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Conserved domains on  [gi|515998033|ref|WP_017428616|]
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MULTISPECIES: ABC transporter ATP-binding protein [Paenibacillus]

Protein Classification

ABC transporter ATP-binding protein( domain architecture ID 11467437)

ABC transporter ATP-binding protein is the ATPase catalytic subunit of an ATP transporter complex responsible for coupling the energy of ATP hydrolysis to the import of one or more from a variety of substrates including Fe(3+) ions and polyamines such as spermidine and putrescine

CATH:  3.40.50.300
EC:  7.-.-.-
Gene Ontology:  GO:0042626|GO:0140359|GO:0005524|GO:0016887
PubMed:  25750732|24638992
SCOP:  4003976
TCDB:  3.A.1

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
 1-351 5.13e-170

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


:

Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 477.28  E-value: 5.13e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   1 MALLTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVNKRNFGFV 80
Cdd:COG3842    3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGMV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  81 FQSYALFPHLSVFDNVAFGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEP 160
Cdd:COG3842   83 FQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEP 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033 161 LSNLDANLRVNMRVEIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNIEQLDAPSTIFKYPTTEFVARFIGFNNFL 240
Cdd:COG3842  163 LSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGEANLL 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033 241 SFDERTEEGERIRlnTGDLSFSVVRNQGTVQPGARQGAIRPDDLVIRTEGnetGENELPGVIKVSTYLGRSYQYVVETAK 320
Cdd:COG3842  243 PGTVLGDEGGGVR--TGGRTLEVPADAGLAAGGPVTVAIRPEDIRLSPEG---PENGLPGTVEDVVFLGSHVRYRVRLGD 317

                        330       340       350
                 ....*....|....*....|....*....|....
gi 515998033 321 GN---FTANQEMDTPYLSGQRVTLHFPADKMVLV 351
Cdd:COG3842  318 GQelvVRVPNRAALPLEPGDRVGLSWDPEDVVVL 351
 
Name Accession Description Interval E-value
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
 1-351 5.13e-170

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 477.28  E-value: 5.13e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   1 MALLTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVNKRNFGFV 80
Cdd:COG3842    3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGMV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  81 FQSYALFPHLSVFDNVAFGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEP 160
Cdd:COG3842   83 FQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEP 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033 161 LSNLDANLRVNMRVEIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNIEQLDAPSTIFKYPTTEFVARFIGFNNFL 240
Cdd:COG3842  163 LSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGEANLL 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033 241 SFDERTEEGERIRlnTGDLSFSVVRNQGTVQPGARQGAIRPDDLVIRTEGnetGENELPGVIKVSTYLGRSYQYVVETAK 320
Cdd:COG3842  243 PGTVLGDEGGGVR--TGGRTLEVPADAGLAAGGPVTVAIRPEDIRLSPEG---PENGLPGTVEDVVFLGSHVRYRVRLGD 317

                        330       340       350
                 ....*....|....*....|....*....|....
gi 515998033 321 GN---FTANQEMDTPYLSGQRVTLHFPADKMVLV 351
Cdd:COG3842  318 GQelvVRVPNRAALPLEPGDRVGLSWDPEDVVVL 351
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
 4-235 2.46e-121

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: 349.23  E-value: 2.46e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   4 LTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVNKRNFGFVFQS 83
Cdd:cd03300    1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  84 YALFPHLSVFDNVAFGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLSN 163
Cdd:cd03300   81 YALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515998033 164 LDANLRVNMRVEIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNIEQLDAPSTIFKYPTTEFVARFIG 235
Cdd:cd03300  161 LDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
PhnT2 TIGR03265
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ...
 1-348 1.16e-113

putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 274496 [Multi-domain]  Cd Length: 353  Bit Score: 334.31  E-value: 1.16e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033    1 MALLTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVNKRNFGFV 80
Cdd:TIGR03265   2 SPYLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYGIV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   81 FQSYALFPHLSVFDNVAFGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEP 160
Cdd:TIGR03265  82 FQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  161 LSNLDANLRVNMRVEIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNIEQLDAPSTIFKYPTTEFVARFIGFNNFL 240
Cdd:TIGR03265 162 LSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVGEVNWL 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  241 SFdeRTEEGERIRLntGDLSFSVvrNQGTVQPGAR-QGAIRPDDLVIRTEGNEtgENELPGVIKVSTYLGRSYQ--YVVE 317
Cdd:TIGR03265 242 PG--TRGGGSRARV--GGLTLAC--APGLAQPGASvRLAVRPEDIRVSPAGNA--ANLLLARVEDMEFLGAFYRlrLRLE 313

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 515998033  318 TAKG-----NFTANQEMDTPYLSGQRVTLHFPADKM 348
Cdd:TIGR03265 314 GLPGqalvaDVSASEVERLGIRAGQPIWIELPAERL 349
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
3-322 5.32e-113

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 333.45  E-value: 5.32e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   3 LLTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVNKRNFGFVFQ 82
Cdd:PRK09452  14 LVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTVFQ 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  83 SYALFPHLSVFDNVAFGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLS 162
Cdd:PRK09452  94 SYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLS 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033 163 NLDANLRVNMRVEIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNIEQLDAPSTIFKYPTTEFVARFIGFNNFL-- 240
Cdd:PRK09452 174 ALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIGEINIFda 253

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033 241 SFDERTEEgERIRLNTGDLSFsVVRNQGTVQPGAR-QGAIRPDDLVIRTEGNETGENELPGVIKVSTYLGRSYQYVVETA 319
Cdd:PRK09452 254 TVIERLDE-QRVRANVEGREC-NIYVNFAVEPGQKlHVLLRPEDLRVEEINDDEHAEGLIGYVRERNYKGMTLDSVVELE 331


                 ...
gi 515998033 320 KGN 322
Cdd:PRK09452 332 NGK 334
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 19-162 5.12e-46

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


Pssm-ID: 394964 [Multi-domain]  Cd Length: 150  Bit Score: 153.96  E-value: 5.12e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   19 LQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVN--KRNFGFVFQSYALFPHLSVFDNV 96
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKslRKEIGYVFQDPQLFPRLTVRENL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   97 AFGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKR----FPGELSGGQRQRVAIARALVIEPDLLLFDEPLS 162
Cdd:pfam00005  81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRpvgeRPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
12-196 1.31e-32

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 120.03  E-value: 1.31e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  12 AYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFlfgdkdyTRVPvnKRNFGFVFQSYAL---FP 88
Cdd:NF040873   1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV-------RRAG--GARVAYVPQRSEVpdsLP 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  89 hLSVFDNVAFGL-----RLRKVKEDDvKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLSN 163
Cdd:NF040873  72 -LTVRDLVAMGRwarrgLWRRLTRDD-RAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTG 149

                        170       180       190
                 ....*....|....*....|....*....|...
gi 515998033 164 LDANLRVNMRVEIRRIQQElGITTVYVSHDQEE 196
Cdd:NF040873 150 LDAESRERIIALLAEEHAR-GATVVVVTHDLEL 181
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
23-165 9.40e-20

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 90.57  E-value: 9.40e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  23 DLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGT-FLFGDkdytrvPVN------KRNFGFVFQSYALFPHLSVFDN 95
Cdd:NF033858 286 SFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEaWLFGQ------PVDagdiatRRRVGYMSQAFSLYGELTVRQN 359

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  96 VAFGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLSNLD 165
Cdd:NF033858 360 LELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
6-160 6.96e-15

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 75.93  E-value: 6.96e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   6 LDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTF--LFGD--KDYTRVPVNKR------ 75
Cdd:NF033858   4 LEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVevLGGDmaDARHRRAVCPRiaympq 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  76 ----NfgfvfqsyaLFPHLSVFDNVAFGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIE 151
Cdd:NF033858  84 glgkN---------LYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHD 154


                 ....*....
gi 515998033 152 PDLLLFDEP 160
Cdd:NF033858 155 PDLLILDEP 163
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 28-196 2.21e-09

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: 55.46  E-value: 2.21e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033    28 RGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDytrvpvnkrnfgfvfqsyalfphlsvfdnvafglrlrkvke 107
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGE----------------------------------------- 39

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   108 ddvkrRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLSNLDANLRVNMRVEIR-----RIQQE 182
Cdd:smart00382  40 -----DILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrlllLLKSE 114

                          170
                   ....*....|....
gi 515998033   183 LGITTVYVSHDQEE 196
Cdd:smart00382 115 KNLTVILTTNDEKD 128
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
101-212 1.97e-07

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 52.04  E-value: 1.97e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033 101 RLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLSNLDANLRVNMRVEIRRIQ 180
Cdd:NF000106 112 R*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMV 191

                         90       100       110
                 ....*....|....*....|....*....|..
gi 515998033 181 QElGITTVYVSHDQEECFSISDQVAIMNKGNI 212
Cdd:NF000106 192 RD-GATVLLTTQYMEEAEQLAHELTVIDRGRV 222
GguA NF040905
sugar ABC transporter ATP-binding protein;
19-217 1.22e-06

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 50.17  E-value: 1.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  19 LQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAkqGTFLfGDKDYTRVPVNKRN------FGFVF--QSYALFPHL 90
Cdd:NF040905  17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPH--GSYE-GEILFDGEVCRFKDirdseaLGIVIihQELALIPYL 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  91 SVFDNVAFGLRLRK---VKEDDVKRRVMTMLDTVSLggfeKRFPGELSG----GQRQRVAIARALVIEPDLLLFDEPLSN 163
Cdd:NF040905  94 SIAENIFLGNERAKrgvIDWNETNRRARELLAKVGL----DESPDTLVTdigvGKQQLVEIAKALSKDVKLLILDEPTAA 169

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 515998033 164 LD----ANLrVNMRVEIRriqqELGITTVYVSHDQEECFSISDQVAIMNKGN-IEQLDA 217
Cdd:NF040905 170 LNeedsAAL-LDLLLELK----AQGITSIIISHKLNEIRRVADSITVLRDGRtIETLDC 223
GguA NF040905
sugar ABC transporter ATP-binding protein;
132-212 8.53e-05

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 44.40  E-value: 8.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033 132 GELSGGQRQRVAIARALVIEPDLLLFDEPLSNLDanlrVNMRVEIRRIQQEL---GITTVYVSHDQEECFSISDQVAIMN 208
Cdd:NF040905 403 GNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGID----VGAKYEIYTIINELaaeGKGVIVISSELPELLGMCDRIYVMN 478


                 ....
gi 515998033 209 KGNI 212
Cdd:NF040905 479 EGRI 482
 
Name Accession Description Interval E-value
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
 1-351 5.13e-170

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 477.28  E-value: 5.13e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   1 MALLTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVNKRNFGFV 80
Cdd:COG3842    3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGMV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  81 FQSYALFPHLSVFDNVAFGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEP 160
Cdd:COG3842   83 FQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEP 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033 161 LSNLDANLRVNMRVEIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNIEQLDAPSTIFKYPTTEFVARFIGFNNFL 240
Cdd:COG3842  163 LSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGEANLL 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033 241 SFDERTEEGERIRlnTGDLSFSVVRNQGTVQPGARQGAIRPDDLVIRTEGnetGENELPGVIKVSTYLGRSYQYVVETAK 320
Cdd:COG3842  243 PGTVLGDEGGGVR--TGGRTLEVPADAGLAAGGPVTVAIRPEDIRLSPEG---PENGLPGTVEDVVFLGSHVRYRVRLGD 317

                        330       340       350
                 ....*....|....*....|....*....|....
gi 515998033 321 GN---FTANQEMDTPYLSGQRVTLHFPADKMVLV 351
Cdd:COG3842  318 GQelvVRVPNRAALPLEPGDRVGLSWDPEDVVVL 351
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
 1-350 3.19e-147

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


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 419.48  E-value: 3.19e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   1 MALLTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVNKRNFGFV 80
Cdd:COG3839    1 MASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIAMV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  81 FQSYALFPHLSVFDNVAFGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEP 160
Cdd:COG3839   81 FQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033 161 LSNLDANLRVNMRVEIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNIEQLDAPSTIFKYPTTEFVARFIGFN--N 238
Cdd:COG3839  161 LSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGFIGSPpmN 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033 239 FLSFderTEEGERIRLntGDLSFSVVRNQGTVQPGARQGAIRPDDLVIRTEgnetGENELPGVIKVSTYLGRSYQYVVET 318
Cdd:COG3839  241 LLPG---TVEGGGVRL--GGVRLPLPAALAAAAGGEVTLGIRPEHLRLADE----GDGGLEATVEVVEPLGSETLVHVRL 311

                        330       340       350
                 ....*....|....*....|....*....|..
gi 515998033 319 AKGNFTANQEMDTPYLSGQRVTLHFPADKMVL 350
Cdd:COG3839  312 GGQELVARVPGDTRLRPGDTVRLAFDPERLHL 343
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
 4-347 1.10e-121

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


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 354.45  E-value: 1.10e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   4 LTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKD-YTRVPVNKRNFGFVFQ 82
Cdd:COG1118    3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDlFTNLPPRERRVGFVFQ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  83 SYALFPHLSVFDNVAFGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLS 162
Cdd:COG1118   83 HYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFG 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033 163 NLDANLRVNMRVEIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNIEQLDAPSTIFKYPTTEFVARFIGFNNFlsF 242
Cdd:COG1118  163 ALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLGCVNV--L 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033 243 DERTEEGeriRLNTGDLSFSVVRNqgtVQPGARQGAIRPDDLVIRTEGNetGENELPGVIKVSTYLGRSYQYVVETAKGN 322
Cdd:COG1118  241 RGRVIGG---QLEADGLTLPVAEP---LPDGPAVAGVRPHDIEVSREPE--GENTFPATVARVSELGPEVRVELKLEDGE 312

                        330       340       350
                 ....*....|....*....|....*....|..
gi 515998033 323 -------FTANQEMDTPYLSGQRVTLHFPADK 347
Cdd:COG1118  313 gqpleaeVTKEAWAELGLAPGDPVYLRPRPAR 344
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
 4-235 2.46e-121

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: 349.23  E-value: 2.46e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   4 LTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVNKRNFGFVFQS 83
Cdd:cd03300    1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  84 YALFPHLSVFDNVAFGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLSN 163
Cdd:cd03300   81 YALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515998033 164 LDANLRVNMRVEIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNIEQLDAPSTIFKYPTTEFVARFIG 235
Cdd:cd03300  161 LDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
PhnT2 TIGR03265
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ...
 1-348 1.16e-113

putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 274496 [Multi-domain]  Cd Length: 353  Bit Score: 334.31  E-value: 1.16e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033    1 MALLTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVNKRNFGFV 80
Cdd:TIGR03265   2 SPYLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYGIV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   81 FQSYALFPHLSVFDNVAFGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEP 160
Cdd:TIGR03265  82 FQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  161 LSNLDANLRVNMRVEIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNIEQLDAPSTIFKYPTTEFVARFIGFNNFL 240
Cdd:TIGR03265 162 LSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVGEVNWL 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  241 SFdeRTEEGERIRLntGDLSFSVvrNQGTVQPGAR-QGAIRPDDLVIRTEGNEtgENELPGVIKVSTYLGRSYQ--YVVE 317
Cdd:TIGR03265 242 PG--TRGGGSRARV--GGLTLAC--APGLAQPGASvRLAVRPEDIRVSPAGNA--ANLLLARVEDMEFLGAFYRlrLRLE 313

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 515998033  318 TAKG-----NFTANQEMDTPYLSGQRVTLHFPADKM 348
Cdd:TIGR03265 314 GLPGqalvaDVSASEVERLGIRAGQPIWIELPAERL 349
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
 4-214 1.46e-113

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: 328.71  E-value: 1.46e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   4 LTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVNKRNFGFVFQS 83
Cdd:cd03259    1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVFQD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  84 YALFPHLSVFDNVAFGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLSN 163
Cdd:cd03259   81 YALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 515998033 164 LDANLRVNMRVEIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNIEQ 214
Cdd:cd03259  161 LDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQ 211
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
3-322 5.32e-113

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 333.45  E-value: 5.32e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   3 LLTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVNKRNFGFVFQ 82
Cdd:PRK09452  14 LVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTVFQ 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  83 SYALFPHLSVFDNVAFGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLS 162
Cdd:PRK09452  94 SYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLS 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033 163 NLDANLRVNMRVEIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNIEQLDAPSTIFKYPTTEFVARFIGFNNFL-- 240
Cdd:PRK09452 174 ALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIGEINIFda 253

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033 241 SFDERTEEgERIRLNTGDLSFsVVRNQGTVQPGAR-QGAIRPDDLVIRTEGNETGENELPGVIKVSTYLGRSYQYVVETA 319
Cdd:PRK09452 254 TVIERLDE-QRVRANVEGREC-NIYVNFAVEPGQKlHVLLRPEDLRVEEINDDEHAEGLIGYVRERNYKGMTLDSVVELE 331


                 ...
gi 515998033 320 KGN 322
Cdd:PRK09452 332 NGK 334
potA TIGR01187
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ...
 34-351 1.50e-105

spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, 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 transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 162242 [Multi-domain]  Cd Length: 325  Bit Score: 312.51  E-value: 1.50e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   34 LLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVNKRNFGFVFQSYALFPHLSVFDNVAFGLRLRKVKEDDVKRR 113
Cdd:TIGR01187   1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  114 VMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLSNLDANLRVNMRVEIRRIQQELGITTVYVSHD 193
Cdd:TIGR01187  81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  194 QEECFSISDQVAIMNKGNIEQLDAPSTIFKYPTTEFVARFIGFNNFLSFDERTEEGERIRLNTGDLSFSVVRNQGTVQPG 273
Cdd:TIGR01187 161 QEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVFEATVIERKSEQVVLAGVEGRRCDIYTDVPVEKD 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  274 AR-QGAIRPDDLVIRTEGNETGENELPGVIKVSTYLGRSYQYVVETAKG------NFTANQEMDTPYLSGQRVTLHFPAD 346
Cdd:TIGR01187 241 QPlHVVLRPEKIVIEEEDEANSSNAIIGHVIDITYLGMTLEVHVRLETGqkvlvsEFFNEDDPHMSPSIGDRVGLTWHPG 320


                  ....*
gi 515998033  347 KMVLV 351
Cdd:TIGR01187 321 SEVVL 325
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
4-316 4.76e-101

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 302.02  E-value: 4.76e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   4 LTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVNKRNFGFVFQS 83
Cdd:PRK11432   7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMVFQS 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  84 YALFPHLSVFDNVAFGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLSN 163
Cdd:PRK11432  87 YALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSN 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033 164 LDANLRVNMRVEIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNIEQLDAPSTIFKYPTTEFVARFIG----FNNF 239
Cdd:PRK11432 167 LDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMGdaniFPAT 246

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515998033 240 LSFDERTEEGERIRLntgDLSFSVVRNQGTVQPGarqgaIRPDDLVIRTEGNETGENElpgvIKVSTYLGRSYQYVV 316
Cdd:PRK11432 247 LSGDYVDIYGYRLPR---PAAFAFNLPDGECTVG-----VRPEAITLSEQGEESQRCT----IKHVAYMGPQYEVTV 311
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
1-347 5.51e-98

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 294.63  E-value: 5.51e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   1 MALLTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVNKRNFGFV 80
Cdd:PRK11000   1 MASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGMV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  81 FQSYALFPHLSVFDNVAFGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEP 160
Cdd:PRK11000  81 FQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033 161 LSNLDANLRVNMRVEIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNIEQLDAPSTIFKYPTTEFVARFIGFN--N 238
Cdd:PRK11000 161 LSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGSPkmN 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033 239 FLS--FDERTEEGERIRLNTGdLSFSVVRNQGTVQPGARQG-AIRPDDLVirteGNETGENELPGVIKVSTYLGRSYQ-Y 314
Cdd:PRK11000 241 FLPvkVTATAIEQVQVELPNR-QQVWLPVEGRGVQVGANMSlGIRPEHLL----PSDIADVTLEGEVQVVEQLGNETQiH 315

                        330       340       350
                 ....*....|....*....|....*....|....
gi 515998033 315 V-VETAKGNFTANQEMDTPYLSGQRVTLHFPADK 347
Cdd:PRK11000 316 IqIPAIRQNLVYRQNDVVLVEEGATFAIGLPPER 349
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
 9-235 9.09e-98

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: 289.62  E-value: 9.09e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   9 VSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVNKRNFGFVFQSYALFP 88
Cdd:cd03296    8 VSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFVFQHYALFR 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  89 HLSVFDNVAFGLRLRKVK----EDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLSNL 164
Cdd:cd03296   88 HMTVFDNVAFGLRVKPRSerppEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGAL 167

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515998033 165 DANLRVNMRVEIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNIEQLDAPSTIFKYPTTEFVARFIG 235
Cdd:cd03296  168 DAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFLG 238
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
 4-216 5.79e-96

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: 283.76  E-value: 5.79e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   4 LTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVNKRNFGFVFQS 83
Cdd:cd03301    1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVFQN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  84 YALFPHLSVFDNVAFGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLSN 163
Cdd:cd03301   81 YALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 515998033 164 LDANLRVNMRVEIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNIEQLD 216
Cdd:cd03301  161 LDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
1-348 1.80e-92

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


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 280.19  E-value: 1.80e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   1 MALLTLDRVSVAYDN-QLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVNKRNFGF 79
Cdd:PRK11650   1 MAGLKLQAVRKSYDGkTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDIAM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  80 VFQSYALFPHLSVFDNVAFGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDE 159
Cdd:PRK11650  81 VFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033 160 PLSNLDANLRVNMRVEIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNIEQLDAPSTIFKYPTTEFVARFIGFN-- 237
Cdd:PRK11650 161 PLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASFIGSPam 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033 238 NFLSFDERtEEGERIRLNTGdLSFSVVRNQGTVQPGARQGAIRPDDLVIrtegnETGENELPGVIKVSTYLGrSYQYV-V 316
Cdd:PRK11650 241 NLLDGRVS-ADGAAFELAGG-IALPLGGGYRQYAGRKLTLGIRPEHIAL-----SSAEGGVPLTVDTVELLG-ADNLAhG 312

                        330       340       350
                 ....*....|....*....|....*....|..
gi 515998033 317 ETAKGNFTANQEMDTPYLSGQRVTLHFPADKM 348
Cdd:PRK11650 313 RWGGQPLVVRLPHQERPAAGSTLWLHLPANQL 344
3a0106s01 TIGR00968
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
 9-240 1.96e-88

sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]


Pssm-ID: 130041 [Multi-domain]  Cd Length: 237  Bit Score: 265.90  E-value: 1.96e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033    9 VSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVNKRNFGFVFQSYALFP 88
Cdd:TIGR00968   6 ISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARDRKIGFVFQHYALFK 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   89 HLSVFDNVAFGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLSNLDANL 168
Cdd:TIGR00968  86 HLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGALDAKV 165

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515998033  169 RVNMRVEIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNIEQLDAPSTIFKYPTTEFVARFIGFNNFL 240
Cdd:TIGR00968 166 RKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLGEVNVL 237
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
 1-210 2.90e-87

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


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 263.49  E-value: 2.90e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   1 MALLTLDRVSVAY----DNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPvnkRN 76
Cdd:COG1116    5 APALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPG---PD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  77 FGFVFQSYALFPHLSVFDNVAFGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLL 156
Cdd:COG1116   82 RGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLL 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 515998033 157 FDEPLSNLDANLRVNMRVEIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKG 210
Cdd:COG1116  162 MDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSAR 215
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
4-241 3.46e-86

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 264.25  E-value: 3.46e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   4 LTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVNKRNFGFVFQS 83
Cdd:PRK10851   3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVFQH 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  84 YALFPHLSVFDNVAFGL----RLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDE 159
Cdd:PRK10851  83 YALFRHMTVFDNIAFGLtvlpRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDE 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033 160 PLSNLDANLRVNMRVEIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNIEQLDAPSTIFKYPTTEFVARFIGFNNF 239
Cdd:PRK10851 163 PFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMGEVNR 242


                 ..
gi 515998033 240 LS 241
Cdd:PRK10851 243 LQ 244
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
 4-209 3.10e-84

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: 254.32  E-value: 3.10e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   4 LTLDRVSVAYDN----QLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPvnkRNFGF 79
Cdd:cd03293    1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG---PDRGY 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  80 VFQSYALFPHLSVFDNVAFGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDE 159
Cdd:cd03293   78 VFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDE 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 515998033 160 PLSNLDANLRVNMRVEIRRIQQELGITTVYVSHDQEECFSISDQVAIMNK 209
Cdd:cd03293  158 PFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSA 207
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
 19-238 4.19e-84

