNYQKAERK---- 215

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 961964003 185 acYMWSSCISELALE-------VAVLYYGGHLVLTDQLSSGGLISFFIYMLELGECFESIASVYSGLMQ 246
Cdd:cd18583  216 --YLFSLNLLNAVQSliltlglLAGCFLAAYQVSQGQATVGDFVTLLTYWAQLSGPLNFFATLYRSIQS 282
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 417-486 1.20e-04

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 44.96  E-value: 1.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   417 QLSGGQKQRVAIarALI-----RQPRVL-ILDEATSALDAesEHIvqQALNSIMQEHT----VLVIAHRLSTVEKADNII 486
Cdd:pfam02463 1077 LLSGGEKTLVAL--ALIfaiqkYKPAPFyLLDEIDAALDD--QNV--SRVANLLKELSknaqFIVISLREEMLEKADKLV 1150
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
 417-490 1.21e-04

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


Pssm-ID: 213207 [Multi-domain]  Cd Length: 204  Bit Score: 43.36  E-value: 1.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 417 QLSGGQKQ------RVAIARALIRQPRVLILDEATSALDAESehiVQQALNSIMQEHT------VLVIAHRLSTVEKADN 484
Cdd:cd03240  115 RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEEN---IEESLAEIIEERKsqknfqLIVITHDEELVDAADH 191


                 ....*.
gi 961964003 485 IIVIDR 490
Cdd:cd03240  192 IYRVEK 197
ABC_6TM_ATM1_ABCB7 cd18582
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ...
 12-248 1.72e-04

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: 43.64  E-value: 1.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  12 LLSSMAIGVRGGVFTLTMARLNVRLRSRLFRTLMTQEIAFFDENHTGDILSRLSADTTQVSDLISQNVNVFLRSVIKGTG 91
Cdd:cd18582   49 ILSSLFNELRDALFARVSQRAVRRLALRVFRHLHSLSLRFHLSRKTGALSRAIERGTRGIEFLLRFLLFNILPTILELLL 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  92 FIIFMFRM-SWK---LTLVTMMGFpfiALVSKLYGEYYKKLTKEVQTVLAEANKVAEETISGMRTVRSFANESREANSY- 166
Cdd:cd18582  129 VCGILWYLyGWSyalITLVTVALY---VAFTIKVTEWRTKFRREMNEADNEANAKAVDSLLNYETVKYFNNEEYEAERYd 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 167 -----YAKLLVMFQ-----LNKKQALAYACYMwssciselaleVAVLYYGGHLVLTDQLSSGGLISFFIYMLELGECFES 236
Cdd:cd18582  206 kalakYEKAAVKSQtslalLNIGQALIISLGL-----------TAIMLLAAQGVVAGTLTVGDFVLVNTYLLQLYQPLNF 274

                        250
                 ....*....|..
gi 961964003 237 IASVYSGLMQGV 248
Cdd:cd18582  275 LGFVYREIRQSL 286
ABC_6TM_MRP4_D2_like cd18601
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ...
 8-161 2.26e-04

Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).


Pssm-ID: 350045 [Multi-domain]  Cd Length: 314  Bit Score: 43.46  E-value: 2.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   8 TLFFLLSSMaigvRGGVFTLTMARLNVRLRSRLFRTLMTQEIAFFDENHTGDILSRLSADTTQVSDLISQNVNVFLRSVI 87
Cdd:cd18601   70 AATFVFGFL----RSLLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLLL 145

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 961964003  88 KGTG-FIIFMFRMSWKLTLVTMMGFPFIALVSklygeYYKKLTKEVQTVLAEANKVA----EETISGMRTVRSFANESR 161
Cdd:cd18601  146 QVVGvVLLAVVVNPWVLIPVIPLVILFLFLRR-----YYLKTSREVKRIEGTTRSPVfshlSSTLQGLWTIRAYSAQER 219
ABC_6TM_MRP5_8_9_D2 cd18599
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ...
 9-117 3.05e-04

Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).


Pssm-ID: 350043 [Multi-domain]  Cd Length: 313  Bit Score: 42.94  E-value: 3.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   9 LFFLLSSMaigVRGGVFTLTMARLNVRLRSRLFRTLMTQEIAFFDENHTGDILSRLSADTTQVSDLISQNVNVFLRSVIk 88
Cdd:cd18599   69 LVILLLSL---IRGFVFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQNVL- 144

                         90       100
                 ....*....|....*....|....*....
gi 961964003  89 gtgFIIFMFrmswkltLVTMMGFPFIALV 117
Cdd:cd18599  145 ---LVVFSL-------IIIAIVFPWFLIA 163
UvrA COG0178
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
418-486 3.77e-04

Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];