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: 254.57  E-value: 4.19e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  19 LQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVNKRNFGFVFQSYALFPHLSVFDNVAF 98
Cdd:cd03299   15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVPQNYALFPHMTVYKNIAY 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  99 GLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLSNLDANLRVNMRVEIRR 178
Cdd:cd03299   95 GLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKK 174

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033 179 IQQELGITTVYVSHDQEECFSISDQVAIMNKGNIEQLDAPSTIFKYPTTEFVARFIGFNN 238
Cdd:cd03299  175 IRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLGFNN 234
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
3-327 2.72e-77

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 242.05  E-value: 2.72e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   3 LLTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVNKRNFGFVFQ 82
Cdd:PRK11607  19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMFQ 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  83 SYALFPHLSVFDNVAFGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLS 162
Cdd:PRK11607  99 SYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMG 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033 163 NLDANLRVNMRVEIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNIEQLDAPSTIFKYPTTEFVARFIGFNNFLS- 241
Cdd:PRK11607 179 ALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNVFEg 258

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033 242 -FDERTEEGERIRLNTGDLSFSVVRNQGTVQPGARQGAIRPDDLVIRTEGNETGENELPGVIKVSTYLGRSYQYVVETAK 320
Cdd:PRK11607 259 vLKERQEDGLVIDSPGLVHPLKVDADASVVDNVPVHVALRPEKIMLCEEPPADGCNFAVGEVIHIAYLGDLSIYHVRLKS 338


                 ....*..
gi 515998033 321 GNFTANQ 327
Cdd:PRK11607 339 GQMISAQ 345
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
 2-234 3.09e-75

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: 232.18  E-value: 3.09e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   2 ALLTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVNK-----RN 76
Cdd:COG1127    4 PMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKElyelrRR 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  77 FGFVFQSYALFPHLSVFDNVAFGLR-LRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLL 155
Cdd:COG1127   84 IGMLFQGGALFDSLTVFENVAFPLReHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEIL 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033 156 LFDEPLSNLDAnlrVNMRV---EIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNIEQLDAPSTIFKYpTTEFVAR 232
Cdd:COG1127  164 LYDEPTAGLDP---ITSAVideLIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLAS-DDPWVRQ 239


                 ..
gi 515998033 233 FI 234
Cdd:COG1127  240 FL 241
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
4-235 4.27e-75

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 231.57  E-value: 4.27e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   4 LTLDRVSVAYDNQLIlqDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVNKRNFGFVFQS 83
Cdd:COG3840    2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSMLFQE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  84 YALFPHLSVFDNVAFGLR--LRKVKEDdvKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPL 161
Cdd:COG3840   80 NNLFPHLTVAQNIGLGLRpgLKLTAEQ--RAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPF 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515998033 162 SNLDANLRVNMRVEIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNIEQLDAPSTIFKYPTTEFVARFIG 235
Cdd:COG3840  158 SALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYLG 231
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
 4-235 8.15e-75

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: 231.04  E-value: 8.15e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   4 LTLDRVSVAY-DNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVNK--RNFGFV 80
Cdd:cd03295    1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElrRKIGYV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  81 FQSYALFPHLSVFDNVAFGLRLRKVKEDDVKRRVMTMLDTVSL--GGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFD 158
Cdd:cd03295   81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515998033 159 EPLSNLDANLRVNMRVEIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNIEQLDAPSTIFKYPTTEFVARFIG 235
Cdd:cd03295  161 EPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVG 237
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
 19-234 3.82e-69

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: 217.51  E-value: 3.82e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  19 LQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVP------VNKRNFGFVFQSYALFPHLSV 92
Cdd:cd03294   40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSrkelreLRRKKISMVFQSFALLPHRTV 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  93 FDNVAFGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLSNLDANLRVNM 172
Cdd:cd03294  120 LENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREM 199

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515998033 173 RVEIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNIEQLDAPSTIFKYPTTEFVARFI 234
Cdd:cd03294  200 QDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFF 261
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
 4-210 1.30e-67

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: 210.51  E-value: 1.30e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   4 LTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTR----VPVNKRNFGF 79
Cdd:cd03229    1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDledeLPPLRRRIGM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  80 VFQSYALFPHLSVFDNVAFGLrlrkvkeddvkrrvmtmldtvslggfekrfpgelSGGQRQRVAIARALVIEPDLLLFDE 159
Cdd:cd03229   81 VFQDFALFPHLTVLENIALGL----------------------------------SGGQQQRVALARALAMDPDVLLLDE 126

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 515998033 160 PLSNLDANLRVNMRVEIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKG 210
Cdd:cd03229  127 PTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
 6-223 3.53e-66

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: 208.51  E-value: 3.53e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   6 LDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVNK-----RNFGFV 80
Cdd:cd03261    3 LRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrlrRRMGML 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  81 FQSYALFPHLSVFDNVAFGLR-LRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDE 159
Cdd:cd03261   83 FQSGALFDSLTVFENVAFPLReHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDE 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515998033 160 PLSNLDAnlrVNMRV---EIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNIEQLDAPSTIFK 223
Cdd:cd03261  163 PTAGLDP---IASGViddLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
2-213 5.88e-65

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 205.28  E-value: 5.88e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   2 ALLTLDRVSVAY---DNQL-ILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVNKR-- 75
Cdd:COG1136    3 PLLELRNLTKSYgtgEGEVtALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELar 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  76 ----NFGFVFQSYALFPHLSVFDNVAFGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIE 151
Cdd:COG1136   83 lrrrHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNR 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515998033 152 PDLLLFDEPLSNLDANLRVNMRVEIRRIQQELGITTVYVSHDqEECFSISDQVAIMNKGNIE 213
Cdd:COG1136  163 PKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHD-PELAARADRVIRLRDGRIV 223
ProV COG4175
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ...
 19-234 1.93e-64

ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 443334 [Multi-domain]  Cd Length: 389  Bit Score: 209.19  E-value: 1.93e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  19 LQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVP------VNKRNFGFVFQSYALFPHLSV 92
Cdd:COG4175   43 VNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITKLSkkelreLRRKKMSMVFQHFALLPHRTV 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  93 FDNVAFGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLSNLDANLRVNM 172
Cdd:COG4175  123 LENVAFGLEIQGVPKAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPLIRREM 202

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515998033 173 RVEIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNIEQLDAPSTIFKYPTTEFVARFI 234
Cdd:COG4175  203 QDELLELQAKLKKTIVFITHDLDEALRLGDRIAIMKDGRIVQIGTPEEILTNPANDYVADFV 264
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
 4-212 7.12e-64

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: 202.33  E-value: 7.12e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   4 LTLDRVSVAYDNQ----LILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVNKR---- 75
Cdd:cd03255    1 IELKNLSKTYGGGgekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  76 --NFGFVFQSYALFPHLSVFDNVAFGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPD 153
Cdd:cd03255   81 rrHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 515998033 154 LLLFDEPLSNLDANLRVNMRVEIRRIQQELGITTVYVSHDQEEcFSISDQVAIMNKGNI 212
Cdd:cd03255  161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPEL-AEYADRIIELRDGKI 218
TauB COG4525
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
1-196 1.09e-63

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


Pssm-ID: 443596 [Multi-domain]  Cd Length: 262  Bit Score: 203.17  E-value: 1.09e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   1 MALLTLDRVSVAYDN----QLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRvPVNKRn 76
Cdd:COG4525    1 MSMLTVRHVSVRYPGggqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG-PGADR- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  77 fGFVFQSYALFPHLSVFDNVAFGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLL 156
Cdd:COG4525   79 -GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLL 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 515998033 157 FDEPLSNLDANLRVNMRVEIRRIQQELGITTVYVSHDQEE 196
Cdd:COG4525  158 MDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEE 197
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
 19-214 2.10e-63

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: 200.98  E-value: 2.10e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  19 LQDFDLQLE---RGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDY--TR----VPVNKRNFGFVFQSYALFPH 89
Cdd:cd03297   10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdSRkkinLPPQQRKIGLVFQQYALFPH 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  90 LSVFDNVAFGLRLRKVKEDdvKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLSNLDANLR 169
Cdd:cd03297   90 LNVRENLAFGLKRKRNRED--RISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALR 167

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 515998033 170 VNMRVEIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNIEQ 214
Cdd:cd03297  168 LQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQY 212
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
 3-235 6.51e-63

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


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 200.22  E-value: 6.51e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   3 LLTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVN----KRNFG 78
Cdd:COG1126    1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDinklRRKVG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  79 FVFQSYALFPHLSVFDNVAFGLR-LRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLF 157
Cdd:COG1126   81 MVFQQFNLFPHLTVLENVTLAPIkVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033 158 DEPLSNLDAN-----LRVnmrveIRRIQQElGITTVYVSHDQEECFSISDQVAIMNKGNIEQLDAPSTIFKYPTTEFVAR 232
Cdd:COG1126  161 DEPTSALDPElvgevLDV-----MRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTRA 234


                 ...
gi 515998033 233 FIG 235
Cdd:COG1126  235 FLS 237
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
 4-223 3.22e-62

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: 198.33  E-value: 3.22e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   4 LTLDRVSVAY-DNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVNK--RNFGFV 80
Cdd:COG1122    1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElrRKVGLV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  81 FQS--YALFpHLSVFDNVAFGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFD 158
Cdd:COG1122   81 FQNpdDQLF-APTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLD 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515998033 159 EPLSNLDANLRVNMRVEIRRIQQElGITTVYVSHDQEECFSISDQVAIMNKGNIEQLDAPSTIFK 223
Cdd:COG1122  160 EPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFS 223
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
4-221 3.39e-62

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 198.36  E-value: 3.39e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   4 LTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVN-KRNFGFVFQ 82
Cdd:COG1131    1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEvRRRIGYVPQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  83 SYALFPHLSVFDNVAFGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLS 162
Cdd:COG1131   81 EPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 515998033 163 NLDANLRVNMRVEIRRIQQElGITTVYVSHDQEECFSISDQVAIMNKGNIEQLDAPSTI 221
Cdd:COG1131  161 GLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
 3-225 4.47e-62

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: 206.29  E-value: 4.47e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   3 LLTLDRVSVAY-----DNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVNK--- 74
Cdd:COG1123  260 LLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlre 339

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  75 --RNFGFVFQ--SYALFPHLSVFDNVAFGLRLRKV-KEDDVKRRVMTMLDTVSLG-GFEKRFPGELSGGQRQRVAIARAL 148
Cdd:COG1123  340 lrRRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLPpDLADRYPHELSGGQRQRVAIARAL 419

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515998033 149 VIEPDLLLFDEPLSNLDANLRVNMRVEIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNIEQLDAPSTIFKYP 225
Cdd:COG1123  420 ALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANP 496
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
 4-195 6.65e-62

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


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 196.93  E-value: 6.65e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   4 LTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAK---QGTFLFGDKDYTRVPVNKRNFGFV 80
Cdd:COG4136    2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAEQRRIGIL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  81 FQSYALFPHLSVFDNVAFGLRlRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEP 160
Cdd:COG4136   82 FQDDLLFPHLSVGENLAFALP-PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEP 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 515998033 161 LSNLDANLRVNMRVEIRRIQQELGITTVYVSHDQE 195
Cdd:COG4136  161 FSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEE 195
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
4-195 2.70e-61

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 195.66  E-value: 2.70e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   4 LTLDRVSVAYDN-QLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVNK-----RNF 77
Cdd:COG2884    2 IRFENVSKRYPGgREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipylrRRI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  78 GFVFQSYALFPHLSVFDNVAFGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLF 157
Cdd:COG2884   82 GVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLA 161

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 515998033 158 DEPLSNLDANLRVN-MRVeIRRIQQeLGITTVYVSHDQE 195
Cdd:COG2884  162 DEPTGNLDPETSWEiMEL-LEEINR-RGTTVLIATHDLE 198
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
 6-210 4.79e-61

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: 194.61  E-value: 4.79e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   6 LDRVSVAYDNQ--LILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVNK--RNFGFVF 81
Cdd:cd03225    2 LKNLSFSYPDGarPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKElrRKVGLVF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  82 QsyalFP-----HLSVFDNVAFGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLL 156
Cdd:cd03225   82 Q----NPddqffGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILL 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 515998033 157 FDEPLSNLDANLRVNMRVEIRRIQQElGITTVYVSHDQEECFSISDQVAIMNKG 210
Cdd:cd03225  158 LDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDG 210
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
 3-235 1.19e-60

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: 195.02  E-value: 1.19e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   3 LLTLDRVSVAY----DNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVP--VNKRN 76
Cdd:COG1124    1 MLEVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRrkAFRRR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  77 FGFVFQSY--ALFPHLSVFDNVAFGLRLRKVkeDDVKRRVMTMLDTVSLG-GFEKRFPGELSGGQRQRVAIARALVIEPD 153
Cdd:COG1124   81 VQMVFQDPyaSLHPRHTVDRILAEPLRIHGL--PDREERIAELLEQVGLPpSFLDRYPHQLSGGQRQRVAIARALILEPE 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033 154 LLLFDEPLSNLDanlrVNMRVEI----RRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNIEQLDAPSTIFKYPTTEF 229
Cdd:COG1124  159 LLLLDEPTSALD----VSVQAEIlnllKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHPY 234


                 ....*.
gi 515998033 230 VARFIG 235
Cdd:COG1124  235 TRELLA 240
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
 3-212 3.64e-59

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: 190.41  E-value: 3.64e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   3 LLTLDRVSVAYDNQL----ILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVP-----VN 73
Cdd:cd03257    1 LLEVKNLSVSFPTGGgsvkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlrkIR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  74 KRNFGFVFQSY--ALFPHLSVFDNVAFGLRLRKVKEDDVKRRVMTMLDTVSLG---GFEKRFPGELSGGQRQRVAIARAL 148
Cdd:cd03257   81 RKEIQMVFQDPmsSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGlpeEVLNRYPHELSGGQRQRVAIARAL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515998033 149 VIEPDLLLFDEPLSNLDANLRVNMRVEIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNI 212
Cdd:cd03257  161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
 21-222 7.92e-58

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: 191.08  E-value: 7.92e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  21 DFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDY------TRVPVNKRNFGFVFQSYALFPHLSVFD 94
Cdd:COG4148   17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLqdsargIFLPPHRRRIGYVFQEARLFPHLSVRG 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  95 NVAFGLRLRKVKEDDVKR-RVMTMLDtvsLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLSNLDANLrvnmR 173
Cdd:COG4148   97 NLLYGRKRAPRAERRISFdEVVELLG---IGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLAR----K 169

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 515998033 174 VEI----RRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNIEQLDAPSTIF 222
Cdd:COG4148  170 AEIlpylERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVL 222
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
 3-222 2.18e-57

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: 186.79  E-value: 2.18e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   3 LLTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVNK--RNFGFV 80
Cdd:COG1120    1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRElaRRIAYV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  81 FQSYALFPHLSVFDNVAFGL-----RLRKVKEDDvKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLL 155
Cdd:COG1120   81 PQEPPAPFGLTVRELVALGRyphlgLFGRPSAED-REAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLL 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515998033 156 LFDEPLSNLDAN--LRVnMRVeIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNIEQLDAPSTIF 222
Cdd:COG1120  160 LLDEPTSHLDLAhqLEV-LEL-LRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVL 226
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
 9-212 5.38e-55

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: 179.26  E-value: 5.38e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   9 VSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVN----KRNFGFVFQSY 84
Cdd:cd03262    6 LHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinelRQKVGMVFQQF 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  85 ALFPHLSVFDNVAFGLR-LRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLSN 163
Cdd:cd03262   86 NLFPHLTVLENITLAPIkVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSA 165

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 515998033 164 LDANLrVNMRVE-IRRIQQElGITTVYVSHDQEECFSISDQVAIMNKGNI 212
Cdd:cd03262  166 LDPEL-VGEVLDvMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
 2-225 1.04e-54

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: 187.03  E-value: 1.04e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   2 ALLTLDRVSVAYDNQ--LILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAK---QGTFLFGDKDYTRVPVNKR- 75
Cdd:COG1123    3 PLLEVRDLSVRYPGGdvPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRg 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  76 -NFGFVFQS--YALFPhLSVFDNVAFGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEP 152
Cdd:COG1123   83 rRIGMVFQDpmTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDP 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515998033 153 DLLLFDEPLSNLDANLRVNMRVEIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNIEQLDAPSTIFKYP 225
Cdd:COG1123  162 DLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAP 234
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
3-196 1.39e-54

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 179.51  E-value: 1.39e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   3 LLTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKdytRV--PVNKRnfGFV 80
Cdd:PRK11248   1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGK---PVegPGAER--GVV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  81 FQSYALFPHLSVFDNVAFGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEP 160
Cdd:PRK11248  76 FQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEP 155

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 515998033 161 LSNLDANLRVNMRVEIRRIQQELGITTVYVSHDQEE 196
Cdd:PRK11248 156 FGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEE 191
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
 1-210 1.31e-52

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 174.12  E-value: 1.31e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   1 MALLTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVpvnKRNFGFV 80
Cdd:COG1121    4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA---RRRIGYV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  81 FQSYAL---FPhLSVFDNVAFGLR-----LRKVKEDDvKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEP 152
Cdd:COG1121   81 PQRAEVdwdFP-ITVRDVVLMGRYgrrglFRRPSRAD-REAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDP 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 515998033 153 DLLLFDEPLSNLDANLRVN-MRVeIRRIQQElGITTVYVSHDQEECFSISDQVAIMNKG 210
Cdd:COG1121  159 DLLLLDEPFAGVDAATEEAlYEL-LRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRG 215
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
 4-212 5.26e-52

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: 171.52  E-value: 5.26e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   4 LTLDRVSVAYDNQLIlqDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVNKRNFGFVFQS 83
Cdd:cd03298    1 VRLDKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  84 YALFPHLSVFDNVAFGL--RLRKVKEDdvKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPL 161
Cdd:cd03298   79 NNLFAHLTVEQNVGLGLspGLKLTAED--RQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPF 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 515998033 162 SNLDANLRVNMRVEIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNI 212
Cdd:cd03298  157 AALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
 3-225 1.18e-51

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: 171.22  E-value: 1.18e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   3 LLTLDRVSVAYDNQ----LILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVNK---- 74
Cdd:cd03258    1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElrka 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  75 -RNFGFVFQSYALFPHLSVFDNVAFGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPD 153
Cdd:cd03258   81 rRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515998033 154 LLLFDEPLSNLDANLRVNMRVEIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNIEQLDAPSTIFKYP 225
Cdd:cd03258  161 VLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANP 232
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
4-212 3.56e-51

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 169.23  E-value: 3.56e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   4 LTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVNK--RNFGFVF 81
Cdd:COG4619    1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwrRQVAYVP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  82 QSYALFPHlSVFDNVAFGLRLRKVKEDDvkRRVMTMLDTVSLGG--FEKRFpGELSGGQRQRVAIARALVIEPDLLLFDE 159
Cdd:COG4619   81 QEPALWGG-TVRDNLPFPFQLRERKFDR--ERALELLERLGLPPdiLDKPV-ERLSGGERQRLALIRALLLQPDVLLLDE 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 515998033 160 PLSNLDANLRVnmRVE--IRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNI 212
Cdd:COG4619  157 PTSALDPENTR--RVEelLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
PhnC COG3638
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ...
 2-219 3.75e-51

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


Pssm-ID: 442855 [Multi-domain]  Cd Length: 249  Bit Score: 170.24  E-value: 3.75e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   2 ALLTLDRVSVAYDNQ-LILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVNK-----R 75
Cdd:COG3638    1 PMLELRNLSKRYPGGtPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAlrrlrR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  76 NFGFVFQSYALFPHLSVFDNVAFG-------LR--LRKVKEDDvKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIAR 146
Cdd:COG3638   81 RIGMIFQQFNLVPRLSVLTNVLAGrlgrtstWRslLGLFPPED-RERALEALERVGLADKAYQRADQLSGGQQQRVAIAR 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515998033 147 ALVIEPDLLLFDEPLSNLD-ANLRVNMRVeIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNIeQLDAPS 219
Cdd:COG3638  160 ALVQEPKLILADEPVASLDpKTARQVMDL-LRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRV-VFDGPP 231
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
 6-212 4.59e-51

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: 168.87  E-value: 4.59e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   6 LDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPvnkRNFGFVFQSYA 85
Cdd:cd03235    2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKER---KRIGYVPQRRS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  86 L---FPhLSVFDNVAFGLR-----LRKVKEDDvKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLF 157
Cdd:cd03235   79 IdrdFP-ISVRDVVLMGLYghkglFRRLSKAD-KAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLL 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 515998033 158 DEPLSNLDANLRVNMRVEIRRIQQElGITTVYVSHDQEECFSISDQVAIMNKGNI 212
Cdd:cd03235  157 DEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
 3-221 5.16e-51

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: 170.04  E-value: 5.16e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   3 LLTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPV-NKRNFGFVF 81
Cdd:COG4555    1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPReARRQIGVLP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  82 QSYALFPHLSVFDNVAFGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPL 161
Cdd:COG4555   81 DERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPT 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033 162 SNLDANLRVNMRVEIRRIQQElGITTVYVSHDQEECFSISDQVAIMNKGNIEQLDAPSTI 221
Cdd:COG4555  161 NGLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
 4-221 6.46e-51

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: 169.28  E-value: 6.46e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   4 LTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQ-----GTFLFGDKDYTRVPVN----K 74
Cdd:cd03260    1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPgapdeGEVLLDGKDIYDLDVDvlelR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  75 RNFGFVFQSYALFPhLSVFDNVAFGLRLRKVKEDDV-KRRVMTMLDTVSLGGFEKR--FPGELSGGQRQRVAIARALVIE 151
Cdd:cd03260   81 RRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEElDERVEEALRKAALWDEVKDrlHALGLSGGQQQRLCLARALANE 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515998033 152 PDLLLFDEPLSNLDAnlRVNMRVE--IRRIQQElgITTVYVSHDQEECFSISDQVAIMNKGNIEQLDAPSTI 221
Cdd:cd03260  160 PEVLLLDEPTSALDP--ISTAKIEelIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...
 1-210 1.42e-50

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: 169.06  E-value: 1.42e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   1 MALLTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVNKRN-FGF 79
Cdd:COG0411    2 DPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIArLGI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  80 V--FQSYALFPHLSVFDNVA---------------FGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRV 142
Cdd:COG0411   82 ArtFQNPRLFPELTVLENVLvaaharlgrgllaalLRLPRARREEREARERAEELLERVGLADRADEPAGNLSYGQQRRL 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515998033 143 AIARALVIEPDLLLFDEPLSNLDANLRVNMRVEIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKG 210
Cdd:COG0411  162 EIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFG 229
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
3-212 3.90e-50

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 167.45  E-value: 3.90e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   3 LLTLDRVSVAYDNQLILqdFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVNKRNFGFVFQ 82
Cdd:PRK10771   1 MLKLTDITWLYHHLPMR--FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  83 SYALFPHLSVFDNVAFG----LRLrkvkEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFD 158
Cdd:PRK10771  79 ENNLFSHLTVAQNIGLGlnpgLKL----NAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLD 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 515998033 159 EPLSNLDANLRVNMRVEIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNI 212
Cdd:PRK10771 155 EPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRI 208
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
19-235 3.08e-49

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 168.33  E-value: 3.08e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  19 LQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGfLE-AKQGTFLFGDKDYTRVPVNK-----RNFGFVFQSYALFPHLSV 92
Cdd:COG1135   21 LDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINL-LErPTSGSVLVDGVDLTALSERElraarRKIGMIFQHFNLLSSRTV 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  93 FDNVAFGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLSNLDAN----- 167
Cdd:COG1135  100 AENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKVLLCDEATSALDPEttrsi 179

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515998033 168 LRVnmrveIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNIEQLDAPSTIFKYPTTEFVARFIG 235
Cdd:COG1135  180 LDL-----LKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSELTRRFLP 242
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
 4-212 1.05e-48

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: 161.41  E-value: 1.05e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   4 LTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVN-KRNFGFVFQ 82
Cdd:cd03230    1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEvKRRIGYLPE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  83 SYALFPHLSVFDNVafglrlrkvkeddvkrrvmtmldtvslggfekrfpgELSGGQRQRVAIARALVIEPDLLLFDEPLS 162
Cdd:cd03230   81 EPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTS 124

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 515998033 163 NLDANLRVNMRVEIRRIQQElGITTVYVSHDQEECFSISDQVAIMNKGNI 212
Cdd:cd03230  125 GLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
thiQ TIGR01277
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ...
 4-215 1.91e-48

thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]


Pssm-ID: 130344 [Multi-domain]  Cd Length: 213  Bit Score: 162.34  E-value: 1.91e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033    4 LTLDRVSVAYDNQLIlqDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVNKRNFGFVFQS 83
Cdd:TIGR01277   1 LALDKVRYEYEHLPM--EFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSMLFQE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   84 YALFPHLSVFDNVAFG----LRLRKVKeddvKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDE 159
Cdd:TIGR01277  79 NNLFAHLTVRQNIGLGlhpgLKLNAEQ----QEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDE 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 515998033  160 PLSNLDANLRVNMRVEIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNIEQL 215
Cdd:TIGR01277 155 PFSALDPLLREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVV 210
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
 6-241 4.69e-48

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 162.11  E-value: 4.69e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   6 LDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIaGFLE-AKQGTFLFGDK--DYTRVPVNK------RN 76
Cdd:PRK11124   5 LNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVL-NLLEmPRSGTLNIAGNhfDFSKTPSDKairelrRN 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  77 FGFVFQSYALFPHLSVFDN-VAFGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLL 155
Cdd:PRK11124  84 VGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVL 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033 156 LFDEPLSNLDANLrVNMRVEIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNI-EQLDAPStiFKYPTTEfvarfi 234
Cdd:PRK11124 164 LFDEPTAALDPEI-TAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIvEQGDASC--FTQPQTE------ 234


                 ....*..
gi 515998033 235 GFNNFLS 241
Cdd:PRK11124 235 AFKNYLS 241
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
8-234 8.49e-48

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 161.41  E-value: 8.49e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   8 RVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVNKRNF----GFVFQS 83
Cdd:PRK09493   6 NVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIrqeaGMVFQQ 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  84 YALFPHLSVFDNVAFG-LRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLS 162
Cdd:PRK09493  86 FYLFPHLTALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTS 165

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515998033 163 NLDANLrvnmRVEIRRIQQEL---GITTVYVSHDQEECFSISDQVAIMNKGNIEQLDAPSTIFKYPTTEFVARFI 234
Cdd:PRK09493 166 ALDPEL----RHEVLKVMQDLaeeGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFL 236
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
6-241 1.09e-47

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


Pssm-ID: 443326 [Multi-domain]  Cd Length: 242  Bit Score: 161.33  E-value: 1.09e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   6 LDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLI-------AGFLEAKQGTFLFGDK-DYTRVPVNKRNF 77
Cdd:COG4161    5 LKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLnlletpdSGQLNIAGHQFDFSQKpSEKAIRLLRQKV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  78 GFVFQSYALFPHLSVFDN-VAFGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLL 156
Cdd:COG4161   85 GMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLL 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033 157 FDEPLSNLDANLrVNMRVEIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNI-EQLDApsTIFKYPTTEfvarfiG 235
Cdd:COG4161  165 FDEPTAALDPEI-TAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIiEQGDA--SHFTQPQTE------A 235


                 ....*.
gi 515998033 236 FNNFLS 241
Cdd:COG4161  236 FAHYLS 241
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
 4-212 5.32e-47

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: 159.14  E-value: 5.32e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   4 LTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVNKRN-FGFV-- 80
Cdd:cd03219    1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIArLGIGrt 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  81 FQSYALFPHLSVFDNVAFGLRLRKV----------KEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVI 150
Cdd:cd03219   81 FQIPRLFPELTVLENVMVAAQARTGsglllararrEEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALAT 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515998033 151 EPDLLLFDEPLSNLDANLRVNMRVEIRRIQQElGITTVYVSHDQEECFSISDQVAIMNKGNI 212
Cdd:cd03219  161 DPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRV 221
FtsE TIGR02673
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ...
 6-195 2.08e-46

cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]


Pssm-ID: 131721 [Multi-domain]  Cd Length: 214  Bit Score: 157.02  E-value: 2.08e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033    6 LDRVSVAYD-NQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTR-----VPVNKRNFGF 79
Cdd:TIGR02673   4 FHNVSKAYPgGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRlrgrqLPLLRRRIGV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   80 VFQSYALFPHLSVFDNVAFGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDE 159
Cdd:TIGR02673  84 VFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLADE 163

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 515998033  160 PLSNLDANLrvnmRVEIRRIQQEL---GITTVYVSHDQE 195
Cdd:TIGR02673 164 PTGNLDPDL----SERILDLLKRLnkrGTTVIVATHDLS 198
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 19-162 5.12e-46

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


Pssm-ID: 394964 [Multi-domain]  Cd Length: 150  Bit Score: 153.96  E-value: 5.12e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   19 LQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVN--KRNFGFVFQSYALFPHLSVFDNV 96
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKslRKEIGYVFQDPQLFPRLTVRENL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   97 AFGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKR----FPGELSGGQRQRVAIARALVIEPDLLLFDEPLS 162
Cdd:pfam00005  81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRpvgeRPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
ECF_ATPase_2 TIGR04521
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
 4-226 1.10e-45

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 downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]


Pssm-ID: 275314 [Multi-domain]  Cd Length: 277  Bit Score: 157.23  E-value: 1.10e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033    4 LTLDRVSVAYD-----NQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKD-YTRVPVNKRNF 77
Cdd:TIGR04521   1 IKLKNVSYIYQpgtpfEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDiTAKKKKKLKDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   78 ----GFVFQ--SYALFpHLSVFDNVAFGLRLRKVKEDDVKRRVMTMLDTVSLG-GFEKRFPGELSGGQRQRVAIARALVI 150
Cdd:TIGR04521  81 rkkvGLVFQfpEHQLF-EETVYKDIAFGPKNLGLSEEEAEERVKEALELVGLDeEYLERSPFELSGGQMRRVAIAGVLAM 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515998033  151 EPDLLLFDEPLSNLDANLRVNMRVEIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNIEQLDAPSTIFKYPT 226
Cdd:TIGR04521 160 EPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDVD 235
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
 4-212 2.61e-45

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 155.61  E-value: 2.61e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   4 LTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGD------KDYTRVpvnkrnf 77
Cdd:PRK11247  13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTaplaeaREDTRL------- 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  78 gfVFQSYALFPHLSVFDNVAFGLRlrkvkeDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLF 157
Cdd:PRK11247  86 --MFQDARLLPWKKVIDNVGLGLK------GQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLL 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 515998033 158 DEPLSNLDANLRVNMRVEIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNI 212
Cdd:PRK11247 158 DEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
17-233 3.42e-45

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


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 159.43  E-value: 3.42e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  17 LILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVP------VNKRNFGFVFQSYALFPHL 90
Cdd:PRK10070  42 LGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISdaelreVRRKKIAMVFQSFALMPHM 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  91 SVFDNVAFGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLSNLDANLRV 170
Cdd:PRK10070 122 TVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRT 201

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515998033 171 NMRVEIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNIEQLDAPSTIFKYPTTEFVARF 233
Cdd:PRK10070 202 EMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTF 264
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
 21-232 3.64e-45

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: 157.97  E-value: 3.64e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   21 DFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQG------TFLFGDKDYTRVPVNKRNFGFVFQSYALFPHLSVFD 94
Cdd:TIGR02142  15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGeivlngRTLFDSRKGIFLPPEKRRIGYVFQEARLFPHLSVRG 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   95 NVAFGLRLRKVKEDDVK-RRVMTMLdtvSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLSNLDANLRVNMR 173
Cdd:TIGR02142  95 NLRYGMKRARPSERRISfERVIELL---GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEIL 171

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 515998033  174 VEIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNIEQLDAPSTIFKYPTTEFVAR 232
Cdd:TIGR02142 172 PYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPWLAR 230
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
 4-212 5.24e-45

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: 153.12  E-value: 5.24e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   4 LTLDRVSVAYDNQLILQDFDLQLERGqLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVNKRN-FGFVFQ 82
Cdd:cd03264    1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRrIGYLPQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  83 SYALFPHLSVFDNVAFGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLS 162
Cdd:cd03264   80 EFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 515998033 163 NLDanlrVNMRVEIRRIQQELGIT-TVYVS-HDQEECFSISDQVAIMNKGNI 212
Cdd:cd03264  160 GLD----PEERIRFRNLLSELGEDrIVILStHIVEDVESLCNQVAVLNKGKL 207
ECF_ATPase_1 TIGR04520
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
 6-223 1.09e-44

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: 154.13  E-value: 1.09e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033    6 LDRVSVAYDNQ--LILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDyTRVPVN----KRNFGF 79
Cdd:TIGR04520   3 VENVSFSYPESekPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLD-TLDEENlweiRKKVGM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   80 VFQSyalfPH-----LSVFDNVAFGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDL 154
Cdd:TIGR04520  82 VFQN----PDnqfvgATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDI 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515998033  155 LLFDEPLSNLDANLRVNMRVEIRRIQQELGITTVYVSHDQEECFSiSDQVAIMNKGNIEQLDAPSTIFK 223
Cdd:TIGR04520 158 IILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREIFS 225
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
 5-212 1.32e-44

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: 151.05  E-value: 1.32e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   5 TLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVNK--RNFGFVFQ 82
Cdd:cd03214    1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKElaRKIAYVPQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  83 syalfphlsvfdnvafglrlrkvkeddvkrrvmtMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLS 162
Cdd:cd03214   81 ----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTS 126

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 515998033 163 NLDANLRVNMRVEIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNI 212
Cdd:cd03214  127 HLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRI 176
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
 5-210 2.84e-44

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: 149.70  E-value: 2.84e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   5 TLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPV--NKRNFGFVFQ 82
Cdd:cd00267    1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLeeLRRRIGYVPQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  83 syalfphlsvfdnvafglrlrkvkeddvkrrvmtmldtvslggfekrfpgeLSGGQRQRVAIARALVIEPDLLLFDEPLS 162
Cdd:cd00267   81 ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 515998033 163 NLDANLRVNMRVEIRRIQQElGITTVYVSHDQEECFSISDQVAIMNKG 210
Cdd:cd00267  110 GLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDG 156
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
 2-196 1.04e-43

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: 149.55  E-value: 1.04e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   2 ALLTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVN-KRNFGFV 80
Cdd:COG4133    1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDyRRRLAYL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  81 FQSYALFPHLSVFDNVAFGLRLRKVKEDDvkRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEP 160
Cdd:COG4133   81 GHADGLKPELTVRENLRFWAALYGLRADR--EAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEP 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 515998033 161 LSNLDANlrvnmRVEI--RRIQQEL--GITTVYVSHDQEE 196
Cdd:COG4133  159 FTALDAA-----GVALlaELIAAHLarGGAVLLTTHQPLE 193
HisP COG4598
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
18-234 1.20e-43

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


Pssm-ID: 443652 [Multi-domain]  Cd Length: 259  Bit Score: 151.11  E-value: 1.20e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  18 ILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIaGFLE-AKQGTFLFG--------DKDYTRVPVNKR-------NFGFVF 81
Cdd:COG4598   23 VLKGVSLTARKGDVISIIGSSGSGKSTFLRCI-NLLEtPDSGEIRVGgeeirlkpDRDGELVPADRRqlqrirtRLGMVF 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  82 QSYALFPHLSVFDNVAFG-LRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEP 160
Cdd:COG4598  102 QSFNLWSHMTVLENVIEApVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIARALAMEPEVMLFDEP 181

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515998033 161 LSNLDANLrVNmrvEIRRIQQEL---GITTVYVSHDQEECFSISDQVAIMNKGNIEQLDAPSTIFKYPTTEFVARFI 234
Cdd:COG4598  182 TSALDPEL-VG---EVLKVMRDLaeeGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGNPKSERLRQFL 254
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
 23-207 1.34e-43

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


Pssm-ID: 443658 [Multi-domain]  Cd Length: 329  Bit Score: 152.96  E-value: 1.34e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  23 DLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVNK-----RNFGFVFQ-SYA-LFPHLSVFDN 95
Cdd:COG4608   38 SFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRElrplrRRMQMVFQdPYAsLNPRMTVGDI 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  96 VAFGLRLRKVK-EDDVKRRVMTMLDTVSLG-GFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLSNLDANLR---V 170
Cdd:COG4608  118 IAEPLRIHGLAsKAERRERVAELLELVGLRpEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQaqvL 197

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 515998033 171 NMrveIRRIQQELGITTVYVSHDqeecFS----ISDQVAIM 207
Cdd:COG4608  198 NL---LEDLQDELGLTYLFISHD----LSvvrhISDRVAVM 231
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
 19-210 4.46e-43

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: 148.77  E-value: 4.46e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   19 LQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRvPVNKRNFgfVFQSYALFPHLSVFDNVAF 98
Cdd:TIGR01184   1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITE-PGPDRMV--VFQNYSLLPWLTVRENIAL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   99 GLR--LRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLSNLDANLRVNMRVEI 176
Cdd:TIGR01184  78 AVDrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEEL 157

                         170       180       190
                  ....*....|....*....|....*....|....
gi 515998033  177 RRIQQELGITTVYVSHDQEECFSISDQVAIMNKG 210
Cdd:TIGR01184 158 MQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
 2-195 4.86e-43

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: 148.74  E-value: 4.86e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   2 ALLTLDRVSVAY---DNQL-ILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGT-FLFG------DKDyTRV 70
Cdd:COG4181    7 PIIELRGLTKTVgtgAGELtILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTvRLAGqdlfalDED-ARA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  71 PVNKRNFGFVFQSYALFPHLSVFDNVAFGLRLRKvkEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVI 150
Cdd:COG4181   86 RLRARHVGFVFQSFQLLPTLTALENVMLPLELAG--RRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFAT 163

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 515998033 151 EPDLLLFDEPLSNLDANLRVNMRVEIRRIQQELGITTVYVSHDQE 195
Cdd:COG4181  164 EPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPA 208
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
 1-235 1.55e-42

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 147.97  E-value: 1.55e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   1 MALLTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDK--DYTRvPVNKR--- 75
Cdd:PRK11264   1 MSAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDItiDTAR-SLSQQkgl 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  76 ------NFGFVFQSYALFPHLSVFDNVAFG-LRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARAL 148
Cdd:PRK11264  80 irqlrqHVGFVFQNFNLFPHRTVLENIIEGpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARAL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033 149 VIEPDLLLFDEPLSNLDANLRVNMRVEIRRIQQElGITTVYVSHDQEECFSISDQVAIMNKGNI-EQLDApSTIFKYP-- 225
Cdd:PRK11264 160 AMRPEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIvEQGPA-KALFADPqq 237

                        250
                 ....*....|..
gi 515998033 226 --TTEFVARFIG 235
Cdd:PRK11264 238 prTRQFLEKFLL 249
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
 19-235 2.38e-42

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 150.34  E-value: 2.38e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  19 LQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVN-----KRNFGFVFQSYALFPHLSVF 93
Cdd:PRK11153  21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKelrkaRRQIGMIFQHFNLLSSRTVF 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  94 DNVAFGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLSNLD-----ANL 168
Cdd:PRK11153 101 DNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATSALDpattrSIL 180

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515998033 169 RVnmrveIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNIEQLDAPSTIFKYPTTEFVARFIG 235
Cdd:PRK11153 181 EL-----LKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTREFIQ 242
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
 4-212 2.42e-42

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: 146.81  E-value: 2.42e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   4 LTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVNKRNF---GFV 80
Cdd:cd03224    1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARagiGYV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  81 FQSYALFPHLSVFDNVAFGLRLRkvKEDDVKRRVMTMLDTVS-LGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDE 159
Cdd:cd03224   81 PEGRRIFPELTVEENLLLGAYAR--RRAKRKARLERVYELFPrLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDE 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 515998033 160 PLSNLDANLRVNMRVEIRRIQQElGITTVYVSHDQEECFSISDQVAIMNKGNI 212
Cdd:cd03224  159 PSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRV 210
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
 3-225 2.45e-42

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: 149.43  E-value: 2.45e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   3 LLTLDRVSVAY--DNQLI--LQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAK---QGTFLFGDKDYTRVP---- 71
Cdd:COG0444    1 LLEVRNLKVYFptRRGVVkaVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKLSekel 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  72 --VNKRNFGFVFQ-SY-ALFPHLSVFDNVAFGLRL-RKVKEDDVKRRVMTMLDTVSLGGFEKR---FPGELSGGQRQRVA 143
Cdd:COG0444   81 rkIRGREIQMIFQdPMtSLNPVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLPDPERRldrYPHELSGGMRQRVM 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033 144 IARALVIEPDLLLFDEPLSNLDanlrVNMRVEI----RRIQQELGITTVYVSHD----QEecfsISDQVAIMNKGNI-EQ 214
Cdd:COG0444  161 IARALALEPKLLIADEPTTALD----VTIQAQIlnllKDLQRELGLAILFITHDlgvvAE----IADRVAVMYAGRIvEE 232

                        250
                 ....*....|..
gi 515998033 215 ldAPS-TIFKYP 225
Cdd:COG0444  233 --GPVeELFENP 242
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
 1-212 3.27e-42

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: 146.67  E-value: 3.27e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   1 MALLTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVNKRN---F 77
Cdd:COG0410    1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIArlgI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  78 GFVFQSYALFPHLSVFDNVAFGLRLRKVKEDDVKRrvmtmLDTVslggFEkRFP----------GELSGGQRQRVAIARA 147
Cdd:COG0410   81 GYVPEGRRIFPSLTVEENLLLGAYARRDRAEVRAD-----LERV----YE-LFPrlkerrrqraGTLSGGEQQMLAIGRA 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515998033 148 LVIEPDLLLFDEPLSNLDANLRVNMRVEIRRIQQElGITTVYVSHDQEECFSISDQVAIMNKGNI 212
Cdd:COG0410  151 LMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRI 214
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
 4-212 7.07e-42

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: 146.17  E-value: 7.07e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   4 LTLDRVSVAYDNQL-ILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVNK-----RNF 77
Cdd:cd03256    1 IEVENLSKTYPNGKkALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrqlrRQI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  78 GFVFQSYALFPHLSVFDNVAFG-------LR--LRKVKEDDvKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARAL 148
Cdd:cd03256   81 GMIFQQFNLIERLSVLENVLSGrlgrrstWRslFGLFPKEE-KQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARAL 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515998033 149 VIEPDLLLFDEPLSNLDANL-RVNMRVeIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNI 212
Cdd:cd03256  160 MQQPKLILADEPVASLDPASsRQVMDL-LKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRI 223
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
 16-212 1.31e-41

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: 144.57  E-value: 1.31e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  16 QLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVN-KRNFGFVFQSYALFPHLSVFD 94
Cdd:cd03263   15 KPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAaRQSLGYCPQFDALFDELTVRE 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  95 NVAFGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLSNLDANLRVNMRV 174
Cdd:cd03263   95 HLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWD 174

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 515998033 175 EIRRIQQELGIttVYVSHDQEECFSISDQVAIMNKGNI 212
Cdd:cd03263  175 LILEVRKGRSI--ILTTHSMDEAEALCDRIAIMSDGKL 210
LolD_lipo_ex TIGR02211
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ...
 18-195 1.76e-41

lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 131266 [Multi-domain]  Cd Length: 221  Bit Score: 144.42  E-value: 1.76e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   18 ILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVNKR------NFGFVFQSYALFPHLS 91
Cdd:TIGR02211  20 VLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERaklrnkKLGFIYQFHHLLPDFT 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   92 VFDNVAFGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLSNLDANLRVN 171
Cdd:TIGR02211 100 ALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLVLADEPTGNLDNNNAKI 179

                         170       180
                  ....*....|....*....|....
gi 515998033  172 MRVEIRRIQQELGITTVYVSHDQE 195
Cdd:TIGR02211 180 IFDLMLELNRELNTSFLVVTHDLE 203
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
9-207 2.18e-41

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 145.68  E-value: 2.18e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   9 VSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDY-----TRVPVNKRNFGFVFQS 83
Cdd:PRK11831  13 VSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamsrSRLYTVRKRMSMLFQS 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  84 YALFPHLSVFDNVAFGLRLR-KVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLS 162
Cdd:PRK11831  93 GALFTDMNVFDNVAYPLREHtQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFV 172

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 515998033 163 NLDAnlrVNMRVEIRRIQQ---ELGITTVYVSHDQEECFSISDQVAIM 207
Cdd:PRK11831 173 GQDP---ITMGVLVKLISElnsALGVTCVVVSHDVPEVLSIADHAYIV 217
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
 4-210 1.11e-40

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: 140.60  E-value: 1.11e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   4 LTLDRVSVAYDN--QLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVNK--RNFGF 79
Cdd:cd03228    1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESlrKNIAY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  80 VFQSYALFpHLSVFDNVafglrlrkvkeddvkrrvmtmldtvslggfekrfpgeLSGGQRQRVAIARALVIEPDLLLFDE 159
Cdd:cd03228   81 VPQDPFLF-SGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDE 122

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 515998033 160 PLSNLDANLRVNMRVEIRRIQQelGITTVYVSHDqEECFSISDQVAIMNKG 210
Cdd:cd03228  123 ATSALDPETEALILEALRALAK--GKTVIVIAHR-LSTIRDADRIIVLDDG 170
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
 19-195 2.04e-40

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: 141.39  E-value: 2.04e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  19 LQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYT-----RVPVNKRNFGFVFQSYALFPHLSVF 93
Cdd:cd03292   17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSdlrgrAIPYLRRKIGVVFQDFRLLPDRNVY 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  94 DNVAFGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLSNLDAnlrvNMR 173
Cdd:cd03292   97 ENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDP----DTT 172

                        170       180
                 ....*....|....*....|....*
gi 515998033 174 VEIRRIQQEL---GITTVYVSHDQE 195
Cdd:cd03292  173 WEIMNLLKKInkaGTTVVVATHAKE 197
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
 4-234 2.29e-40

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


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 142.48  E-value: 2.29e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   4 LTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLR-------LIAGF-LEakqGTFLFGDKD-YTR-VPVN 73
Cdd:COG1117   12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRclnrmndLIPGArVE---GEILLDGEDiYDPdVDVV 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  74 K--RNFGFVFQSYALFPHlSVFDNVAFGLRLRKVKE------------------DDVKRRvmtmLDTVSLGgfekrfpge 133
Cdd:COG1117   89 ElrRRVGMVFQKPNPFPK-SIYDNVAYGLRLHGIKSkseldeiveeslrkaalwDEVKDR----LKKSALG--------- 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033 134 LSGGQRQRVAIARALVIEPDLLLFDEPLSNLD--AnlrvNMRVE--IRRIQQELGIttVYVSHDQEECFSISDQVAIMNK 209
Cdd:COG1117  155 LSGGQQQRLCIARALAVEPEVLLMDEPTSALDpiS----TAKIEelILELKKDYTI--VIVTHNMQQAARVSDYTAFFYL 228

                        250       260
                 ....*....|....*....|....*
gi 515998033 210 GNIEQLDAPSTIFKYPTTEFVARFI 234
Cdd:COG1117  229 GELVEFGPTEQIFTNPKDKRTEDYI 253
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
 1-212 3.25e-40

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: 142.15  E-value: 3.25e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   1 MALLTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGT--FLFGdKDYTRVPVN--KRN 76
Cdd:COG1119    1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdvRLFG-ERRGGEDVWelRKR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  77 FGFVfqSYALF----PHLSVFDNVAFGL-----RLRKVKEDDvKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARA 147
Cdd:COG1119   80 IGLV--SPALQlrfpRDETVLDVVLSGFfdsigLYREPTDEQ-RERARELLELLGLAHLADRPFGTLSQGEQRRVLIARA 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515998033 148 LVIEPDLLLFDEPLSNLDANLRVNMRVEIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNI 212
Cdd:COG1119  157 LVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRV 221
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
 13-218 3.51e-40

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: 140.97  E-value: 3.51e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  13 YDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVN-KRNFGFVFQSYALFPHLS 91
Cdd:cd03265   10 YGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREvRRRIGIVFQDLSVDDELT 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  92 VFDNVAFGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLSNLDANLRVN 171
Cdd:cd03265   90 GWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAH 169

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 515998033 172 MRVEIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNIEQLDAP 218
Cdd:cd03265  170 VWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTP 216
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
4-214 6.09e-40

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 148.39  E-value: 6.09e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   4 LTLDRVSVAYDN-QLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVNK--RNFGFV 80
Cdd:COG1132  340 IEFENVSFSYPGdRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESlrRQIGVV 419