Pssm-ID: 439948 [Multi-domain]  Cd Length: 941  Bit Score: 43.48  E-value: 3.77e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 961964003 418 LSGGQKQRVAIARALIR--QPRVL-ILDEATSALdaeseHI--VQQALNSIM----QEHTVLVIAHRLSTVEKADNII 486
Cdd:COG0178  827 LSGGEAQRVKLASELSKrsTGKTLyILDEPTTGL-----HFhdIRKLLEVLHrlvdKGNTVVVIEHNLDVIKTADWII 899
PLN03073 PLN03073
ABC transporter F family; Provisional
 417-449 5.48e-04

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 42.92  E-value: 5.48e-04
                         10        20        30
                 ....*....|....*....|....*....|...
gi 961964003 417 QLSGGQKQRVAIARALIRQPRVLILDEATSALD 449
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
ABC_6TM_LapB_like cd18587
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; ...
 92-228 6.66e-04

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: 42.04  E-value: 6.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  92 FIIFMFRMSWKLTLVTMMGFPFIALVSKLYGEYYKKLTKEVQTVLAEANKVAEETISGMRTVRSFANESReansyyakll 171
Cdd:cd18587  131 FLAVIALIGGPLALVPLVAIPLVLLYGLLLQKPLRRLVEESMRESAQKNALLVESLSGLETIKALGAEGR---------- 200

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 961964003 172 vmFQLNKKQALAYACY------MWSSCISELAL------EVAVLYYGGHLVLTDQLSSGGLISffIYML 228
Cdd:cd18587  201 --MQRRWEEAVAALARsslksrLLSSSATNFAQfvqqlvTVAIVIVGVYLISDGELTMGGLIA--CVIL 265
ABC_6TM_PrtD_like cd18586
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS ...
 10-221 9.19e-04

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: 41.43  E-value: 9.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  10 FFLLSSMAI--GVRGGVFTLTMARLNVRLRSRLFRTLMtqeiaffdenHTGDILSRLSADTTQVSDLISqnvnvfLRSVI 87
Cdd:cd18586   49 VVLLAFDGLlrQVRSRILQRVGLRLDVELGRRVFRAVL----------ELPLESRPSGYWQQLLRDLDT------LRNFL 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  88 KGTG------------FIIFMFRMSWKLTLVTMMGFPFIALVSKLYGEYYKKLTKEVQTVLAEANKVAEETISGMRTVRS 155
Cdd:cd18586  113 TGPSlfaffdlpwaplFLAVIFLIHPPLGWVALVGAPVLVGLAWLNHRATRKPLGEANEAQAARDALAAETLRNAETIKA 192

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 961964003 156 FANESREANSYYAKLLVMFQLNKKQALAYACYMWSSCISELALEVAVLYYGGHLVLTDQLSSGGLI 221
Cdd:cd18586  193 LGMLGNLRRRWEARHAETLELQIRASDLAGAISAIGKTLRMALQSLILGVGAYLVIDGELTIGALI 258
ABC_6TM_VMR1_D2_like cd18604
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ...
 7-161 1.19e-03

Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.


Pssm-ID: 350048 [Multi-domain]  Cd Length: 297  Bit Score: 40.91  E-value: 1.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   7 FTLFFLLSSMAIGVRGGvftLTMARlnvRLRSRLFRTLMTQEIAFFDENHTGDILSRLSADTTQVSDLISQNVNVFLRSV 86
Cdd:cd18604   55 LSVLLGTLRYLLFFFGS---LRASR---KLHERLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLEST 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  87 IKGTGFIIFMFRMSWKLTLVTMmgfpFIALVSKLYGEYYKKLTKEVQTVlaEANKVA------EETISGMRTVRSFANES 160
Cdd:cd18604  129 LSLLVILIAIVVVSPAFLLPAV----VLAALYVYIGRLYLRASRELKRL--ESVARSpilshfGETLAGLVTIRAFGAEE 202


                 .
gi 961964003 161 R 161
Cdd:cd18604  203 R 203
uvrA PRK00349
excinuclease ABC subunit UvrA;
418-486 1.45e-03

excinuclease ABC subunit UvrA;


Pssm-ID: 234734 [Multi-domain]  Cd Length: 943  Bit Score: 41.60  E-value: 1.45e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 961964003 418 LSGGQKQRVAIARALIRQP--RVL-ILDEATSALdaeseHI--VQQALNsIMQE-----HTVLVIAHRLSTVEKADNII 486
Cdd:PRK00349 831 LSGGEAQRVKLAKELSKRStgKTLyILDEPTTGL-----HFedIRKLLE-VLHRlvdkgNTVVVIEHNLDVIKTADWII 903
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
300-449 1.73e-03