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  81 FQSYALFpHLSVFDNVAFGlrlrkvKEDDVKRRVMTMLDTVSLGGFEKRFP-------GE----LSGGQRQRVAIARALV 149
Cdd:COG1132  420 PQDTFLF-SGTIRENIRYG------RPDATDEEVEEAAKAAQAHEFIEALPdgydtvvGErgvnLSGGQRQRIAIARALL 492

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515998033 150 IEPDLLLFDEPLSNLDAnlrvnmRVEiRRIQQEL-----GITTVYVSHdqeecfSIS-----DQVAIMNKGNIEQ 214
Cdd:COG1132  493 KDPPILILDEATSALDT------ETE-ALIQEALerlmkGRTTIVIAH------RLStirnaDRILVLDDGRIVE 554
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
 3-212 6.69e-40

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: 140.20  E-value: 6.69e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   3 LLTLDRVSVAYDNQ----LILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVN-KRNF 77
Cdd:cd03266    1 MITADALTKRFRDVkktvQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEaRRRL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  78 GFVFQSYALFPHLSVFDNVAFGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLF 157
Cdd:cd03266   81 GFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLL 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 515998033 158 DEPLSNLDANLRVNMRVEIRRiQQELGITTVYVSHDQEECFSISDQVAIMNKGNI 212
Cdd:cd03266  161 DEPTTGLDVMATRALREFIRQ-LRALGKCILFSTHIMQEVERLCDRVVVLHRGRV 214
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
 19-228 9.55e-40

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: 147.14  E-value: 9.55e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  19 LQDFDLQLERGQLLSLLGPSGCGKTTT----LRLIAGfleakQGTFLFGDKDYTRVPVN-----KRNFGFVFQS-YA-LF 87
Cdd:COG4172  302 VDGVSLTLRRGETLGLVGESGSGKSTLglalLRLIPS-----EGEIRFDGQDLDGLSRRalrplRRRMQVVFQDpFGsLS 376

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  88 PHLSVFDNVAFGLRLRKVKEDDVKR--RVMTMLDTVSL-GGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLSNL 164
Cdd:COG4172  377 PRMTVGQIIAEGLRVHGPGLSAAERraRVAEALEEVGLdPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSAL 456

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515998033 165 DanlrVNMRVEI----RRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNI-EQLDApSTIFKYPTTE 228
Cdd:COG4172  457 D----VSVQAQIldllRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVvEQGPT-EQVFDAPQHP 520
cbiO PRK13650
energy-coupling factor transporter ATPase;
1-222 2.52e-39

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 140.64  E-value: 2.52e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   1 MALLTLDRVSVAYD---NQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPV--NKR 75
Cdd:PRK13650   2 SNIIEVKNLTFKYKedqEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVwdIRH 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  76 NFGFVFQSY-ALFPHLSVFDNVAFGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDL 154
Cdd:PRK13650  82 KIGMVFQNPdNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKI 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515998033 155 LLFDEPLSNLDANLRVNMRVEIRRIQQELGITTVYVSHDQEEcFSISDQVAIMNKGNIEQLDAPSTIF 222
Cdd:PRK13650 162 IILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDE-VALSDRVLVMKNGQVESTSTPRELF 228
ABC_phnC TIGR02315
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ...
 3-221 7.85e-39

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: 138.20  E-value: 7.85e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033    3 LLTLDRVSVAYDNQ-LILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVNK-----RN 76
Cdd:TIGR02315   1 MLEVENLSKVYPNGkQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKlrklrRR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   77 FGFVFQSYALFPHLSVFDNVAFGlRL-----------RKVKEDdvKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIA 145
Cdd:TIGR02315  81 IGMIFQHYNLIERLTVLENVLHG-RLgykptwrsllgRFSEED--KERALSALERVGLADKAYQRADQLSGGQQQRVAIA 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515998033  146 RALVIEPDLLLFDEPLSNLDANLRVNMRVEIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNIEQLDAPSTI 221
Cdd:TIGR02315 158 RALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSEL 233
cbiO PRK13637
energy-coupling factor transporter ATPase;
19-223 1.90e-38

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 138.64  E-value: 1.90e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  19 LQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVN----KRNFGFVFQ--SYALFPHlSV 92
Cdd:PRK13637  23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKlsdiRKKVGLVFQypEYQLFEE-TI 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  93 FDNVAFGLRLRKVKEDDVKRRVMTMLDTVSLG--GFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLSNLDANLRV 170
Cdd:PRK13637 102 EKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRD 181

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 515998033 171 NMRVEIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNIEQLDAPSTIFK 223
Cdd:PRK13637 182 EILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFK 234
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
 5-212 5.26e-38

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: 134.69  E-value: 5.26e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   5 TLDRVSVAY-DNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRvPVNKRNFGFVFQS 83
Cdd:cd03226    1 RIENISFSYkKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA-KERRKSIGYVMQD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  84 --YALFphlsvFDNVAFGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPL 161
Cdd:cd03226   80 vdYQLF-----TDSVREELLLGLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPT 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 515998033 162 SNLDanlRVNMRV--EIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNI 212
Cdd:cd03226  155 SGLD---YKNMERvgELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
3-224 1.60e-37

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 135.91  E-value: 1.60e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   3 LLTLDRVSVAYDNQ--LILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPV--NKRNFG 78
Cdd:PRK13635   5 IIRVEHISFRYPDAatYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVwdVRRQVG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  79 FVFQSY-ALFPHLSVFDNVAFGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLF 157
Cdd:PRK13635  85 MVFQNPdNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIIL 164

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515998033 158 DEPLSNLDANLRVNMRVEIRRIQQELGITTVYVSHDQEECFSiSDQVAIMNKGNIEQLDAPSTIFKY 224
Cdd:PRK13635 165 DEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFKS 230
nickel_nikE TIGR02769
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ...
 16-225 5.05e-37

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: 134.16  E-value: 5.05e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   16 QLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRV-PVNKRNF----GFVFQ-SYALF-P 88
Cdd:TIGR02769  24 APVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLdRKQRRAFrrdvQLVFQdSPSAVnP 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   89 HLSVFDNVAFGLR-LRKVKEDDVKRRVMTMLDTVSL-GGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLSNLDA 166
Cdd:TIGR02769 104 RMTVRQIIGEPLRhLTSLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDM 183

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515998033  167 NLRVNMRVEIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNI--EQLDAPSTIFKYP 225
Cdd:TIGR02769 184 VLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIveECDVAQLLSFKHP 244
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
 4-214 7.26e-37

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: 139.51  E-value: 7.26e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   4 LTLDRVSVAYDN-QLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVN--KRNFGFV 80
Cdd:COG4988  337 IELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPAswRRQIAWV 416

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  81 FQSYALFpHLSVFDNVAFGlrlrkvKEDDVKRRVMTMLDTVSLGGFEKRFP-------GE----LSGGQRQRVAIARALV 149
Cdd:COG4988  417 PQNPYLF-AGTIRENLRLG------RPDASDEELEAALEAAGLDEFVAALPdgldtplGEggrgLSGGQAQRLALARALL 489

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033 150 IEPDLLLFDEPLSNLDANLRvnmrveiRRIQQEL-----GITTVYVSHDQEECfSISDQVAIMNKGNIEQ 214
Cdd:COG4988  490 RDAPLLLLDEPTAHLDAETE-------AEILQALrrlakGRTVILITHRLALL-AQADRILVLDDGRIVE 551
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
 4-212 3.56e-36

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: 138.81  E-value: 3.56e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   4 LTLDRVSVAY--DNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVNK--RNFGF 79
Cdd:COG2274  474 IELENVSFRYpgDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASlrRQIGV 553

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  80 VFQSYALFpHLSVFDNVAFGlrlRKVKEDDvkrRVMTMLDTVSLGGFEKRFP-------GE----LSGGQRQRVAIARAL 148
Cdd:COG2274  554 VLQDVFLF-SGTIRENITLG---DPDATDE---EIIEAARLAGLHDFIEALPmgydtvvGEggsnLSGGQRQRLAIARAL 626

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515998033 149 VIEPDLLLFDEPLSNLDANLRvnmrveiRRIQQEL-----GITTVYVSHDqEECFSISDQVAIMNKGNI 212
Cdd:COG2274  627 LRNPRILILDEATSALDAETE-------AIILENLrrllkGRTVIIIAHR-LSTIRLADRIIVLDKGRI 687
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
21-212 5.15e-36

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 133.46  E-value: 5.15e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  21 DFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQG------TFLFGDKDYTRVPVNKRNFGFVFQSYALFPHLSVFD 94
Cdd:PRK11144  16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGrivlngRVLFDAEKGICLPPEKRRIGYVFQDARLFPHYKVRG 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  95 NVAFGLRlRKVKE--DDVkrrvmtmldtVSLGGFE---KRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLSNLDANLR 169
Cdd:PRK11144  96 NLRYGMA-KSMVAqfDKI----------VALLGIEpllDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRK 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 515998033 170 VNMRVEIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNI 212
Cdd:PRK11144 165 RELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKV 207
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
 4-212 7.99e-36

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: 129.26  E-value: 7.99e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   4 LTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVNKRNFGFVFQS 83
Cdd:cd03268    1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIEA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  84 YALFPHLSVFDNVAFGLRLRKVKeddvKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLSN 163
Cdd:cd03268   81 PGFYPNLTARENLRLLARLLGIR----KKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNG 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 515998033 164 LDANLRVNMRVEIRRIQQElGITTVYVSHDQEECFSISDQVAIMNKGNI 212
Cdd:cd03268  157 LDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKL 204
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
 4-212 9.33e-36

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: 129.59  E-value: 9.33e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   4 LTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVNKR---NFGFV 80
Cdd:cd03218    1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRarlGIGYL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  81 FQSYALFPHLSVFDNVAFGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEP 160
Cdd:cd03218   81 PQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 515998033 161 LSNLDAnlrvnMRV-EIRRIQQEL---GITTVYVSHDQEECFSISDQVAIMNKGNI 212
Cdd:cd03218  161 FAGVDP-----IAVqDIQKIIKILkdrGIGVLITDHNVRETLSITDRAYIIYEGKV 211
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
3-193 1.65e-35

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 128.84  E-value: 1.65e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   3 LLTLDRVSVAY-DNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTR-----VPVNKRN 76
Cdd:PRK10908   1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRlknreVPFLRRQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  77 FGFVFQSYALFPHLSVFDNVAFGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLL 156
Cdd:PRK10908  81 IGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLL 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 515998033 157 FDEPLSNLDANLRVNmrveIRRIQQE---LGITTVYVSHD 193
Cdd:PRK10908 161 ADEPTGNLDDALSEG----ILRLFEEfnrVGVTVLMATHD 196
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
 2-212 3.38e-35

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: 134.89  E-value: 3.38e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   2 ALLTLDRVSVAYDNQ--LILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVNK--RNF 77
Cdd:COG4987  332 PSLELEDVSFRYPGAgrPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDlrRRI 411

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  78 GFVFQSYALFpHLSVFDNvafgLRLRKVKEDDvkRRVMTMLDTVSLGGFEKRFP-------GE----LSGGQRQRVAIAR 146
Cdd:COG4987  412 AVVPQRPHLF-DTTLREN----LRLARPDATD--EELWAALERVGLGDWLAALPdgldtwlGEggrrLSGGERRRLALAR 484

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515998033 147 ALVIEPDLLLFDEPLSNLDANLRvnmrveiRRIQQEL-----GITTVYVSHDQEEcFSISDQVAIMNKGNI 212
Cdd:COG4987  485 ALLRDAPILLLDEPTEGLDAATE-------QALLADLlealaGRTVLLITHRLAG-LERMDRILVLEDGRI 547
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 4-212 4.33e-35

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


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 129.84  E-value: 4.33e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   4 LTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTrvPVNKRNFGFVFQS 83
Cdd:COG4152    2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD--PEDRRRIGYLPEE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  84 YALFPHLSVFDNVAFGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLSN 163
Cdd:COG4152   80 RGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSG 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 515998033 164 LDAnlrVN---MRVEIRRIQQElGITTVYVSHDQEECFSISDQVAIMNKGNI 212
Cdd:COG4152  160 LDP---VNvelLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRK 207
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
 1-212 7.10e-35

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


Pssm-ID: 440752 [Multi-domain]  Cd Length: 240  Bit Score: 127.45  E-value: 7.10e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   1 MALLTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVNKR---NF 77
Cdd:COG1137    1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRarlGI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  78 GFVFQSYALFPHLSVFDNVAFGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLF 157
Cdd:COG1137   81 GYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILL 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 515998033 158 DEPLSNLDAnLRVNmrvEIRRIQQEL---GITTVYVSHDQEECFSISDQVAIMNKGNI 212
Cdd:COG1137  161 DEPFAGVDP-IAVA---DIQKIIRHLkerGIGVLITDHNVRETLGICDRAYIISEGKV 214
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
 11-234 9.68e-35

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 127.65  E-value: 9.68e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  11 VAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTF------LFGDKDYTRV--PVN-KRNFGFVF 81
Cdd:PRK14267  12 VYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARvegevrLFGRNIYSPDvdPIEvRREVGMVF 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  82 QSYALFPHLSVFDNVAFGLRLRKV--KEDDVKRRVMTMLDTVSLGGFEKR----FPGELSGGQRQRVAIARALVIEPDLL 155
Cdd:PRK14267  92 QYPNPFPHLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALWDEVKDrlndYPSNLSGGQRQRLVIARALAMKPKIL 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033 156 LFDEPLSNLDAnlrvnmrVEIRRIQQEL-----GITTVYVSHDQEECFSISDQVAIMNKGNIEQLDAPSTIFKYPTTEFV 230
Cdd:PRK14267 172 LMDEPTANIDP-------VGTAKIEELLfelkkEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELT 244


                 ....
gi 515998033 231 ARFI 234
Cdd:PRK14267 245 EKYV 248
urea_trans_UrtE TIGR03410
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ...
 4-212 1.01e-34

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: 126.87  E-value: 1.01e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033    4 LTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVNKR---NFGFV 80
Cdd:TIGR03410   1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaraGIAYV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   81 FQSYALFPHLSVFDNVAFGLRLRKVKEDDVKRRVMTMLDTvsLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEP 160
Cdd:TIGR03410  81 PQGREIFPRLTVEENLLTGLAALPRRSRKIPDEIYELFPV--LKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEP 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 515998033  161 LSNLDANLRVNMRVEIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNI 212
Cdd:TIGR03410 159 TEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRV 210
L_ocin_972_ABC TIGR03608
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ...
 9-195 1.05e-34

putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]


Pssm-ID: 188353 [Multi-domain]  Cd Length: 206  Bit Score: 126.19  E-value: 1.05e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033    9 VSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVP-VNKRNF-----GFVFQ 82
Cdd:TIGR03608   4 ISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNsKKASKFrreklGYLFQ 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   83 SYALFPHLSVFDNVAFGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLS 162
Cdd:TIGR03608  84 NFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEPTG 163

                         170       180       190
                  ....*....|....*....|....*....|...
gi 515998033  163 NLDANLRvNMRVEIRRIQQELGITTVYVSHDQE 195
Cdd:TIGR03608 164 SLDPKNR-DEVLDLLLELNDEGKTIIIVTHDPE 195
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
 3-223 1.27e-34

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 127.95  E-value: 1.27e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   3 LLTLDRVSVAY--DNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKdytrvPVNKRNF--- 77
Cdd:PRK13648   7 IIVFKNVSFQYqsDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQ-----AITDDNFekl 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  78 ----GFVFQS-YALFPHLSVFDNVAFGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEP 152
Cdd:PRK13648  82 rkhiGIVFQNpDNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNP 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515998033 153 DLLLFDEPLSNLDANLRVNMRVEIRRIQQELGITTVYVSHDQEECFSiSDQVAIMNKGNIEQLDAPSTIFK 223
Cdd:PRK13648 162 SVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFD 231
CeuD COG4604
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ...
 5-193 2.30e-34

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


Pssm-ID: 443654 [Multi-domain]  Cd Length: 252  Bit Score: 126.74  E-value: 2.30e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   5 TLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVNK--RNFGFVFQ 82
Cdd:COG4604    3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRElaKRLAILRQ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  83 SYALFPHLSVFDNVAFGL------RLRKvkEDdvKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLL 156
Cdd:COG4604   83 ENHINSRLTVRELVAFGRfpyskgRLTA--ED--REIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVL 158

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 515998033 157 FDEPLSNLDANLRVNMRVEIRRIQQELGITTVYVSHD 193
Cdd:COG4604  159 LDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHD 195
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
1-225 3.77e-34

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 126.73  E-value: 3.77e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   1 MALLTLDRVSVAYDN---------QLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVP 71
Cdd:PRK10419   1 MTLLNVSGLSHHYAHgglsgkhqhQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  72 VN-----KRNFGFVFQSY--ALFPHLSVFDNVAFGLR-LRKVKEDDVKRRVMTMLDTVSLG-GFEKRFPGELSGGQRQRV 142
Cdd:PRK10419  81 RAqrkafRRDIQMVFQDSisAVNPRKTVREIIREPLRhLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033 143 AIARALVIEPDLLLFDEPLSNLDANLRVNMRVEIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNI--EQLDAPST 220
Cdd:PRK10419 161 CLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIveTQPVGDKL 240


                 ....*
gi 515998033 221 IFKYP 225
Cdd:PRK10419 241 TFSSP 245
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
 23-226 3.54e-33

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 125.59  E-value: 3.54e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  23 DLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVNKR-----NFGFVFQS--YALFPHLSVFDN 95
Cdd:PRK15079  41 TLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWravrsDIQMIFQDplASLNPRMTIGEI 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  96 VAFGLRLR--KVKEDDVKRRVMTMLDTVSL-GGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLSNLDANLR--- 169
Cdd:PRK15079 121 IAEPLRTYhpKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQaqv 200

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 515998033 170 VNMrveIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNIEQLDAPSTIFKYPT 226
Cdd:PRK15079 201 VNL---LQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPL 254
cbiO PRK13640
energy-coupling factor transporter ATPase;
4-226 5.74e-33

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 123.76  E-value: 5.74e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   4 LTLDRVSVAYDN--QLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLeakqgtfLFGDKDYTRVPVN-------- 73
Cdd:PRK13640   6 VEFKHVSFTYPDskKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLL-------LPDDNPNSKITVDgitltakt 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  74 ----KRNFGFVFQSY-ALFPHLSVFDNVAFGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARAL 148
Cdd:PRK13640  79 vwdiREKVGIVFQNPdNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGIL 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515998033 149 VIEPDLLLFDEPLSNLDANLRVNMRVEIRRIQQELGITTVYVSHDQEECfSISDQVAIMNKGNIEQLDAPSTIFKYPT 226
Cdd:PRK13640 159 AVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKVE 235
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
12-196 1.31e-32

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 120.03  E-value: 1.31e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  12 AYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFlfgdkdyTRVPvnKRNFGFVFQSYAL---FP 88
Cdd:NF040873   1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV-------RRAG--GARVAYVPQRSEVpdsLP 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  89 hLSVFDNVAFGL-----RLRKVKEDDvKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLSN 163
Cdd:NF040873  72 -LTVRDLVAMGRwarrgLWRRLTRDD-RAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTG 149

                        170       180       190
                 ....*....|....*....|....*....|...
gi 515998033 164 LDANLRVNMRVEIRRIQQElGITTVYVSHDQEE 196
Cdd:NF040873 150 LDAESRERIIALLAEEHAR-GATVVVVTHDLEL 181
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
13-234 2.74e-32

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 121.23  E-value: 2.74e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  13 YDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIaGFLEA-KQGTFLFGDKDYTRVPVN---------------KRN 76
Cdd:PRK10619  15 YGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCI-NFLEKpSEGSIVVNGQTINLVRDKdgqlkvadknqlrllRTR 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  77 FGFVFQSYALFPHLSVFDNVAFG-LRLRKVKEDDVKRRVMTMLDTVSLGGFEK-RFPGELSGGQRQRVAIARALVIEPDL 154
Cdd:PRK10619  94 LTMVFQHFNLWSHMTVLENVMEApIQVLGLSKQEARERAVKYLAKVGIDERAQgKYPVHLSGGQQQRVSIARALAMEPEV 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033 155 LLFDEPLSNLDANLrvnmRVEIRRIQQEL---GITTVYVSHDQEECFSISDQVAIMNKGNIEQLDAPSTIFKYPTTEFVA 231
Cdd:PRK10619 174 LLFDEPTSALDPEL----VGEVLRIMQQLaeeGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRLQ 249


                 ...
gi 515998033 232 RFI 234
Cdd:PRK10619 250 QFL 252
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
 18-210 7.35e-32

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: 118.92  E-value: 7.35e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  18 ILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVNKrnFGFVFQSYALFPHLSVFDNVA 97
Cdd:cd03269   15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNR--IGYLPEERGLYPKMKVIDQLV 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  98 FGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLSNLD-ANLRVnMRVEI 176
Cdd:cd03269   93 YLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDpVNVEL-LKDVI 171

                        170       180       190
                 ....*....|....*....|....*....|....
gi 515998033 177 RRiQQELGITTVYVSHDQEECFSISDQVAIMNKG 210
Cdd:cd03269  172 RE-LARAGKTVILSTHQMELVEELCDRVLLLNKG 204
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
 6-223 9.00e-32

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 120.48  E-value: 9.00e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   6 LDRVSVAYDN--QLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGT-FLFGdKDYTRVPVNK-RNF-GFV 80
Cdd:PRK13632  10 VENVSFSYPNseNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEiKIDG-ITISKENLKEiRKKiGII 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  81 FQSY-ALFPHLSVFDNVAFGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDE 159
Cdd:PRK13632  89 FQNPdNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDE 168

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515998033 160 PLSNLDANLRVNMRVEIRRIQQELGITTVYVSHDQEECFsISDQVAIMNKGNIEQLDAPSTIFK 223
Cdd:PRK13632 169 STSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEILN 231
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
 23-221 1.17e-31

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: 124.53  E-value: 1.17e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   23 DLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGT--FLFGDK--DYTRVPVN-----KRNFGFVFQSYALFPHLSVF 93
Cdd:TIGR03269 304 SLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnVRVGDEwvDMTKPGPDgrgraKRYIGILHQEYDLYPHRTVL 383

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   94 DNV--AFGLRLRKvkeDDVKRRVMTMLDTVslgGFEK--------RFPGELSGGQRQRVAIARALVIEPDLLLFDEPLSN 163
Cdd:TIGR03269 384 DNLteAIGLELPD---ELARMKAVITLKMV---GFDEekaeeildKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGT 457

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 515998033  164 LDANLRVNMRVEIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNIEQLDAPSTI 221
Cdd:TIGR03269 458 MDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEI 515
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
 1-234 1.30e-31

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 119.25  E-value: 1.30e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   1 MALLTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLR----LIAGFLEAK-QGTFLFGDKDYTRVPVN-- 73
Cdd:PRK14247   1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRvfnrLIELYPEARvSGEVYLDGQDIFKMDVIel 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  74 KRNFGFVFQSYALFPHLSVFDNVAFGLRL-RKVK-EDDVKRRVMTMLDTVSL-GGFEKRF---PGELSGGQRQRVAIARA 147
Cdd:PRK14247  81 RRRVQMVFQIPNPIPNLSIFENVALGLKLnRLVKsKKELQERVRWALEKAQLwDEVKDRLdapAGKLSGGQQQRLCIARA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033 148 LVIEPDLLLFDEPLSNLDANLRVNMRVEIRRIQQELGIttVYVSHDQEECFSISDQVAIMNKGNIEQLDAPSTIFKYPTT 227
Cdd:PRK14247 161 LAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTI--VLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRH 238


                 ....*..
gi 515998033 228 EFVARFI 234
Cdd:PRK14247 239 ELTEKYV 245
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
 4-212 2.22e-31

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: 117.69  E-value: 2.22e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   4 LTLDRVSVAYDNQLI--LQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVN--KRNFGF 79
Cdd:cd03245    3 IEFRNVSFSYPNQEIpaLDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPAdlRRNIGY 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  80 VFQSYALFpHLSVFDNVAFGLRLrkvkEDDvkRRVMTMLDTVSLGGFEKRFP-------GE----LSGGQRQRVAIARAL 148
Cdd:cd03245   83 VPQDVTLF-YGTLRDNITLGAPL----ADD--ERILRAAELAGVTDFVNKHPngldlqiGErgrgLSGGQRQAVALARAL 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515998033 149 VIEPDLLLFDEPLSNLDanLRVNMRVeIRRIQQEL-GITTVYVSHDQeECFSISDQVAIMNKGNI 212
Cdd:cd03245  156 LNDPPILLLDEPTSAMD--MNSEERL-KERLRQLLgDKTLIIITHRP-SLLDLVDRIIVMDSGRI 216
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
 3-234 3.87e-31

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 118.23  E-value: 3.87e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   3 LLTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLE------AKQGTFLFGDKDYTRVPVNK-- 74
Cdd:PRK14246  10 VFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIKlr 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  75 RNFGFVFQSYALFPHLSVFDNVAFGLRLRKVKED-DVKRRVMTMLDTVSL-GGFEKRF---PGELSGGQRQRVAIARALV 149
Cdd:PRK14246  90 KEVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKEKrEIKKIVEECLRKVGLwKEVYDRLnspASQLSGGQQQRLTIARALA 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033 150 IEPDLLLFDEPLSNLDANLRVNMRVEIRRIQQElgITTVYVSHDQEECFSISDQVAIMNKGNIEQLDAPSTIFKYPTTEF 229
Cdd:PRK14246 170 LKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNEL 247


                 ....*
gi 515998033 230 VARFI 234
Cdd:PRK14246 248 TEKYV 252
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
 2-196 4.21e-31

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 117.12  E-value: 4.21e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   2 ALLTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVP--VNKRNFGF 79
Cdd:PRK10247   6 PLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKpeIYRQQVSY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  80 VFQSYALFPHlSVFDNVAFGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFpGELSGGQRQRVAIARALVIEPDLLLFDE 159
Cdd:PRK10247  86 CAQTPTLFGD-TVYDNLIFPWQIRNQQPDPAIFLDDLERFALPDTILTKNI-AELSGGEKQRISLIRNLQFMPKVLLLDE 163

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 515998033 160 PLSNLDANLRVNMRVEIRRIQQELGITTVYVSHDQEE 196
Cdd:PRK10247 164 ITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE 200
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
 14-227 6.50e-31

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 118.26  E-value: 6.50e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  14 DNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDK--DYTRVPVNK--RNFGFVFQSY--ALF 87
Cdd:PRK13639  13 DGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEpiKYDKKSLLEvrKTVGIVFQNPddQLF 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  88 PHlSVFDNVAFGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLSNLDAn 167
Cdd:PRK13639  93 AP-TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDP- 170

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515998033 168 lrvNMRVEIRRIQQEL---GITTVYVSHDQEECFSISDQVAIMNKGNIEQLDAPSTIFKYPTT 227
Cdd:PRK13639 171 ---MGASQIMKLLYDLnkeGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIET 230
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
 16-226 9.06e-31

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 118.20  E-value: 9.06e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  16 QLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVNK------RNFGFVFQsyalFPH 89
Cdd:PRK13634  20 RRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKklkplrKKVGIVFQ----FPE 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  90 LSVFD-----NVAFGLRLRKVKEDDVKRRVMTMLDTVSLGgfEK---RFPGELSGGQRQRVAIARALVIEPDLLLFDEPL 161
Cdd:PRK13634  96 HQLFEetvekDICFGPMNFGVSEEDAKQKAREMIELVGLP--EEllaRSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPT 173

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515998033 162 SNLDANLRVNMRVEIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNIEQLDAPSTIFKYPT 226
Cdd:PRK13634 174 AGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
 1-222 9.75e-31

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 116.92  E-value: 9.75e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   1 MALLTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVN---KRNF 77
Cdd:PRK10895   1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHaraRRGI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  78 GFVFQSYALFPHLSVFDNVAFGLRLRK-VKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLL 156
Cdd:PRK10895  81 GYLPQEASIFRRLSVYDNLMAVLQIRDdLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFIL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515998033 157 FDEPLSNLDAnLRVnmrVEIRRIQQEL---GITTVYVSHDQEECFSISDQVAIMNKGNIEQLDAPSTIF 222
Cdd:PRK10895 161 LDEPFAGVDP-ISV---IDIKRIIEHLrdsGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEIL 225
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
1-207 2.42e-30

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 120.51  E-value: 2.42e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   1 MALLTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYT-RVPVNKRNFG- 78
Cdd:COG1129    2 EPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRfRSPRDAQAAGi 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  79 -FVFQSYALFPHLSVFDNVAFGLRLRK---VKEDDVKRRVMTMLDTVSLggfekRFP-----GELSGGQRQRVAIARALV 149
Cdd:COG1129   82 aIIHQELNLVPNLSVAENIFLGREPRRgglIDWRAMRRRARELLARLGL-----DIDpdtpvGDLSVAQQQLVEIARALS 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515998033 150 IEPDLLLFDEPLSNLDAN-----LRVnmrveIRRIQQElGITTVYVSHDQEECFSISDQVAIM 207
Cdd:COG1129  157 RDARVLILDEPTASLTEReverlFRI-----IRRLKAQ-GVAIIYISHRLDEVFEIADRVTVL 213
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
3-214 3.14e-30

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 115.30  E-value: 3.14e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   3 LLTLDRVSVAY-DNQL---ILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYT------RVPV 72
Cdd:PRK11629   5 LLQCDNLCKRYqEGSVqtdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSklssaaKAEL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  73 NKRNFGFVFQSYALFPHLSVFDNVAFGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEP 152
Cdd:PRK11629  85 RNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNP 164

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515998033 153 DLLLFDEPLSNLD---ANLRVNMRVEIRRIQqelGITTVYVSHDQEECFSISDQVAiMNKGNIEQ 214
Cdd:PRK11629 165 RLVLADEPTGNLDarnADSIFQLLGELNRLQ---GTAFLVVTHDLQLAKRMSRQLE-MRDGRLTA 225
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
4-222 3.19e-30

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 115.88  E-value: 3.19e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   4 LTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVNKrnfgfVFQS 83
Cdd:PRK11231   3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQ-----LARR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  84 YALFP--HL-----SVFDNVAFG----LRL-RKVKEDDVKRRVMTMLDTvSLGGFEKRFPGELSGGQRQRVAIARALVIE 151
Cdd:PRK11231  78 LALLPqhHLtpegiTVRELVAYGrspwLSLwGRLSAEDNARVNQAMEQT-RINHLADRRLTDLSGGQRQRAFLAMVLAQD 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515998033 152 PDLLLFDEPLSNLDANLRVNMRVEIRRIQQElGITTVYVSHDQEECFSISDQVAIMNKGNIEQLDAPSTIF 222
Cdd:PRK11231 157 TPVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVM 226
LPS_export_lptB TIGR04406
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ...
 4-212 3.81e-30

LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]


Pssm-ID: 275199 [Multi-domain]  Cd Length: 239  Bit Score: 115.06  E-value: 3.81e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033    4 LTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVNKR---NFGFV 80
Cdd:TIGR04406   2 LVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERarlGIGYL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   81 FQSYALFPHLSVFDNVAFGLRLRK-VKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDE 159
Cdd:TIGR04406  82 PQEASIFRKLTVEENIMAVLEIRKdLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDE 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 515998033  160 PLSNLDAnLRVNMRVEIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNI 212
Cdd:TIGR04406 162 PFAGVDP-IAVGDIKKIIKHLKERGIGVLITDHNVRETLDICDRAYIISDGKV 213
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
 3-229 4.46e-30

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 120.20  E-value: 4.46e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   3 LLTLDRVSVAY-----------DNQLILQDFDLQLERGQLLSLLGPSGCGKTTT----LRLIAGfleakQGTFLFGDK-- 65
Cdd:PRK15134 275 LLDVEQLQVAFpirkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTTglalLRLINS-----QGEIWFDGQpl 349

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  66 -DYTR---VPVnKRNFGFVFQ--SYALFPHLSVFDNVAFGLRL--RKVKEDDVKRRVMTMLDTVSLGGFEK-RFPGELSG 136
Cdd:PRK15134 350 hNLNRrqlLPV-RHRIQVVFQdpNSSLNPRLNVLQIIEEGLRVhqPTLSAAQREQQVIAVMEEVGLDPETRhRYPAEFSG 428

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033 137 GQRQRVAIARALVIEPDLLLFDEPLSNLDANLRVNMRVEIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGN-IEQL 215
Cdd:PRK15134 429 GQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEvVEQG 508

                        250
                 ....*....|....
gi 515998033 216 DApSTIFKYPTTEF 229
Cdd:PRK15134 509 DC-ERVFAAPQQEY 521
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
 4-230 7.92e-30

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 114.75  E-value: 7.92e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   4 LTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLI------AGFLEAKQGTFLFGDKDYTR-VPVNK-- 74
Cdd:PRK14258   8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLnrmnelESEVRVEGRVEFFNQNIYERrVNLNRlr 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  75 RNFGFVFQSYALFPhLSVFDNVAFGLRL----RKVKEDDVkrrVMTMLDTVSLGGFEK----RFPGELSGGQRQRVAIAR 146
Cdd:PRK14258  88 RQVSMVHPKPNLFP-MSVYDNVAYGVKIvgwrPKLEIDDI---VESALKDADLWDEIKhkihKSALDLSGGQQQRLCIAR 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033 147 ALVIEPDLLLFDEPLSNLD--ANLRVNMRVEIRRIQQELgiTTVYVSHDQEECFSISDQVAIM--NKGNIEQL---DAPS 219
Cdd:PRK14258 164 ALAVKPKVLLMDEPCFGLDpiASMKVESLIQSLRLRSEL--TMVIVSHNLHQVSRLSDFTAFFkgNENRIGQLvefGLTK 241

                        250
                 ....*....|....*
gi 515998033 220 TIFKYP----TTEFV 230
Cdd:PRK14258 242 KIFNSPhdsrTREYV 256
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
 3-233 9.90e-30

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 114.88  E-value: 9.90e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   3 LLTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLR-------LIAGFleAKQGTFLFGDKDYTRVPVN-- 73
Cdd:PRK14243  10 VLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGF--RVEGKVTFHGKNLYAPDVDpv 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  74 --KRNFGFVFQSYALFPHlSVFDNVAFGLRLRKVKED-D--VKR--RVMTMLDTVSlggfEK-RFPG-ELSGGQRQRVAI 144
Cdd:PRK14243  88 evRRRIGMVFQKPNPFPK-SIYDNIAYGARINGYKGDmDelVERslRQAALWDEVK----DKlKQSGlSLSGGQQQRLCI 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033 145 ARALVIEPDLLLFDEPLSNLD--ANLRvnmrveIRRIQQELG--ITTVYVSHDQEECFSISDQVAIMN---------KGN 211
Cdd:PRK14243 163 ARAIAVQPEVILMDEPCSALDpiSTLR------IEELMHELKeqYTIIIVTHNMQQAARVSDMTAFFNveltegggrYGY 236

                        250       260
                 ....*....|....*....|....*..
gi 515998033 212 IEQLDAPSTIFKYP----TTEFVA-RF 233
Cdd:PRK14243 237 LVEFDRTEKIFNSPqqqaTRDYVSgRF 263
cbiO PRK13643
energy-coupling factor transporter ATPase;
19-223 1.15e-29

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 115.22  E-value: 1.15e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  19 LQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRV-------PVNKRnFGFVFQsyalFPHLS 91
Cdd:PRK13643  22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTskqkeikPVRKK-VGVVFQ----FPESQ 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  92 VFD-----NVAFGLRLRKVKEDDVKRRVMTMLDTVSLGG-FEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLSNLD 165
Cdd:PRK13643  97 LFEetvlkDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADeFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLD 176

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 515998033 166 ANLRVNMRVEIRRIQQElGITTVYVSHDQEECFSISDQVAIMNKGNIEQLDAPSTIFK 223
Cdd:PRK13643 177 PKARIEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQ 233
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
 1-214 1.25e-29

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: 119.02  E-value: 1.25e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   1 MALLTLDRVSVAYDN----QLILQDFDLQLERGQLLSLLGPSGCGKTTT----LRLIAGFLEAKQGTFLFGDKDYTRVP- 71
Cdd:COG4172    4 MPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSVTalsiLRLLPDPAAHPSGSILFDGQDLLGLSe 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  72 -----VNKRNFGFVFQ--SYALFPHLSVFDNVAFGLRL-RKVKEDDVKRRVMTMLDTVSLGGFEKR---FPGELSGGQRQ 140
Cdd:COG4172   84 relrrIRGNRIAMIFQepMTSLNPLHTIGKQIAEVLRLhRGLSGAAARARALELLERVGIPDPERRldaYPHQLSGGQRQ 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033 141 RVAIARALVIEPDLLLFDEPLSNLDanlrVNMRVEI----RRIQQELGITTVYVSHDqeecFSI----SDQVAIMNKGNI 212
Cdd:COG4172  164 RVMIAMALANEPDLLIADEPTTALD----VTVQAQIldllKDLQRELGMALLLITHD----LGVvrrfADRVAVMRQGEI 235


                 ...
gi 515998033 213 -EQ 214
Cdd:COG4172  236 vEQ 238
COG4559 COG4559
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
3-232 1.49e-29

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


Pssm-ID: 443620 [Multi-domain]  Cd Length: 258  Bit Score: 114.06  E-value: 1.49e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   3 LLTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVNK--RNFGFV 80
Cdd:COG4559    1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWElaRRRAVL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  81 FQSYAL-FPhLSVFDNVAFGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARAL--VIEPD---- 153
Cdd:COG4559   81 PQHSSLaFP-FTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLaqLWEPVdggp 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033 154 -LLLFDEPLSNLDAN--LRVnMRVeIRRIQQElGITTVYVSHD-----QeecfsISDQVAIMNKGNIEQLDAPSTIFkyp 225
Cdd:COG4559  160 rWLFLDEPTSALDLAhqHAV-LRL-ARQLARR-GGGVVAVLHDlnlaaQ-----YADRILLLHQGRLVAQGTPEEVL--- 228


                 ....*..
gi 515998033 226 TTEFVAR 232
Cdd:COG4559  229 TDELLER 235
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
13-222 1.95e-29

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 113.95  E-value: 1.95e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  13 YDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDK--DYTR--VPVNKRNFGFVFQSyalfP 88
Cdd:PRK13638  11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKrgLLALRQQVATVFQD----P 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  89 HLSVF-----DNVAFGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLSN 163
Cdd:PRK13638  87 EQQIFytdidSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAG 166

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 515998033 164 LDANLRVNMRVEIRRIQQElGITTVYVSHDQEECFSISDQVAIMNKGNIEQLDAPSTIF 222
Cdd:PRK13638 167 LDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
 14-195 2.58e-29

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 112.56  E-value: 2.58e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  14 DNQL-ILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQG-TFLFGD-----KDYTRVPVNKRNFGFVFQSYAL 86
Cdd:PRK10584  20 EHELsILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGeVSLVGQplhqmDEEARAKLRAKHVGFVFQSFML 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  87 FPHLSVFDNVAFGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLSNLDA 166
Cdd:PRK10584 100 IPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDR 179

                        170       180
                 ....*....|....*....|....*....
gi 515998033 167 NLRVNMRVEIRRIQQELGITTVYVSHDQE 195
Cdd:PRK10584 180 QTGDKIADLLFSLNREHGTTLILVTHDLQ 208
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
 22-225 2.99e-29

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 118.42  E-value: 2.99e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  22 FDLQleRGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVNK-----RNFGFVFQS-YA-LFPHLSVFD 94
Cdd:PRK10261 345 FDLW--PGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKlqalrRDIQFIFQDpYAsLDPRQTVGD 422

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  95 NVAFGLRLRKVKE-DDVKRRVMTMLDTVSLGGFEK-RFPGELSGGQRQRVAIARALVIEPDLLLFDEPLSNLDANLRVNM 172
Cdd:PRK10261 423 SIMEPLRVHGLLPgKAAAARVAWLLERVGLLPEHAwRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQI 502

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 515998033 173 RVEIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNIEQLDAPSTIFKYP 225
Cdd:PRK10261 503 INLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENP 555
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
 4-195 3.07e-29

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: 117.77  E-value: 3.07e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033    4 LTLDRVSVAY-DNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVN--KRNFGFV 80
Cdd:TIGR02857 322 LEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADswRDQIAWV 401

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   81 FQSYALFPHlSVFDNVAFGLRlrKVKEDDVKRrvmtMLDTVSLGGFEKRFP-------GE----LSGGQRQRVAIARALV 149
Cdd:TIGR02857 402 PQHPFLFAG-TIAENIRLARP--DASDAEIRE----ALERAGLDEFVAALPqgldtpiGEggagLSGGQAQRLALARAFL 474

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 515998033  150 IEPDLLLFDEPLSNLDANLRVNMRVEIRRIQQelGITTVYVSHDQE 195
Cdd:TIGR02857 475 RDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLA 518
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
 4-210 6.51e-29

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


Pssm-ID: 213183 [Multi-domain]  Cd Length: 163  Bit Score: 109.44  E-value: 6.51e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   4 LTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRV-PVNKRNFG--FV 80
Cdd:cd03216    1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFAsPRDARRAGiaMV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  81 FQsyalfphlsvfdnvafglrlrkvkeddvkrrvmtmldtvslggfekrfpgeLSGGQRQRVAIARALVIEPDLLLFDEP 160
Cdd:cd03216   81 YQ---------------------------------------------------LSVGERQMVEIARALARNARLLILDEP 109

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 515998033 161 LSNLDANLRVNMRVEIRRIQQElGITTVYVSHDQEECFSISDQVAIMNKG 210
Cdd:cd03216  110 TAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDG 158
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
 4-193 1.25e-28

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: 115.92  E-value: 1.25e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033    4 LTLDRVSVAY-DNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVN--KRNFGFV 80
Cdd:TIGR02868 335 LELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDevRRRVSVC 414

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   81 FQSYALFpHLSVFDNVAFGLR----------LRKVKEDDVKRRVMTMLDTVsLGGFEKRfpgeLSGGQRQRVAIARALVI 150
Cdd:TIGR02868 415 AQDAHLF-DTTVRENLRLARPdatdeelwaaLERVGLADWLRALPDGLDTV-LGEGGAR----LSGGERQRLALARALLA 488

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 515998033  151 EPDLLLFDEPLSNLDANLRVNMRVEIRRIQQELgiTTVYVSHD 193
Cdd:TIGR02868 489 DAPILLLDEPTEHLDAETADELLEDLLAALSGR--TVVLITHH 529
anch_rpt_ABC TIGR03771
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ...
 24-208 3.65e-28

anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]


Pssm-ID: 163483 [Multi-domain]  Cd Length: 223  Bit Score: 109.56  E-value: 3.65e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   24 LQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRvpvNKRNFGFVFQSYAL---FPhLSVFDNVAFGL 100
Cdd:TIGR03771   1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPGK---GWRHIGYVPQRHEFawdFP-ISVAHTVMSGR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  101 R-----LRKVKEDDVkRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLSNLDaNLRVNMRVE 175
Cdd:TIGR03771  77 TghigwLRRPCVADF-AAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLD-MPTQELLTE 154

                         170       180       190
                  ....*....|....*....|....*....|...
gi 515998033  176 IRRIQQELGITTVYVSHDQEECFSISDQVAIMN 208
Cdd:TIGR03771 155 LFIELAGAGTAILMTTHDLAQAMATCDRVVLLN 187
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
 2-220 3.96e-28

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 110.25  E-value: 3.96e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   2 ALLTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVNK--RNFGF 79
Cdd:PRK13548   1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElaRRRAV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  80 VFQSYAL-FPhLSVFDNVAFGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALV------IEP 152
Cdd:PRK13548  81 LPQHSSLsFP-FTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPP 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515998033 153 DLLLFDEPLSNLDanLR---VNMRVeIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNIEQLDAPST 220
Cdd:PRK13548 160 RWLLLDEPTSALD--LAhqhHVLRL-ARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAE 227
cbiO PRK13642
energy-coupling factor transporter ATPase;
19-222 1.04e-27

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 109.80  E-value: 1.04e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  19 LQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPV--NKRNFGFVFQSY-ALFPHLSVFDN 95
Cdd:PRK13642  23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVwnLRRKIGMVFQNPdNQFVGATVEDD 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  96 VAFGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLSNLDANLRVNMRVE 175
Cdd:PRK13642 103 VAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRV 182

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 515998033 176 IRRIQQELGITTVYVSHDQEECFSiSDQVAIMNKGNIEQLDAPSTIF 222
Cdd:PRK13642 183 IHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
SapF COG4167
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
26-234 1.07e-27

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


Pssm-ID: 443328 [Multi-domain]  Cd Length: 265  Bit Score: 109.16  E-value: 1.07e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  26 LERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKdytrvPVNKRNFGF-------VFQ--SYALFPHLSVFDNV 96
Cdd:COG4167   36 LEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGH-----KLEYGDYKYrckhirmIFQdpNTSLNPRLNIGQIL 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  97 AFGLRLR-KVKEDDVKRRVMTMLDTVSLGGFEKRF-PGELSGGQRQRVAIARALVIEPDLLLFDEPLSNLDANLR---VN 171
Cdd:COG4167  111 EEPLRLNtDLTAEEREERIFATLRLVGLLPEHANFyPHMLSSGQKQRVALARALILQPKIIIADEALAALDMSVRsqiIN 190

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515998033 172 MRVEirrIQQELGITTVYVSHDQEECFSISDQVAIMNKGNIEQLDAPSTIFKYPTTEFVARFI 234
Cdd:COG4167  191 LMLE---LQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVFANPQHEVTKRLI 250
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
 19-212 1.64e-27

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: 107.80  E-value: 1.64e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  19 LQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKD-YTRVPVNKRNFGFVF-QSYALFPHLSVFDNV 96
Cdd:cd03267   37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVpWKRRKKFLRRIGVVFgQKTQLWWDLPVIDSF 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  97 AFGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLSNLDANLRVNMRVEI 176
Cdd:cd03267  117 YLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFL 196

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 515998033 177 RRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNI 212
Cdd:cd03267  197 KEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
type_I_sec_LssB TIGR03375
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ...
 6-212 1.77e-27

type I secretion system ATPase, LssB 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. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]


Pssm-ID: 274550 [Multi-domain]  Cd Length: 694  Bit Score: 113.42  E-value: 1.77e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033    6 LDRVSVAYDNQLI--LQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVN--KRNFGFVF 81
Cdd:TIGR03375 466 FRNVSFAYPGQETpaLDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPAdlRRNIGYVP 545

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   82 QSYALFpHLSVFDNVAFGLRLrkvkEDDvkRRVMTMLDTVSLGGFEKRFP-------GE----LSGGQRQRVAIARALVI 150
Cdd:TIGR03375 546 QDPRLF-YGTLRDNIALGAPY----ADD--EEILRAAELAGVTEFVRRHPdgldmqiGErgrsLSGGQRQAVALARALLR 618

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515998033  151 EPDLLLFDEPLSNLDANLRvnMRVeIRRIQQEL-GITTVYVSHDQeECFSISDQVAIMNKGNI 212
Cdd:TIGR03375 619 DPPILLLDEPTSAMDNRSE--ERF-KDRLKRWLaGKTLVLVTHRT-SLLDLVDRIIVMDNGRI 677
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
 4-212 1.95e-27

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: 105.76  E-value: 1.95e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   4 LTLDRVSVAY--DNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRV-PVNKR-NFGF 79
Cdd:cd03246    1 LEVENVSFRYpgAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWdPNELGdHVGY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  80 VFQSYALFPHlSVFDNVafglrlrkvkeddvkrrvmtmldtvslggfekrfpgeLSGGQRQRVAIARALVIEPDLLLFDE 159
Cdd:cd03246   81 LPQDDELFSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDE 122

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 515998033 160 PLSNLD-ANLRVNMRVeIRRIqQELGITTVYVSHdQEECFSISDQVAIMNKGNI 212
Cdd:cd03246  123 PNSHLDvEGERALNQA-IAAL-KAAGATRIVIAH-RPETLASADRILVLEDGRV 173
cbiO PRK13644
energy-coupling factor transporter ATPase;
3-230 2.14e-27

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 108.54  E-value: 2.14e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   3 LLTLDRVSVAY-DNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFL---FGDKDYTRVPVNKRNFG 78
Cdd:PRK13644   1 MIRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLvsgIDTGDFSKLQGIRKLVG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  79 FVFQS-YALFPHLSVFDNVAFGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLF 157
Cdd:PRK13644  81 IVFQNpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIF 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515998033 158 DEPLSNLDANLRVNMRVEIRRIQQElGITTVYVSHDQEEcFSISDQVAIMNKGNIEQLDAPSTIFKYPTTEFV 230
Cdd:PRK13644 161 DEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDVSLQTL 231
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
 17-212 2.49e-27