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 41.26  E-value: 1.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 300 VSFTLRPGEVTALVGPSGSGKSSCVSLLENFYLPQGGQVLLDGKPVNEfqHD--------YLHSKIAL-----VGQEPVL 366
Cdd:NF033858 285 VSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDA--GDiatrrrvgYMSQAFSLygeltVRQNLEL 362

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 367 FARTikenisYGLSDVSM-EMVVQAATKANAHDFITTLPKGydtsvgekglqLSGGQKQRVAIARALIRQPRVLILDEAT 445
Cdd:NF033858 363 HARL------FHLPAAEIaARVAEMLERFDLADVADALPDS-----------LPLGIRQRLSLAVAVIHKPELLILDEPT 425


                 ....
gi 961964003 446 SALD 449
Cdd:NF033858 426 SGVD 429
ABC_6TM_VMR1_D1_like cd18596
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ...
 53-161 3.89e-03

Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.


Pssm-ID: 350040 [Multi-domain]  Cd Length: 309  Bit Score: 39.40  E-value: 3.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  53 DENHTGDILSRLSADTTQVSDLISqNVNVFLRSVIKGTGFIIFMFRMSWKLTLV----TMMGFPFIALVSKLYGEYYKKL 128
Cdd:cd18596  110 SSASVGKINNLMSVDANRISEFAA-FLHLLVSAPLQIVIAIVFLYRLLGWSALVglavMVLLLPLNGYLAKRYSRAQKEL 188

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 961964003 129 TK----EVQTVlaeankvaEETISGMRTVRSFANESR 161
Cdd:cd18596  189 MKardaRVQLV--------TEVLQGIRMIKFFAWERK 217
ABC_6TM_AarD_CydDC_like cd18561
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ...
 7-254 4.80e-03

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: 39.19  E-value: 4.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   7 FTLFFLLSSMAIGVRGGVFTL-------TMARLNVRLRSRLFRTLMTQEIAFFDENHTGDILSRLSADTTQVSDLISQNV 79
Cdd:cd18561   35 IMPPLAGIAGVIVLRAALLWLrervahrAAQRVKQHLRRRLFAKLLKLGPGYLEGERTGELQTTVVDGVEALEAYYGRYL 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003  80 NVFLRSVIKGTGFIIFMFRMSWKLTLVTMMGFPFIALVSKLYGEYYKKLTKEVQTVLAEANKVAEETISGMRTVRSFANE 159
Cdd:cd18561  115 PQLLVALLGPLLILIYLFFLDPLVALILLVFALLIPLSPALWDRLAKDTGRRHWAAYGRLSAQFLDSLQGMTTLKAFGAS 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003 160 SREANSYYAKLLVMFQLNKKQaLAYAcyMWSSCISELALE---VAVLYYGGHLVLTDQLSSGGLisFFIYMLeLGECFES 236
Cdd:cd18561  195 KRRGNELAARAEDLRQATMKV-LAVS--LLSSGIMGLATAlgtALALGVGALRVLGGQLTLSSL--LLILFL-SREFFRP 268

                        250       260
                 ....*....|....*....|.
gi 961964003 237 I---ASVYSGLMQGVGAAEKV 254
Cdd:cd18561  269 LrdlGAYWHAGYQGISAADSI 289
SbcC_Walker_B pfam13558
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ...
 417-452 5.46e-03

SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.


Pssm-ID: 463921 [Multi-domain]  Cd Length: 90  Bit Score: 36.44  E-value: 5.46e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 961964003  417 QLSGGQKQR---VAIARALIRQ----------PRVLILDEATSALDAES 452
Cdd:pfam13558  32 GLSGGEKQLlayLPLAAALAAQygsaegrppaPRLVFLDEAFAKLDEEN 80
ABC_6TM_MRP1_2_3_6_D2_like cd18603
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ...
 9-94 6.78e-03

Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).


Pssm-ID: 350047 [Multi-domain]  Cd Length: 296  Bit Score: 38.61  E-value: 6.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961964003   9 LFFLLSSMAIgvrggvfTLTMARLNVRLRSRLFRTLMTQEIAFFDENHTGDILSRLSADTTQVSDLISQNVNVFLRSVIK 88
Cdd:cd18603   56 IFVFLGSLAL-------ALGCVRASRNLHNKLLHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQ 128


                 ....*...
gi 961964003  89 --GTGFII 94
Cdd:cd18603  129 viSTLVVI 136
AAA_29 pfam13555
P-loop containing region of AAA domain;
299-322 7.25e-03

P-loop containing region of AAA domain;


Pssm-ID: 433304 [Multi-domain]  Cd Length: 61  Bit Score: 35.27  E-value: 7.25e-03
                          10        20
                  ....*....|....*....|....
gi 961964003  299 GVSFTLRPGEVTALVGPSGSGKSS 322
Cdd:pfam13555  14 GHTIPIDPRGNTLLTGPSGSGKST 37
 
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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