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: 107.36  E-value: 2.49e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  17 LILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLE---AKQGTFLFGDKDYTRVPVnKRNFGFVFQSYALFPHLSVF 93
Cdd:cd03234   21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFNGQPRKPDQF-QKCVAYVRQDDILLPGLTVR 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  94 DNVAFGLRLR---------KVKEDDVKRrvMTMLDTVSLGGfeKRFPGeLSGGQRQRVAIARALVIEPDLLLFDEPLSNL 164
Cdd:cd03234  100 ETLTYTAILRlprkssdaiRKKRVEDVL--LRDLALTRIGG--NLVKG-ISGGERRRVSIAVQLLWDPKVLILDEPTSGL 174

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 515998033 165 DANLRVNMRVEIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNI 212
Cdd:cd03234  175 DSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEI 222
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
 19-222 3.61e-27

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 108.40  E-value: 3.61e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  19 LQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDK--DYTRVPVNK--RNFGFVFQS--YALFPhLSV 92
Cdd:PRK13636  22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMKlrESVGMVFQDpdNQLFS-ASV 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  93 FDNVAFGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLSNLDANLRVNM 172
Cdd:PRK13636 101 YQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEI 180

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 515998033 173 RVEIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNIEQLDAPSTIF 222
Cdd:PRK13636 181 MKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
 5-192 3.96e-27

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: 106.85  E-value: 3.96e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   5 TLDRVSVAYD---NQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVN--KRNFGF 79
Cdd:cd03249    2 EFKNVSFRYPsrpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRwlRSQIGL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  80 VFQSYALFPhLSVFDNVAFGLRLRKVKEDDVKRRVMTMLDTV-SL-GGFEKRFpGE----LSGGQRQRVAIARALVIEPD 153
Cdd:cd03249   82 VSQEPVLFD-GTIAENIRYGKPDATDEEVEEAAKKANIHDFImSLpDGYDTLV-GErgsqLSGGQKQRIAIARALLRNPK 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 515998033 154 LLLFDEPLSNLDANlrvnmrVEiRRIQQEL-----GITTVYVSH 192
Cdd:cd03249  160 ILLLDEATSALDAE------SE-KLVQEALdramkGRTTIVIAH 196
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
 4-212 4.27e-27

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: 106.93  E-value: 4.27e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   4 LTLDRVSVAYD-NQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVN--KRNFGFV 80
Cdd:cd03253    1 IEFENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDslRRAIGVV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  81 FQSYALFpHLSVFDNVAFGlRLRKVKED--------DVKRRVMTMLDtvslgGFEKRFpGE----LSGGQRQRVAIARAL 148
Cdd:cd03253   81 PQDTVLF-NDTIGYNIRYG-RPDATDEEvieaakaaQIHDKIMRFPD-----GYDTIV-GErglkLSGGEKQRVAIARAI 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515998033 149 VIEPDLLLFDEPLSNLDANLRvnmrveiRRIQQEL-----GITTVYVSHDQEECFSiSDQVAIMNKGNI 212
Cdd:cd03253  153 LKNPPILLLDEATSALDTHTE-------REIQAALrdvskGRTTIVIAHRLSTIVN-ADKIIVLKDGRI 213
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
 4-165 4.34e-27

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: 106.93  E-value: 4.34e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   4 LTLDRVSVAY--DNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVN--KRNFGF 79
Cdd:cd03251    1 VEFKNVTFRYpgDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLAslRRQIGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  80 VFQSYALFpHLSVFDNVAFGlrlrkvKEDDVKRRVMTMLDTVSLGGFEKRFP-------GE----LSGGQRQRVAIARAL 148
Cdd:cd03251   81 VSQDVFLF-NDTVAENIAYG------RPGATREEVEEAARAANAHEFIMELPegydtviGErgvkLSGGQRQRIAIARAL 153

                        170
                 ....*....|....*..
gi 515998033 149 VIEPDLLLFDEPLSNLD 165
Cdd:cd03251  154 LKDPPILILDEATSALD 170
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
 4-214 5.16e-27

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: 111.76  E-value: 5.16e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   4 LTLDRVSVAY--DNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVNK--RNFGF 79
Cdd:COG4618  331 LSVENLTVVPpgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREElgRHIGY 410

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  80 VFQSYALFPHlSVFDNVAfglRLRKVKEDDVKR-----RVMTMLdtVSL-GGFEKRfPGE----LSGGQRQRVAIARALV 149
Cdd:COG4618  411 LPQDVELFDG-TIAENIA---RFGDADPEKVVAaaklaGVHEMI--LRLpDGYDTR-IGEggarLSGGQRQRIGLARALY 483

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515998033 150 IEPDLLLFDEPLSNLDANLRVNMRVEIRRIQQElGITTVYVSHDQeECFSISDQVAIMNKGNIEQ 214
Cdd:COG4618  484 GDPRLVVLDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHRP-SLLAAVDKLLVLRDGRVQA 546
NHLM_micro_ABC2 TIGR03797
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ...
 4-165 8.77e-27

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: 111.20  E-value: 8.77e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033    4 LTLDRVSVAY--DNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVN--KRNFGF 79
Cdd:TIGR03797 452 IEVDRVTFRYrpDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQavRRQLGV 531

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   80 VFQSYALFPHlSVFDNVAFGLRL---------RKVK-EDDVKRRVMTMLDTVSLGGfekrfpGELSGGQRQRVAIARALV 149
Cdd:TIGR03797 532 VLQNGRLMSG-SIFENIAGGAPLtldeaweaaRMAGlAEDIRAMPMGMHTVISEGG------GTLSGGQRQRLLIARALV 604

                         170
                  ....*....|....*.
gi 515998033  150 IEPDLLLFDEPLSNLD 165
Cdd:TIGR03797 605 RKPRILLFDEATSALD 620
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
 18-222 1.53e-26

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 107.24  E-value: 1.53e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  18 ILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGT-----FLFGDKDYTRVPVN-------------KRNFGF 79
Cdd:PRK13631  41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTiqvgdIYIGDKKNNHELITnpyskkiknfkelRRRVSM 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  80 VFQ--SYALFPHlSVFDNVAFGLRLRKVKEDDVKRRVMTMLDTVSLG-GFEKRFPGELSGGQRQRVAIARALVIEPDLLL 156
Cdd:PRK13631 121 VFQfpEYQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDdSYLERSPFGLSGGQKRRVAIAGILAIQPEILI 199

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515998033 157 FDEPLSNLDANLRVNMRVEIRRIQQElGITTVYVSHDQEECFSISDQVAIMNKGNIEQLDAPSTIF 222
Cdd:PRK13631 200 FDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIF 264
cbiO PRK13645
energy-coupling factor transporter ATPase;
4-222 2.32e-26

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 106.25  E-value: 2.32e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   4 LTLDRVSVAYDNQL-----ILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGD-------KDYTRVP 71
Cdd:PRK13645   7 IILDNVSYTYAKKTpfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipanlKKIKEVK 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  72 VNKRNFGFVFQ--SYALFPHlSVFDNVAFGLRLRKVKEDDVKRRVMTMLDTVSLG-GFEKRFPGELSGGQRQRVAIARAL 148
Cdd:PRK13645  87 RLRKEIGLVFQfpEYQLFQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPeDYVKRSPFELSGGQKRRVALAGII 165

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515998033 149 VIEPDLLLFDEPLSNLDANLRVNMRVEIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNIEQLDAPSTIF 222
Cdd:PRK13645 166 AMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIF 239
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
 18-212 3.03e-26

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: 103.40  E-value: 3.03e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  18 ILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFL--EAKQGTFLFGDKdytrvPVNKRNF----GFVFQSYALFPHLS 91
Cdd:cd03213   24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRtgLGVSGEVLINGR-----PLDKRSFrkiiGYVPQDDILHPTLT 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  92 VFDNVAFGLRLRKvkeddvkrrvmtmldtvslggfekrfpgeLSGGQRQRVAIARALVIEPDLLLFDEPLSNLDANLRVN 171
Cdd:cd03213   99 VRETLMFAAKLRG-----------------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQ 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 515998033 172 MRVEIRRIQQElGITTVYVSHD-QEECFSISDQVAIMNKGNI 212
Cdd:cd03213  150 VMSLLRRLADT-GRTIICSIHQpSSEIFELFDKLLLLSQGRV 190
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
 1-275 3.27e-26

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 108.01  E-value: 3.27e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   1 MALLTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKdytrvPVNKRNFGFV 80
Cdd:PRK09536   1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGD-----DVEALSARAA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  81 FQSYALFPHLSvfdNVAFGLRLRKVKE--------------DDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIAR 146
Cdd:PRK09536  76 SRRVASVPQDT---SLSFEFDVRQVVEmgrtphrsrfdtwtETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLAR 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033 147 ALVIEPDLLLFDEPLSNLDANLRVNMRVEIRRIQQElGITTVYVSHDQEECFSISDQVAIMNKGNIEQLDAPSTIFKYPT 226
Cdd:PRK09536 153 ALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDD-GKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADT 231

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033 227 TE--FVAR-FIGFN--------NFLSFDERTEEGErirlntgDLSFSVVrnqGTVQPGAR 275
Cdd:PRK09536 232 LRaaFDARtAVGTDpatgaptvTPLPDPDRTEAAA-------DTRVHVV---GGGQPAAR 281
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
 3-233 6.31e-26

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 104.04  E-value: 6.31e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   3 LLTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKdyTRVpvnkrnfGFVFQ 82
Cdd:PRK09544   4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK--LRI-------GYVPQ 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  83 SYALFPHLSVfdNVAFGLRLRK-VKEDDVkrrvMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPL 161
Cdd:PRK09544  75 KLYLDTTLPL--TVNRFLRLRPgTKKEDI----LPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPT 148

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515998033 162 SNLDANLRVNMRVEIRRIQQELGITTVYVSHDQEECFSISDQVAIMNkGNIEQLDAPSTIFKYPttEFVARF 233
Cdd:PRK09544 149 QGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLN-HHICCSGTPEVVSLHP--EFISMF 217
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
 25-259 7.10e-26

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 105.82  E-value: 7.10e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  25 QLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVN-----KRNFGFVFQS-YA-LFPHLSVFDNVA 97
Cdd:PRK11308  37 TLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEaqkllRQKIQIVFQNpYGsLNPRKKVGQILE 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  98 FGLRLR-KVKEDDVKRRVMTMLDTVSLGG-FEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLSNLDANLR---VNM 172
Cdd:PRK11308 117 EPLLINtSLSAAERREKALAMMAKVGLRPeHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQaqvLNL 196

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033 173 RVEirrIQQELGITTVYVSHDQEECFSISDQVAIMNKGNIEQLDAPSTIFKYPTTEFVARFIGFNNFLSFDERteeGERI 252
Cdd:PRK11308 197 MMD---LQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPRHPYTQALLSATPRLNPDDR---RERI 270


                 ....*..
gi 515998033 253 RLnTGDL 259
Cdd:PRK11308 271 KL-TGEL 276
cbiO PRK13649
energy-coupling factor transporter ATPase;
19-223 8.02e-26

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 104.44  E-value: 8.02e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  19 LQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVNK------RNFGFVFQsyalFPHLSV 92
Cdd:PRK13649  23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKdikqirKKVGLVFQ----FPESQL 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  93 FD-----NVAFGLRLRKVKEDDVKRRVMTMLDTVSLGG--FEKRfPGELSGGQRQRVAIARALVIEPDLLLFDEPLSNLD 165
Cdd:PRK13649  99 FEetvlkDVAFGPQNFGVSQEEAEALAREKLALVGISEslFEKN-PFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515998033 166 AnlrvNMRVEIRRIQQEL---GITTVYVSHDQEECFSISDQVAIMNKGNIEQLDAPSTIFK 223
Cdd:PRK13649 178 P----KGRKELMTLFKKLhqsGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQ 234
cbiO PRK13646
energy-coupling factor transporter ATPase;
19-223 1.27e-25

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 104.09  E-value: 1.27e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  19 LQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGD-------KDYTRVPVNKRnFGFVFQsyalFPHLS 91
Cdd:PRK13646  23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitithktKDKYIRPVRKR-IGMVFQ----FPESQ 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  92 VF-DNVA----FGLRLRKVKEDDVKRRVMTMLDTVslgGFEKRF----PGELSGGQRQRVAIARALVIEPDLLLFDEPLS 162
Cdd:PRK13646  98 LFeDTVEreiiFGPKNFKMNLDEVKNYAHRLLMDL---GFSRDVmsqsPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTA 174

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515998033 163 NLDANLRVNMRVEIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNIEQLDAPSTIFK 223
Cdd:PRK13646 175 GLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFK 235
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
15-223 1.67e-25

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 103.63  E-value: 1.67e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  15 NQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDyTRVPVN----KRNFGFVFQSyalfPHL 90
Cdd:PRK13633  22 EKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLD-TSDEENlwdiRNKAGMVFQN----PDN 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  91 S-----VFDNVAFGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLSNLD 165
Cdd:PRK13633  97 QivatiVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLD 176

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 515998033 166 ANLRVNMRVEIRRIQQELGITTVYVSHDQEECFSiSDQVAIMNKGNIEQLDAPSTIFK 223
Cdd:PRK13633 177 PSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFK 233
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
 9-212 2.18e-25

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: 101.92  E-value: 2.18e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   9 VSVAYDNQ-LILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVN--KRNFGFVFQSYA 85
Cdd:cd03254    8 VNFSYDEKkPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKslRSMIGVVLQDTF 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  86 LFPHlSVFDNVAFGlRLRKVKEDdvkrrVMTMLDTVSLGGFEKRFP-----------GELSGGQRQRVAIARALVIEPDL 154
Cdd:cd03254   88 LFSG-TIMENIRLG-RPNATDEE-----VIEAAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLLAIARAMLRDPKI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515998033 155 LLFDEPLSNLDANLRVNMRVEIRRIQQelGITTVYVSHDqeecFSI---SDQVAIMNKGNI 212
Cdd:cd03254  161 LILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHR----LSTiknADKILVLDDGKI 215
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
2-210 2.62e-25

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 103.73  E-value: 2.62e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   2 ALLTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTF-LFGDKDYTRVPVNKRNFGFV 80
Cdd:PRK13537   6 APIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSIsLCGEPVPSRARHARQRVGVV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  81 FQSYALFPHLSVFDNVAFGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEP 160
Cdd:PRK13537  86 PQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEP 165

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 515998033 161 LSNLDANLRVNMRVEIRRIQQElGITTVYVSHDQEECFSISDQVAIMNKG 210
Cdd:PRK13537 166 TTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEG 214
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
 2-225 3.68e-25

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 102.16  E-value: 3.68e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   2 ALLTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLI--AGFLEAK---QGTFLFGDKD-YTR----VP 71
Cdd:PRK14239   4 PILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGHNiYSPrtdtVD 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  72 VNKRnFGFVFQSYALFPhLSVFDNVAFGLRLRKVKE------------------DDVKRRvmtmLDTVSLGgfekrfpge 133
Cdd:PRK14239  84 LRKE-IGMVFQQPNPFP-MSIYENVVYGLRLKGIKDkqvldeavekslkgasiwDEVKDR----LHDSALG--------- 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033 134 LSGGQRQRVAIARALVIEPDLLLFDEPLSNLDAnlrvnmrVEIRRIQQEL-----GITTVYVSHDQEECFSISDQVAIMN 208
Cdd:PRK14239 149 LSGGQQQRVCIARVLATSPKIILLDEPTSALDP-------ISAGKIEETLlglkdDYTMLLVTRSMQQASRISDRTGFFL 221

                        250
                 ....*....|....*..
gi 515998033 209 KGNIEQLDAPSTIFKYP 225
Cdd:PRK14239 222 DGDLIEYNDTKQMFMNP 238
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
 3-193 4.59e-25

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 105.53  E-value: 4.59e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   3 LLTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGdkdyTRVpvnkrNFGFVFQ 82
Cdd:COG0488  315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLG----ETV-----KIGYFDQ 385

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  83 SYALF-PHLSVFDNvafglrLRKVKEDDVKRRVMTMldtvsLGGFekRFPGE--------LSGGQRQRVAIARALVIEPD 153
Cdd:COG0488  386 HQEELdPDKTVLDE------LRDGAPGGTEQEVRGY-----LGRF--LFSGDdafkpvgvLSGGEKARLALAKLLLSPPN 452

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 515998033 154 LLLFDEPLSNLDanlrvnmrVEIRRIQQEL-----GiTTVYVSHD 193
Cdd:COG0488  453 VLLLDEPTNHLD--------IETLEALEEAlddfpG-TVLLVSHD 488
cbiO PRK13641
energy-coupling factor transporter ATPase;
19-223 7.11e-25

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 102.21  E-value: 7.11e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  19 LQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVNK------RNFGFVFQsyalFPHLSV 92
Cdd:PRK13641  23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKnlkklrKKVSLVFQ----FPEAQL 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  93 FDN-----VAFGLRLRKVKEDDVKRRVMTMLDTVSLG-GFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLSNLDA 166
Cdd:PRK13641  99 FENtvlkdVEFGPKNFGFSEDEAKEKALKWLKKVGLSeDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDP 178

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 515998033 167 NLRVNMrVEIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNIEQLDAPSTIFK 223
Cdd:PRK13641 179 EGRKEM-MQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFS 234
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
 27-225 2.11e-24

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 100.65  E-value: 2.11e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  27 ERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVN--KRNFGFVFQSyalfPHLSVFD-----NVAFG 99
Cdd:PRK13652  28 PRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIRevRKFVGLVFQN----PDDQIFSptveqDIAFG 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033 100 LRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLSNLDANLRVNMRVEIRRI 179
Cdd:PRK13652 104 PINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDL 183

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 515998033 180 QQELGITTVYVSHDQEECFSISDQVAIMNKGNIEQLDAPSTIFKYP 225
Cdd:PRK13652 184 PETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
 23-210 5.22e-24

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


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 98.91  E-value: 5.22e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  23 DLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVNK-RNFGFV--FQSYALFPHLSVFDN--VA 97
Cdd:PRK11300  25 NLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQiARMGVVrtFQHVRLFREMTVIENllVA 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  98 FGLRLR-------------KVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLSNL 164
Cdd:PRK11300 105 QHQQLKtglfsgllktpafRRAESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGL 184

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 515998033 165 DANLRVNMRVEIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKG 210
Cdd:PRK11300 185 NPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQG 230
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
 2-212 6.48e-24

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: 96.73  E-value: 6.48e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   2 ALLTLDRVSVAydnqLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPV---NKRNFG 78
Cdd:cd03215    3 PVLEVRGLSVK----GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPrdaIRAGIA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  79 FV---FQSYALFPHLSVFDNVAFGLRLrkvkeddvkrrvmtmldtvslggfekrfpgelSGGQRQRVAIARALVIEPDLL 155
Cdd:cd03215   79 YVpedRKREGLVLDLSVAENIALSSLL--------------------------------SGGNQQKVVLARWLARDPRVL 126

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033 156 LFDEPLSNLDanlrVNMRVEIRRIQQEL---GITTVYVSHDQEECFSISDQVAIMNKGNI 212
Cdd:cd03215  127 ILDEPTRGVD----VGAKAEIYRLIRELadaGKAVLLISSELDELLGLCDRILVMYEGRI 182
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
 4-212 1.10e-23

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: 97.56  E-value: 1.10e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   4 LTLDRVSVAY--DNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVN--KRNFGF 79
Cdd:cd03252    1 ITFEHVRFRYkpDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAwlRRQVGV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  80 VFQSYALFpHLSVFDNVAF---GLRLRKVKEddvkrrvmtmldTVSLGG---FEKRFP-------GE----LSGGQRQRV 142
Cdd:cd03252   81 VLQENVLF-NRSIRDNIALadpGMSMERVIE------------AAKLAGahdFISELPegydtivGEqgagLSGGQRQRI 147

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033 143 AIARALVIEPDLLLFDEPLSNLDANLRVNMRVEIRRIQQelGITTVYVSHdQEECFSISDQVAIMNKGNI 212
Cdd:cd03252  148 AIARALIHNPRILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAH-RLSTVKNADRIIVMEKGRI 214
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 18-212 3.30e-23

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


Pssm-ID: 440718 [Multi-domain]  Cd Length: 264  Bit Score: 97.08  E-value: 3.30e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  18 ILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVNKR--NFGFVFQSYAL--FPHLSVF 93
Cdd:COG1101   21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRakYIGRVFQDPMMgtAPSMTIE 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  94 DNVA--------FGLRLRKVKEDdvKRRVMTMLDTVSLGgFEKRFP---GELSGGQRQRVAIARALVIEPDLLLFDEPLS 162
Cdd:COG1101  101 ENLAlayrrgkrRGLRRGLTKKR--RELFRELLATLGLG-LENRLDtkvGLLSGGQRQALSLLMATLTKPKLLLLDEHTA 177

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 515998033 163 NLD---ANLRVNMrveIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNI 212
Cdd:COG1101  178 ALDpktAALVLEL---TEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRI 227
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
3-212 5.83e-23

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 96.24  E-value: 5.83e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   3 LLTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTF----LFGD------KDYTRVPV 72
Cdd:PRK09984   4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAGshieLLGRtvqregRLARDIRK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  73 NKRNFGFVFQSYALFPHLSVFDNVAFGLR---------LRKVKEDDvKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVA 143
Cdd:PRK09984  84 SRANTGYIFQQFNLVNRLSVLENVLIGALgstpfwrtcFSWFTREQ-KQRALQALTRVGMVHFAHQRVSTLSGGQQQRVA 162

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033 144 IARALVIEPDLLLFDEPLSNLDA-NLRVNMRVeIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNI 212
Cdd:PRK09984 163 IARALMQQAKVILADEPIASLDPeSARIVMDT-LRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
 4-167 5.90e-23

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: 94.73  E-value: 5.90e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033    4 LTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRV-PVNKRNFGFVFQ 82
Cdd:TIGR01189   1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQrDEPHENILYLGH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   83 SYALFPHLSVFDNVAFGLRLrkvkEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLS 162
Cdd:TIGR01189  81 LPGLKPELSALENLHFWAAI----HGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTT 156


                  ....*
gi 515998033  163 NLDAN 167
Cdd:TIGR01189 157 ALDKA 161
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 19-233 5.98e-23

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


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 97.47  E-value: 5.98e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  19 LQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKD-YTRVPVNKRNFGFVF-QSYALFPHLSVFDNv 96
Cdd:COG4586   38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVpFKRRKEFARRIGVVFgQRSQLWWDLPAIDS- 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  97 afgLRLRK----VKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLSNLDANLRVNM 172
Cdd:COG4586  117 ---FRLLKaiyrIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAI 193

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515998033 173 RVEIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNIeqldapstIFKYPTTEFVARF 233
Cdd:COG4586  194 REFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRI--------IYDGSLEELKERF 246
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
 6-167 8.02e-23

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 98.98  E-value: 8.02e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   6 LDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFgDKDYTrvpvnkrnFGFVFQSYA 85
Cdd:COG0488    1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI-PKGLR--------IGYLPQEPP 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  86 LFPHLSVFDNVAFGL-RLRKVK-------------EDDVKR------------------RVMTMLDTVSLGG--FEKRFp 131
Cdd:COG0488   72 LDDDLTVLDTVLDGDaELRALEaeleeleaklaepDEDLERlaelqeefealggweaeaRAEEILSGLGFPEedLDRPV- 150

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 515998033 132 GELSGGQRQRVAIARALVIEPDLLLFDEPLSNLDAN 167
Cdd:COG0488  151 SELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLE 186
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
 19-210 1.32e-22

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 95.57  E-value: 1.32e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  19 LQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTF-LFGDKdytrvpVNKRN-------FGFVFQSY--ALFP 88
Cdd:PRK13647  21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVkVMGRE------VNAENekwvrskVGLVFQDPddQVFS 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  89 hLSVFDNVAFGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLSNLDANL 168
Cdd:PRK13647  95 -STVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRG 173

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 515998033 169 RVNMRVEIRRIQQElGITTVYVSHDQEECFSISDQVAIMNKG 210
Cdd:PRK13647 174 QETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEG 214
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
 4-167 2.62e-22

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 93.01  E-value: 2.62e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   4 LTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTrvpvnkrnFGFVFQS 83
Cdd:PRK13539   3 LEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDID--------DPDVAEA 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  84 --Y-----ALFPHLSVFDNVAFGLRLRKVKEddvkRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLL 156
Cdd:PRK13539  75 chYlghrnAMKPALTVAENLEFWAAFLGGEE----LDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWI 150

                        170
                 ....*....|.
gi 515998033 157 FDEPLSNLDAN 167
Cdd:PRK13539 151 LDEPTAALDAA 161
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
 4-167 3.46e-22

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: 92.56  E-value: 3.46e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   4 LTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLF-GDKDYTRVPVNKRNFGFVFQ 82
Cdd:cd03231    1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLnGGPLDFQRDSIARGLLYLGH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  83 SYALFPHLSVFDNVAFglrLRKVKEDDvkrRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLS 162
Cdd:cd03231   81 APGIKTTLSVLENLRF---WHADHSDE---QVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTT 154


                 ....*
gi 515998033 163 NLDAN 167
Cdd:cd03231  155 ALDKA 159
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
 1-226 6.03e-22

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 96.70  E-value: 6.03e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   1 MALLTLDRVSVAYDNQ----LILQDFDLQLERGQLLSLLGPSGCGKTTT----LRLI-AGFLEAKQGTFLFGDKDYTRVP 71
Cdd:PRK15134   3 QPLLAIENLSVAFRQQqtvrTVVNDVSLQIEAGETLALVGESGSGKSVTalsiLRLLpSPPVVYPSGDIRFHGESLLHAS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  72 ------VNKRNFGFVFQS--YALFPHLSVFDNVAFGLRL-RKVKEDDVKRRVMTMLDTVSLGGFEKR---FPGELSGGQR 139
Cdd:PRK15134  83 eqtlrgVRGNKIAMIFQEpmVSLNPLHTLEKQLYEVLSLhRGMRREAARGEILNCLDRVGIRQAAKRltdYPHQLSGGER 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033 140 QRVAIARALVIEPDLLLFDEPLSNLDANLRVNMRVEIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNIEQLDAPS 219
Cdd:PRK15134 163 QRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAA 242


                 ....*..
gi 515998033 220 TIFKYPT 226
Cdd:PRK15134 243 TLFSAPT 249
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
 4-166 8.74e-22

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: 90.84  E-value: 8.74e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   4 LTLDRVSVAYDNQ--LILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVNKRN-FGFV 80
Cdd:cd03247    1 LSINNVSFSYPEQeqQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSlISVL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  81 FQSyalfPHLsvfdnvaFGLRLRkvkeDDVKRRvmtmldtvslggfekrfpgeLSGGQRQRVAIARALVIEPDLLLFDEP 160
Cdd:cd03247   81 NQR----PYL-------FDTTLR----NNLGRR--------------------FSGGERQRLALARILLQDAPIVLLDEP 125


                 ....*.
gi 515998033 161 LSNLDA 166
Cdd:cd03247  126 TVGLDP 131
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
 4-192 1.27e-21

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 95.64  E-value: 1.27e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   4 LTLDRVSVA-YDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFlfgdkdytRVPVNKRNFgFVFQ 82
Cdd:COG4178  363 LALEDLTLRtPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRI--------ARPAGARVL-FLPQ 433

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  83 -SYalFPHLSVFDNVAFGLRLRKVKEDDVKrrvmTMLDTVSLGGF------EKRFPGELSGGQRQRVAIARALVIEPDLL 155
Cdd:COG4178  434 rPY--LPLGTLREALLYPATAEAFSDAELR----EALEAVGLGHLaerldeEADWDQVLSLGEQQRLAFARLLLHKPDWL 507

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 515998033 156 LFDEPLSNLDANLRVNMrveIRRIQQEL-GITTVYVSH 192
Cdd:COG4178  508 FLDEATSALDEENEAAL---YQLLREELpGTTVISVGH 542
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
 4-195 1.30e-21

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: 89.43  E-value: 1.30e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   4 LTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGdkdytrvpvnkrnfgfvfqs 83
Cdd:cd03221    1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG-------------------- 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  84 yalfphlsvfdnvafglrlrkvkeddvkrrvmtmlDTVSLGGFEKrfpgeLSGGQRQRVAIARALVIEPDLLLFDEPLSN 163
Cdd:cd03221   61 -----------------------------------STVKIGYFEQ-----LSGGEKMRLALAKLLLENPNLLLLDEPTNH 100

                        170       180       190
                 ....*....|....*....|....*....|..
gi 515998033 164 LDanlrVNMRVEIRRIQQELGITTVYVSHDQE 195
Cdd:cd03221  101 LD----LESIEALEEALKEYPGTVILVSHDRY 128
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
 9-167 2.32e-21

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: 90.99  E-value: 2.32e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   9 VSVAYDNQ---LILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKdytrvPVN-------KRNFG 78
Cdd:cd03248   17 VTFAYPTRpdtLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGK-----PISqyehkylHSKVS 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  79 FVFQSYALFPHlSVFDNVAFGLR---LRKVKEDDVKRR----VMTMLDTVSLGGFEKrfPGELSGGQRQRVAIARALVIE 151
Cdd:cd03248   92 LVGQEPVLFAR-SLQDNIAYGLQscsFECVKEAAQKAHahsfISELASGYDTEVGEK--GSQLSGGQKQRVAIARALIRN 168

                        170
                 ....*....|....*.
gi 515998033 152 PDLLLFDEPLSNLDAN 167
Cdd:cd03248  169 PQVLILDEATSALDAE 184
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
19-212 3.30e-21

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 94.31  E-value: 3.30e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  19 LQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYT-RVPVNKRNFGFVF-----QSYALFPHLSV 92
Cdd:COG1129  268 VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRiRSPRDAIRAGIAYvpedrKGEGLVLDLSI 347

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  93 FDNVAF--------GLRLRKVKEDDVKRRVMTMLDTvslggfekRFP------GELSGGQRQRVAIARALVIEPDLLLFD 158
Cdd:COG1129  348 RENITLasldrlsrGGLLDRRRERALAEEYIKRLRI--------KTPspeqpvGNLSGGNQQKVVLAKWLATDPKVLILD 419

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 515998033 159 EPLSNLDanlrVNMRVEIRRIQQEL---GITTVYVSHDQEECFSISDQVAIMNKGNI 212
Cdd:COG1129  420 EPTRGID----VGAKAEIYRLIRELaaeGKAVIVISSELPELLGLSDRILVMREGRI 472
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
 3-210 4.43e-21

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 93.94  E-value: 4.43e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   3 LLTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKdytrvPVNKRNF----- 77
Cdd:COG3845    5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGK-----PVRIRSPrdaia 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  78 ---GFVFQSYALFPHLSVFDNVAFGL---RLRKVKEDDVKRRVMTMLDTVslgGFE---KRFPGELSGGQRQRVAIARAL 148
Cdd:COG3845   80 lgiGMVHQHFMLVPNLTVAENIVLGLeptKGGRLDRKAARARIRELSERY---GLDvdpDAKVEDLSVGEQQRVEILKAL 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515998033 149 VIEPDLLLFDEPLSNL-----DANLRVnmrveIRRIQQElGITTVYVSHDQEECFSISDQVAIMNKG 210
Cdd:COG3845  157 YRGARILILDEPTAVLtpqeaDELFEI-----LRRLAAE-GKSIIFITHKLREVMAIADRVTVLRRG 217
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
 9-212 5.14e-21

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: 94.01  E-value: 5.14e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033    9 VSVAY--DNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGD---KDYTRVPVnKRNFGFVFQS 83
Cdd:TIGR02203 336 VTFRYpgRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGhdlADYTLASL-RRQVALVSQD 414

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   84 YALFPHlSVFDNVAFGlRLRKVKEDDVKRRV-----MTMLDTVSLGgfeKRFP-----GELSGGQRQRVAIARALVIEPD 153
Cdd:TIGR02203 415 VVLFND-TIANNIAYG-RTEQADRAEIERALaaayaQDFVDKLPLG---LDTPigengVLLSGGQRQRLAIARALLKDAP 489

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 515998033  154 LLLFDEPLSNLDANLRVNMRVEIRRIQQelGITTVYVSHdQEECFSISDQVAIMNKGNI 212
Cdd:TIGR02203 490 ILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAH-RLSTIEKADRIVVMDDGRI 545
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
 9-235 8.52e-21

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 90.54  E-value: 8.52e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   9 VSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDK--------DYTRVPVNKRNFGFV 80
Cdd:PRK14271  27 LTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVllggrsifNYRDVLEFRRRVGML 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  81 FQSYALFPhLSVFDNVAFGLRLRK-VKEDDVKRRVMTMLDTVSL-GGFEKRF---PGELSGGQRQRVAIARALVIEPDLL 155
Cdd:PRK14271 107 FQRPNPFP-MSIMDNVLAGVRAHKlVPRKEFRGVAQARLTEVGLwDAVKDRLsdsPFRLSGGQQQLLCLARTLAVNPEVL 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033 156 LFDEPLSNLDANLRVNMRVEIRRIQQELgiTTVYVSHDQEECFSISDQVAIMNKGNIEQLDAPSTIFKYPTTEFVARFIG 235
Cdd:PRK14271 186 LLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYVA 263
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
2-193 1.13e-20

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 93.25  E-value: 1.13e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   2 ALLTLDRVSVAY---DNQL-ILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRV------P 71
Cdd:PRK10535   3 ALLELKDIRRSYpsgEEQVeVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLdadalaQ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  72 VNKRNFGFVFQSYALFPHLSVFDNVAFGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIE 151
Cdd:PRK10535  83 LRREHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNG 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 515998033 152 PDLLLFDEPLSNLDANLRVNMRVEIRRIQQElGITTVYVSHD 193
Cdd:PRK10535 163 GQVILADEPTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHD 203
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
 10-210 1.48e-20

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: 88.30  E-value: 1.48e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  10 SVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTflfgdkdytrVPVNKRnFGFVFQSYALFPh 89
Cdd:cd03250   12 SGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGS----------VSVPGS-IAYVSQEPWIQN- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  90 LSVFDNVAFGLRLRKVKEDDVKR--------RVMTMLDTVSLGgfEKrfpG-ELSGGQRQRVAIARALVIEPDLLLFDEP 160
Cdd:cd03250   80 GTIRENILFGKPFDEERYEKVIKacalepdlEILPDGDLTEIG--EK---GiNLSGGQKQRISLARAVYSDADIYLLDDP 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 515998033 161 LSNLDANlrvnmrVEiRRIQQEL-------GITTVYVSHdQEECFSISDQVAIMNKG 210
Cdd:cd03250  155 LSAVDAH------VG-RHIFENCilglllnNKTRILVTH-QLQLLPHADQIVVLDNG 203
type_I_sec_PrtD TIGR01842
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ...
 4-212 2.81e-20

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: 91.64  E-value: 2.81e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033    4 LTLDRVSVAY--DNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVNK--RNFGF 79
Cdd:TIGR01842 317 LSVENVTIVPpgGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETfgKHIGY 396

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   80 VFQSYALFPHlSVFDNVA-FGLRL--RKVKEDDVKRRVMTML-------DT-VSLGGfekrfpGELSGGQRQRVAIARAL 148
Cdd:TIGR01842 397 LPQDVELFPG-TVAENIArFGENAdpEKIIEAAKLAGVHELIlrlpdgyDTvIGPGG------ATLSGGQRQRIALARAL 469

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515998033  149 VIEPDLLLFDEPLSNLDANLRVNMRVEIRRIQQElGITTVYVSHdQEECFSISDQVAIMNKGNI 212
Cdd:TIGR01842 470 YGDPKLVVLDEPNSNLDEEGEQALANAIKALKAR-GITVVVITH-RPSLLGCVDKILVLQDGRI 531
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
 3-218 4.35e-20

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 88.06  E-value: 4.35e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   3 LLTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVN-----KRNF 77
Cdd:PRK11701   6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYalseaERRR 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  78 ------GFVFQSYA--LFPHLSVFDNVafGLRLRKVKED---DVKRRVMTMLDTVSLGgfEKR---FPGELSGGQRQRVA 143
Cdd:PRK11701  86 llrtewGFVHQHPRdgLRMQVSAGGNI--GERLMAVGARhygDIRATAGDWLERVEID--AARiddLPTTFSGGMQQRLQ 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033 144 IARALVIEPDLLLFDEPLSNLDANLRVNMRVEIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGN-IEQ------LD 216
Cdd:PRK11701 162 IARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRvVESgltdqvLD 241


                 ..
gi 515998033 217 AP 218
Cdd:PRK11701 242 DP 243
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
 19-210 4.43e-20

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: 87.49  E-value: 4.43e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  19 LQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFgDKDYTRVP-----------VNKRNFGFVFQSYALF 87
Cdd:COG4778   27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILV-RHDGGWVDlaqaspreilaLRRRTIGYVSQFLRVI 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  88 PHLSVFDNVAFGLRLRKVKEDDVKRRVMTMLDTVSLggfEKR----FPGELSGGQRQRVAIARALVIEPDLLLFDEPLSN 163
Cdd:COG4778  106 PRVSALDVVAEPLLERGVDREEARARARELLARLNL---PERlwdlPPATFSGGEQQRVNIARGFIADPPLLLLDEPTAS 182

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 515998033 164 LDAnlrVNMRVEIRRIQQEL--GITTVYVSHDQEECFSISDQVAIMNKG 210
Cdd:COG4778  183 LDA---ANRAVVVELIEEAKarGTAIIGIFHDEEVREAVADRVVDVTPF 228
PLN03211 PLN03211
ABC transporter G-25; Provisional
 29-210 4.82e-20

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 91.48  E-value: 4.82e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  29 GQLLSLLGPSGCGKTTTLRLIAGFLEAK--QGTFLFGDKDYTRvPVNKRNfGFVFQSYALFPHLSVFDNVAFG--LRLRK 104
Cdd:PLN03211  94 GEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTK-QILKRT-GFVTQDDILYPHLTVRETLVFCslLRLPK 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033 105 VKEDDVKRRVM-TMLDTVSLGGFEKRFPGE-----LSGGQRQRVAIARALVIEPDLLLFDEPLSNLDANLRVNMRVEIRR 178
Cdd:PLN03211 172 SLTKQEKILVAeSVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGS 251

                        170       180       190
                 ....*....|....*....|....*....|...
gi 515998033 179 IQQElGITTVYVSHD-QEECFSISDQVAIMNKG 210
Cdd:PLN03211 252 LAQK-GKTIVTSMHQpSSRVYQMFDSVLVLSEG 283
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
 19-212 5.22e-20

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 88.99  E-value: 5.22e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  19 LQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGT--FLFGDKDYTRVPVNK---------------------- 74
Cdd:PRK13651  23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTieWIFKDEKNKKKTKEKekvleklviqktrfkkikkike 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  75 --RNFGFVFQ--SYALFPHlSVFDNVAFGLRLRKVKEDDVKRRVMTMLDTVSLG-GFEKRFPGELSGGQRQRVAIARALV 149
Cdd:PRK13651 103 irRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDeSYLQRSPFELSGGQKRRVALAGILA 181

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515998033 150 IEPDLLLFDEPLSNLDANLRVNMrVEIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNI 212
Cdd:PRK13651 182 MEPDFLVFDEPTAGLDPQGVKEI-LEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKI 243
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
 4-321 5.69e-20

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


Pssm-ID: 132313 [Multi-domain]  Cd Length: 520  Bit Score: 90.63  E-value: 5.69e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033    4 LTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGF------------------------------- 52
Cdd:TIGR03269   1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqyeptsgriiyhvalcekcgyverpskvge 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   53 --------LEAKQGTFLFGDKDYTRvPVNKRNFGFVFQSYALFPHLSVFDNVAFGLRLRKVKEDDVKRRVMTMLDTVSLG 124
Cdd:TIGR03269  81 pcpvcggtLEPEEVDFWNLSDKLRR-RIRKRIAIMLQRTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLS 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  125 GFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLSNLD---ANLRVNMrveIRRIQQELGITTVYVSHDQEECFSIS 201
Cdd:TIGR03269 160 HRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDpqtAKLVHNA---LEEAVKASGISMVLTSHWPEVIEDLS 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  202 DQVAIMNKGNIEQLDAPSTIfkypttefVARFIGFNNFLSFDERTEEGERIrLNTGDLS---FSVVRnqgtvqpgarqGA 278
Cdd:TIGR03269 237 DKAIWLENGEIKEEGTPDEV--------VAVFMEGVSEVEKECEVEVGEPI-IKVRNVSkryISVDR-----------GV 296

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 515998033  279 IRPDDLVirteGNETGENELPGVIKVS----TYLGRSYQYVVETAKG 321
Cdd:TIGR03269 297 VKAVDNV----SLEVKEGEIFGIVGTSgagkTTLSKIIAGVLEPTSG 339
NHLM_micro_ABC1 TIGR03796
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ...
 18-192 6.06e-20

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: 91.16  E-value: 6.06e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   18 ILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVP--VNKRNFGFVFQSYALFPHlSVFDN 95
Cdd:TIGR03796 494 LIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPreVLANSVAMVDQDIFLFEG-TVRDN 572

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   96 VAfgLRLRKVKEDDVKR--RVMTMLDTVSL--GGFEKRFP---GELSGGQRQRVAIARALVIEPDLLLFDEPLSNLDA-- 166
Cdd:TIGR03796 573 LT--LWDPTIPDADLVRacKDAAIHDVITSrpGGYDAELAeggANLSGGQRQRLEIARALVRNPSILILDEATSALDPet 650

                         170       180       190
                  ....*....|....*....|....*....|..
gi 515998033  167 ------NLRvnmrveiRRiqqelGITTVYVSH 192
Cdd:TIGR03796 651 ekiiddNLR-------RR-----GCTCIIVAH 670
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
23-165 9.40e-20

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 90.57  E-value: 9.40e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  23 DLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGT-FLFGDkdytrvPVN------KRNFGFVFQSYALFPHLSVFDN 95
Cdd:NF033858 286 SFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEaWLFGQ------PVDagdiatRRRVGYMSQAFSLYGELTVRQN 359

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  96 VAFGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLSNLD 165
Cdd:NF033858 360 LELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
26-234 1.52e-19

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 86.77  E-value: 1.52e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  26 LERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFL-------FGDKDYtrvpvNKRNFGFVFQ--SYALFPHLSVFDNV 96
Cdd:PRK15112  36 LREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLiddhplhFGDYSY-----RSQRIRMIFQdpSTSLNPRQRISQIL 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  97 AFGLRLR-KVKEDDVKRRVMTMLDTVSL-GGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLSNLDANLR---VN 171
Cdd:PRK15112 111 DFPLRLNtDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRsqlIN 190

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515998033 172 MRVEirrIQQELGITTVYVSHDQEECFSISDQVAIMNKGNIEQLDAPSTIFKYPTTEFVARFI 234
Cdd:PRK15112 191 LMLE---LQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPLHELTKRLI 250
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
1-212 1.64e-19

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


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 86.09  E-value: 1.64e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   1 MALLTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVP---VNKRNF 77
Cdd:PRK11614   3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQtakIMREAV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  78 GFVFQSYALFPHLSVFDNVAF-GLRLRKVKEDDVKRRVMTMLDTVslggFEKRF--PGELSGGQRQRVAIARALVIEPDL 154
Cdd:PRK11614  83 AIVPEGRRVFSRMTVEENLAMgGFFAERDQFQERIKWVYELFPRL----HERRIqrAGTMSGGEQQMLAIGRALMSQPRL 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 515998033 155 LLFDEPLSNLDANLRVNMRVEIRRIQQElGITTVYVSHDQEECFSISDQVAIMNKGNI 212
Cdd:PRK11614 159 LLLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHV 215
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
 3-212 3.28e-19

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 88.57  E-value: 3.28e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   3 LLTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRV-PVNKRNFG--F 79
Cdd:PRK15439  11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLtPAKAHQLGiyL 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  80 VFQSYALFPHLSVFDNVAFGLrlrkVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDE 159
Cdd:PRK15439  91 VPQEPLLFPNLSVKENILFGL----PKRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDE 166

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 515998033 160 PLSNLDANLRVNMRVEIRRIQQElGITTVYVSHDQEECFSISDQVAIMNKGNI 212
Cdd:PRK15439 167 PTASLTPAETERLFSRIRELLAQ-GVGIVFISHKLPEIRQLADRISVMRDGTI 218
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
 19-226 1.00e-18

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 87.22  E-value: 1.00e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  19 LQDFDLQLERGQLLSLLGPSGCGKTTT----LRLI--AGFLEAKQGTFL------------FGDKDYTRVpvNKRNFGFV 80
Cdd:PRK10261  32 VRNLSFSLQRGETLAIVGESGSGKSVTalalMRLLeqAGGLVQCDKMLLrrrsrqvielseQSAAQMRHV--RGADMAMI 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  81 FQS--YALFPHLSVFDNVAFGLRLRK-VKEDDVKRRVMTMLDTVSLGGFE---KRFPGELSGGQRQRVAIARALVIEPDL 154
Cdd:PRK10261 110 FQEpmTSLNPVFTVGEQIAESIRLHQgASREEAMVEAKRMLDQVRIPEAQtilSRYPHQLSGGMRQRVMIAMALSCRPAV 189

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515998033 155 LLFDEPLSNLDANLRVNMRVEIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNIEQLDAPSTIFKYPT 226
Cdd:PRK10261 190 LIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQ 261
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
7-236 1.51e-18

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 84.27  E-value: 1.51e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   7 DRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQG-TFLFGD--KDYTRVPVNKRnFGFVFQS 83
Cdd:PRK10253  11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGhVWLDGEhiQHYASKEVARR-IGLLAQN 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  84 YALFPHLSVFDNVAFG--------LRLRKVKEDDVKRrVMTMLDTVSLGGfekRFPGELSGGQRQRVAIARALVIEPDLL 155
Cdd:PRK10253  90 ATTPGDITVQELVARGryphqplfTRWRKEDEEAVTK-AMQATGITHLAD---QSVDTLSGGQRQRAWIAMVLAQETAIM 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033 156 LFDEPLSNLDANLRVNMRVEIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNIEQLDAPSTIFkypTTEFVARFIG 235
Cdd:PRK10253 166 LLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIV---TAELIERIYG 242


                 .
gi 515998033 236 F 236
Cdd:PRK10253 243 L 243
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
 4-212 1.52e-18

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: 86.72  E-value: 1.52e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033    4 LTLDRVSVAYD-NQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVN--KRNFGFV 80
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHtlRQFINYL 553

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   81 FQSYALFPHlSVFDNVAFGLRlRKVKEDDVKR-----RVMTMLDTVSLGgFEKRFPGE---LSGGQRQRVAIARALVIEP 152
Cdd:TIGR01193 554 PQEPYIFSG-SILENLLLGAK-ENVSQDEIWAaceiaEIKDDIENMPLG-YQTELSEEgssISGGQKQRIALARALLTDS 630

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515998033  153 DLLLFDEPLSNLDanlrvnMRVEIRRIQQELGI---TTVYVSHdQEECFSISDQVAIMNKGNI 212
Cdd:TIGR01193 631 KVLILDESTSNLD------TITEKKIVNNLLNLqdkTIIFVAH-RLSVAKQSDKIIVLDHGKI 686
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
 18-216 1.59e-18

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: 82.97  E-value: 1.59e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  18 ILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTflfgdkdytrVPVNKRNFGFVFQSYALFPHLSVFDNVA 97
Cdd:cd03220   37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGT----------VTVRGRVSSLLGLGGGFNPELTGRENIY 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  98 FGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLSNLDANLRVNMRVEIR 177
Cdd:cd03220  107 LNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLR 186

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 515998033 178 RIQQElGITTVYVSHDQEECFSISDQVAIMNKGNIEQLD 216
Cdd:cd03220  187 ELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
 21-226 2.02e-18

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 84.78  E-value: 2.02e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  21 DFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAK---QGTFLFGDKDYTRVPVNKRN------FGFVFQS--YALFPH 89
Cdd:PRK09473  34 DLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNLPEKELNklraeqISMIFQDpmTSLNPY 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  90 LSVFDNVAFGLRLRK------VKEDDVKrrvmtMLDTVSLGGFEKR---FPGELSGGQRQRVAIARALVIEPDLLLFDEP 160
Cdd:PRK09473 114 MRVGEQLMEVLMLHKgmskaeAFEESVR-----MLDAVKMPEARKRmkmYPHEFSGGMRQRVMIAMALLCRPKLLIADEP 188

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515998033 161 LSNLDANLRVNMRVEIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNIEQLDAPSTIFKYPT 226
Cdd:PRK09473 189 TTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPS 254
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
 2-215 2.10e-18

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 86.03  E-value: 2.10e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   2 ALLTLDRVSVAYDNQ--LILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVN--KRNF 77
Cdd:PRK11160 337 VSLTLNNVSFTYPDQpqPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAalRQAI 416

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  78 GFVFQSYALFPHlSVFDNvafgLRLRKVKEDDvkRRVMTMLDTVSLGGFEKRFPG----------ELSGGQRQRVAIARA 147
Cdd:PRK11160 417 SVVSQRVHLFSA-TLRDN----LLLAAPNASD--EALIEVLQQVGLEKLLEDDKGlnawlgeggrQLSGGEQRRLGIARA 489

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515998033 148 LVIEPDLLLFDEPLSNLDAnlrvnmRVEiRRIQQEL-----GITTVYVSH-----DQEECFSISDQVAIMNKGNIEQL 215
Cdd:PRK11160 490 LLHDAPLLLLDEPTEGLDA------ETE-RQILELLaehaqNKTVLMITHrltglEQFDRICVMDNGQIIEQGTHQEL 560
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
 30-212 2.35e-18

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


Pssm-ID: 130324 [Multi-domain]  Cd Length: 2272  Bit Score: 86.61  E-value: 2.35e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033    30 QLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDY-TRVPVNKRNFGFVFQSYALFPHLSVFDNVAFGLRLRKVKED 108
Cdd:TIGR01257  957 QITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIeTNLDAVRQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSWE 1036

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   109 DVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLSNLDANLRVNMRVEIRRIQQelGITTV 188
Cdd:TIGR01257 1037 EAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRS--GRTII 1114

                          170       180
                   ....*....|....*....|....
gi 515998033   189 YVSHDQEECFSISDQVAIMNKGNI 212
Cdd:TIGR01257 1115 MSTHHMDEADLLGDRIAIISQGRL 1138
type_I_sec_HlyB TIGR01846
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ...
 4-212 2.53e-18

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: 86.33  E-value: 2.53e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033    4 LTLDRVSVAY--DNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVN--KRNFGF 79
Cdd:TIGR01846 456 ITFENIRFRYapDSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAwlRRQMGV 535

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   80 VFQSYALFPHlSVFDNVAFGLRLRKVKEDDVKRRVMTMLDTVSL--GGFEKRFP---GELSGGQRQRVAIARALVIEPDL 154
Cdd:TIGR01846 536 VLQENVLFSR-SIRDNIALCNPGAPFEHVIHAAKLAGAHDFISElpQGYNTEVGekgANLSGGQRQRIAIARALVGNPRI 614

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 515998033  155 LLFDEPLSNLDANLRVNMRVEIRRIQQelGITTVYVSHdQEECFSISDQVAIMNKGNI 212
Cdd:TIGR01846 615 LIFDEATSALDYESEALIMRNMREICR--GRTVIIIAH-RLSTVRACDRIIVLEKGQI 669
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
 9-215 3.65e-18

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 85.54  E-value: 3.65e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033    9 VSVAYDN---QLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDkdytrVPVNK-------RNFG 78
Cdd:TIGR00958 484 VSFSYPNrpdVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDG-----VPLVQydhhylhRQVA 558

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   79 FVFQSYALFPHlSVFDNVAFGLRlrKVKEDDVKRRVMTMLDTVSLGGFEKRFPGE-------LSGGQRQRVAIARALVIE 151
Cdd:TIGR00958 559 LVGQEPVLFSG-SVRENIAYGLT--DTPDEEIMAAAKAANAHDFIMEFPNGYDTEvgekgsqLSGGQKQRIAIARALVRK 635

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515998033  152 PDLLLFDEPLSNLDAnlRVNMRVEIRRIQQELgiTTVYVSHDQEECFSiSDQVAIMNKGNIEQL 215
Cdd:TIGR00958 636 PRVLILDEATSALDA--ECEQLLQESRSRASR--TVLLIAHRLSTVER-ADQILVLKKGSVVEM 694
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
 4-232 4.02e-18

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 82.83  E-value: 4.02e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   4 LTLDRVSVAYDNQLIlQDFDLQLERGQLLSLLGPSGCGKTTT----LRLIAGFLEAKQGTFLFGDKDYTRVPVNKRNFGF 79
Cdd:PRK10418   5 IELRNIALQAAQPLV-HGVSLTLQRGRVLALVGGSGSGKSLTcaaaLGILPAGVRQTAGRVLLDGKPVAPCALRGRKIAT 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  80 VFQS--YALFPHLSVFDNVAFGLRLRKVKEDDvkRRVMTMLDTVSLGGFE---KRFPGELSGGQRQRVAIARALVIEPDL 154
Cdd:PRK10418  84 IMQNprSAFNPLHTMHTHARETCLALGKPADD--ATLTAALEAVGLENAArvlKLYPFEMSGGMLQRMMIALALLCEAPF 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033 155 LLFDEPLSNLDanLRVNMRV--EIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNIEQLDAPSTIFKYPTTEfVAR 232
Cdd:PRK10418 162 IIADEPTTDLD--VVAQARIldLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHA-VTR 238
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
 4-214 4.23e-18

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: 85.26  E-value: 4.23e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   4 LTLDRVSVAYD-NQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVN--KRNFGFV 80
Cdd:COG5265  358 VRFENVSFGYDpERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQAslRAAIGIV 437

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  81 FQSYALFpHLSVFDNVAFGlrlrkvKEDDVKRRVMTMLDTVSLGGFEKRFP-------GE----LSGGQRQRVAIARALV 149
Cdd:COG5265  438 PQDTVLF-NDTIAYNIAYG------RPDASEEEVEAAARAAQIHDFIESLPdgydtrvGErglkLSGGEKQRVAIARTLL 510

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515998033 150 IEPDLLLFDEPLSNLDanlrvnMRVEiRRIQQEL-----GITTVYVSH------DqeecfsiSDQVAIMNKGNI-EQ 214
Cdd:COG5265  511 KNPPILIFDEATSALD------SRTE-RAIQAALrevarGRTTLVIAHrlstivD-------ADEILVLEAGRIvER 573
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
14-167 8.80e-18

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 80.62  E-value: 8.80e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  14 DNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVpvnkrnfGFVFQSYALF------ 87
Cdd:PRK13538  12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQ-------RDEYHQDLLYlghqpg 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  88 --PHLSVFDNVAFGLRLRKVKEDDvkrRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLSNLD 165
Cdd:PRK13538  85 ikTELTALENLRFYQRLHGPGDDE---ALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAID 161


                 ..
gi 515998033 166 AN 167
Cdd:PRK13538 162 KQ 163
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
19-210 1.29e-17

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 83.68  E-value: 1.29e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  19 LQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVP---VNKRNFGFVFQSYALFPHLSVFDN 95
Cdd:PRK09700  21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDhklAAQLGIGIIYQELSVIDELTVLEN 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  96 VAFG-LRLRKVKEDDV------KRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLSNLdanl 168
Cdd:PRK09700 101 LYIGrHLTKKVCGVNIidwremRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSL---- 176

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 515998033 169 rVNMRVE-----IRRIQQElGITTVYVSHDQEECFSISDQVAIMNKG 210
Cdd:PRK09700 177 -TNKEVDylfliMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDG 221
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
 11-214 2.75e-17

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 82.97  E-value: 2.75e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  11 VAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLeAKQGTFLFGDKDYTRVPVN--KRNFGFVFQSYALFp 88
Cdd:PRK11174 358 LSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPEswRKHLSWVGQNPQLP- 435

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  89 HLSVFDNVAFGlrlrkvKEDDVKRRVMTMLDTVSLGGFEKRFP-------GE----LSGGQRQRVAIARALVIEPDLLLF 157
Cdd:PRK11174 436 HGTLRDNVLLG------NPDASDEQLQQALENAWVSEFLPLLPqgldtpiGDqaagLSVGQAQRLALARALLQPCQLLLL 509

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515998033 158 DEPLSNLDAnlrvnmRVEiRRIQQEL-----GITTVYVSH--DQEECFsisDQVAIMNKGNIEQ 214
Cdd:PRK11174 510 DEPTASLDA------HSE-QLVMQALnaasrRQTTLMVTHqlEDLAQW---DQIWVMQDGQIVQ 563
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
 18-212 3.12e-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: 78.84  E-value: 3.12e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  18 ILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAK---QGTFLFGDKDYTR-VPVNKRNFGFVFQSYALFPHLSVF 93
Cdd:cd03233   22 ILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEfAEKYPGEIIYVSEEDVHFPTLTVR 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  94 DNVAFGLRLRKvkeDDVKRRVmtmldtvslggfekrfpgelSGGQRQRVAIARALVIEPDLLLFDEPLSNLDANLRVNMR 173
Cdd:cd03233  102 ETLDFALRCKG---NEFVRGI--------------------SGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEIL 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 515998033 174 VEIRRIQQELGITTVyVSHDQ--EECFSISDQVAIMNKGNI 212
Cdd:cd03233  159 KCIRTMADVLKTTTF-VSLYQasDEIYDLFDKVLVLYEGRQ 198
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
 3-210 3.47e-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: 82.57  E-value: 3.47e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033    3 LLTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLeaKQGTFLfGDKDYTRVPVNKRN------ 76
Cdd:TIGR02633   1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY--PHGTWD-GEIYWSGSPLKASNirdter 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   77 --FGFVFQSYALFPHLSVFDNVAFG----LRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFP-GELSGGQRQRVAIARALV 149
Cdd:TIGR02633  78 agIVIIHQELTLVPELSVAENIFLGneitLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALN 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515998033  150 IEPDLLLFDEPLSNLDANlRVNMRVEIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKG 210
Cdd:TIGR02633 158 KQARLLILDEPSSSLTEK-ETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDG 217
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
 4-192 4.51e-17

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


Pssm-ID: 213190 [Multi-domain]  Cd Length: 166  Bit Score: 77.58  E-value: 4.51e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   4 LTLDRVSVAY-DNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFlfgdkdytRVPVNKRNFgFVFQ 82
Cdd:cd03223    1 IELENLSLATpDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI--------GMPEGEDLL-FLPQ 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  83 -SYalFPHLSVFDNVAFGLrlrkvkeDDVkrrvmtmldtvslggfekrfpgeLSGGQRQRVAIARALVIEPDLLLFDEPL 161
Cdd:cd03223   72 rPY--LPLGTLREQLIYPW-------DDV-----------------------LSGGEQQRLAFARLLLHKPKFVFLDEAT 119

                        170       180       190
                 ....*....|....*....|....*....|.
gi 515998033 162 SNLDanlrVNMRVEIRRIQQELGITTVYVSH 192
Cdd:cd03223  120 SALD----EESEDRLYQLLKELGITVISVGH 146
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
9-210 4.60e-17

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 81.03  E-value: 4.60e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   9 VSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTF-LFGDKDYTRVPVNKRNFGFVFQSYALF 87
Cdd:PRK13536  47 VSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKItVLGVPVPARARLARARIGVVPQFDNLD 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  88 PHLSVFDN-VAFGlRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLSNLDA 166
Cdd:PRK13536 127 LEFTVRENlLVFG-RYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDP 205

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 515998033 167 NLRvNMRVEIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKG 210
Cdd:PRK13536 206 HAR-HLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAG 248
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
 26-219 6.36e-17

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


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 82.02  E-value: 6.36e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   26 LERGQLLSLLGPSGCGKTTTLRLIAGFLEAkqGTFLFGDKDYTRVPVNKRNF----GFVFQSYALFPHLSVFDNVAFG-- 99
Cdd:TIGR00955  48 AKPGELLAVMGSSGAGKTTLMNALAFRSPK--GVKGSGSVLLNGMPIDAKEMraisAYVQQDDLFIPTLTVREHLMFQah 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  100 LRLRKVKEDDVKR-RVMTMLDTVSLG-------GFEKRFPGeLSGGQRQRVAIARALVIEPDLLLFDEPLSNLDAnlrvN 171
Cdd:TIGR00955 126 LRMPRRVTKKEKReRVDEVLQALGLRkcantriGVPGRVKG-LSGGERKRLAFASELLTDPPLLFCDEPTSGLDS----F 200

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 515998033  172 MRVEIRRIQQEL---GITTVYVSHD-QEECFSISDQVAIMNKGNIEQLDAPS 219
Cdd:TIGR00955 201 MAYSVVQVLKGLaqkGKTIICTIHQpSSELFELFDKIILMAEGRVAYLGSPD 252
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
 29-215 6.69e-17

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: 82.37  E-value: 6.69e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033    29 GQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKD-YTRVPVNKRNFGFVFQSYALFPHLSVFDNVAFGLRLRKVKE 107
Cdd:TIGR01257 1965 GECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSiLTNISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRGVPA 2044

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   108 DDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLSNLDANLRVNMRVEIRRIQQElGITT 187
Cdd:TIGR01257 2045 EEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAV 2123

                          170       180
                   ....*....|....*....|....*...
gi 515998033   188 VYVSHDQEECFSISDQVAIMNKGNIEQL 215
Cdd:TIGR01257 2124 VLTSHSMEECEALCTRLAIMVKGAFQCL 2151
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
1-263 1.33e-16

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 80.73  E-value: 1.33e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   1 MALLTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKdytrvPVNKRN---- 76
Cdd:PRK11288   2 SPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQ-----EMRFASttaa 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  77 ----FGFVFQSYALFPHLSVFDNVAFGL---RLRKVKEDDVKRRVMTMLDTVSLGgFEKRFP-GELSGGQRQRVAIARAL 148
Cdd:PRK11288  77 laagVAIIYQELHLVPEMTVAENLYLGQlphKGGIVNRRLLNYEAREQLEHLGVD-IDPDTPlKYLSIGQRQMVEIAKAL 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033 149 VIEPDLLLFDEPLSNLDA-NLRVNMRVeIRRIQQElGITTVYVSHDQEECFSISDQVAIMNKG-------NIEQLDAPST 220
Cdd:PRK11288 156 ARNARVIAFDEPTSSLSArEIEQLFRV-IRELRAE-GRVILYVSHRMEEIFALCDAITVFKDGryvatfdDMAQVDRDQL 233

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 515998033 221 IfkyptTEFVARFIGfnNFLSFDERTEEGERIRLN-------TGDLSFSV 263
Cdd:PRK11288 234 V-----QAMVGREIG--DIYGYRPRPLGEVRLRLDglkgpglREPISFSV 276
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
18-214 3.97e-16

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


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 79.37  E-value: 3.97e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  18 ILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVN--KRNFGFVFQSYALFPHlSVFDN 95
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDswRSRLAVVSQTPFLFSD-TVANN 408

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  96 VAFG------------LRLRKVKEDDVK-----------RRVMtmldtvslggfekrfpgeLSGGQRQRVAIARALVIEP 152
Cdd:PRK10789 409 IALGrpdatqqeiehvARLASVHDDILRlpqgydtevgeRGVM------------------LSGGQKQRISIARALLLNA 470

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515998033 153 DLLLFDEPLSNLDANLRVNMRVEIRRIQQElgiTTVYVSHDQEECFSISDQVAIMNKGNIEQ 214
Cdd:PRK10789 471 EILILDDALSAVDGRTEHQILHNLRQWGEG---RTVIISAHRLSALTEASEILVMQHGHIAQ 529
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
 4-212 4.92e-16

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: 75.64  E-value: 4.92e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   4 LTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGF--LEAKQGTFLFGDKDYTRVPVNKR---NFG 78
Cdd:cd03217    1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEERarlGIF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  79 FVFQSYALFPHLSVFDnvaFglrLRKVKEddvkrrvmtmldtvslgGFekrfpgelSGGQRQRVAIARALVIEPDLLLFD 158
Cdd:cd03217   81 LAFQYPPEIPGVKNAD---F---LRYVNE-----------------GF--------SGGEKKRNEILQLLLLEPDLAILD 129

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 515998033 159 EPLSNLDA-NLRVNMRVeIRRIQQElGITTVYVSHDQEEC-FSISDQVAIMNKGNI 212
Cdd:cd03217  130 EPDSGLDIdALRLVAEV-INKLREE-GKSVLIITHYQRLLdYIKPDRVHVLYDGRI 183
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
 18-224 6.42e-16

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


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 76.27  E-value: 6.42e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  18 ILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGtflfgdkdytRVPVNKR-----NFGFVFQsyalfPHLSV 92
Cdd:COG1134   41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSG----------RVEVNGRvsallELGAGFH-----PELTG 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  93 FDNVAFGLRLRKVKEDDVKRRVMTMLDTVSLGGFE----KRFpgelSGGQRQRVAIARALVIEPDLLLFDEPLSNLDANL 168
Cdd:COG1134  106 RENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIdqpvKTY----SSGMRARLAFAVATAVDPDILLVDEVLAVGDAAF 181

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033 169 RVNMRVEIRRIQQElGITTVYVSHD----QEECfsisDQVAIMNKGNIEQLDAPSTIFKY 224
Cdd:COG1134  182 QKKCLARIRELRES-GRTVIFVSHSmgavRRLC----DRAIWLEKGRLVMDGDPEEVIAA 236
PRK13543 PRK13543
heme ABC exporter ATP-binding protein CcmA;
2-165 1.25e-15

heme ABC exporter ATP-binding protein CcmA;


Pssm-ID: 184129 [Multi-domain]  Cd Length: 214  Bit Score: 74.89  E-value: 1.25e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   2 ALLTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPvNKRNFGFVF 81
Cdd:PRK13543  10 PLLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD-RSRFMAYLG 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  82 QSYALFPHLSVFDNVAF--GLRLRKVKeddvkRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDE 159
Cdd:PRK13543  89 HLPGLKADLSTLENLHFlcGLHGRRAK-----QMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDE 163


                 ....*.
gi 515998033 160 PLSNLD 165
Cdd:PRK13543 164 PYANLD 169
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
4-212 2.63e-15

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 74.92  E-value: 2.63e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   4 LTLDRVSVAYDN-QLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGtflfgDKDYTRVPVN---KRNF-G 78
Cdd:PRK15056   7 IVVNDVTVTWRNgHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASG-----KISILGQPTRqalQKNLvA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  79 FVFQSYAL---FPHLsVFDNVAFGLR-----LRKVKEDDvKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVI 150
Cdd:PRK15056  82 YVPQSEEVdwsFPVL-VEDVVMMGRYghmgwLRRAKKRD-RQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQ 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515998033 151 EPDLLLFDEPLSNLDANLRVNMRVEIRRIQQElGITTVYVSHDQEECFSISDqVAIMNKGNI 212
Cdd:PRK15056 160 QGQVILLDEPFTGVDVKTEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCD-YTVMVKGTV 219
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
 9-169 2.72e-15

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: 76.90  E-value: 2.72e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033    9 VSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKdytrVPVnkrnfGFVFQSY-ALF 87
Cdd:TIGR03719 328 LTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGET----VKL-----AYVDQSRdALD 398

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   88 PHLSVFDNVAFGLRLRKVKEDDVKRRVMtmldtVSLGGF-----EKRFpGELSGGQRQRVAIARALVIEPDLLLFDEPLS 162
Cdd:TIGR03719 399 PNKTVWEEISGGLDIIKLGKREIPSRAY-----VGRFNFkgsdqQKKV-GQLSGGERNRVHLAKTLKSGGNVLLLDEPTN 472


                  ....*...
gi 515998033  163 NLDAN-LR 169
Cdd:TIGR03719 473 DLDVEtLR 480
BtuD COG4138
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ...
 4-193 3.82e-15

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


Pssm-ID: 443313 [Multi-domain]  Cd Length: 248  Bit Score: 74.11  E-value: 3.82e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   4 LTLDRVSVAYDnqliLQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAkQGTFLFGDKDYTRVPVN----KRNFgF 79
Cdd:COG4138    1 LQLNDVAVAGR----LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPG-QGEILLNGRPLSDWSAAelarHRAY-L 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  80 VFQSYALFPhLSVFDNVAFGLRlRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALV-----IEPD- 153
Cdd:COG4138   75 SQQQSPPFA-MPVFQYLALHQP-AGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLqvwptINPEg 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 515998033 154 -LLLFDEPLSNLD-----ANLRVnmrveIRRIQQeLGITTVYVSHD 193
Cdd:COG4138  153 qLLLLDEPMNSLDvaqqaALDRL-----LRELCQ-QGITVVMSSHD 192
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
 13-192 3.99e-15

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127 [Multi-domain]  Cd Length: 200  Bit Score: 73.06  E-value: 3.99e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  13 YDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQG-TFLFGDKDYTRVPVNKRNFGFVFQSYALFPHLS 91
Cdd:PRK13540  11 YHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGeILFERQSIKKDLCTYQKQLCFVGHRSGINPYLT 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  92 VFDNVAFGLRLRKVKEDdvkrrvMTMLDTVSLGGFEKRFP-GELSGGQRQRVAIARALVIEPDLLLFDEPLSNLD--ANL 168
Cdd:PRK13540  91 LRENCLYDIHFSPGAVG------ITELCRLFSLEHLIDYPcGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDelSLL 164

                        170       180
                 ....*....|....*....|....
gi 515998033 169 RVNMRVEIRRIQqelGITTVYVSH 192
Cdd:PRK13540 165 TIITKIQEHRAK---GGAVLLTSH 185
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
 3-212 5.30e-15

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 75.83  E-value: 5.30e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   3 LLTLDRVSVA-YDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVNK-RNFGFV 80
Cdd:COG3845  257 VLEVENLSVRdDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRErRRLGVA 336

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  81 F-----QSYALFPHLSVFDNVAFG------------LRLRKVKEDdvKRRVMTMLDtVSLGGFEKRFpGELSGGQRQRVA 143
Cdd:COG3845  337 YipedrLGRGLVPDMSVAENLILGryrrppfsrggfLDRKAIRAF--AEELIEEFD-VRTPGPDTPA-RSLSGGNQQKVI 412

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515998033 144 IARALVIEPDLLLFDEPLSNLD--AnlrvnmrveIRRIQQEL------GITTVYVSHDQEECFSISDQVAIMNKGNI 212
Cdd:COG3845  413 LARELSRDPKLLIAAQPTRGLDvgA---------IEFIHQRLlelrdaGAAVLLISEDLDEILALSDRIAVMYEGRI 480
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
6-160 6.96e-15

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 75.93  E-value: 6.96e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   6 LDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTF--LFGD--KDYTRVPVNKR------ 75
Cdd:NF033858   4 LEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVevLGGDmaDARHRRAVCPRiaympq 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  76 ----NfgfvfqsyaLFPHLSVFDNVAFGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIE 151
Cdd:NF033858  84 glgkN---------LYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHD 154


                 ....*....
gi 515998033 152 PDLLLFDEP 160
Cdd:NF033858 155 PDLLILDEP 163
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
 19-210 1.14e-14

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 74.97  E-value: 1.14e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  19 LQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLE--AKQGTFLFGDKdytrvPVNKRNF------GFV--FQSYALFP 88
Cdd:PRK13549  21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPhgTYEGEIIFEGE-----ELQASNIrdteraGIAiiHQELALVK 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  89 HLSVFDNVAFGLRLRK---VKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLSNL- 164
Cdd:PRK13549  96 ELSVLENIFLGNEITPggiMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASLt 175

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 515998033 165 DANLRVNMRVeIRRIQQElGITTVYVSHDQEECFSISDQVAIMNKG 210
Cdd:PRK13549 176 ESETAVLLDI-IRDLKAH-GIACIYISHKLNEVKAISDTICVIRDG 219
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 3-193 1.43e-14

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: 74.82  E-value: 1.43e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   3 LLTLDRVSVAYDnqlilqDFDLQLERGQL-----LSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDK----------DY 67
Cdd:COG1245  341 LVEYPDLTKSYG------GFSLEVEGGEIregevLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKisykpqyispDY 414

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  68 T-RV-----PVNKRNFGfvfQSYalfphlsVFDNVAFGLRLRKVKEDDVKrrvmtmldtvslggfekrfpgELSGGQRQR 141
Cdd:COG1245  415 DgTVeeflrSANTDDFG---SSY-------YKTEIIKPLGLEKLLDKNVK---------------------DLSGGELQR 463

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 515998033 142 VAIARALVIEPDLLLFDEPLSNLDANLRVNMRVEIRRIQQELGITTVYVSHD 193
Cdd:COG1245  464 VAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHD 515
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
5-228 1.52e-14

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 72.51  E-value: 1.52e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   5 TLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKdytrvPVNKRNFGFVFQSY 84
Cdd:PRK10575  13 ALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQ-----PLESWSSKAFARKV 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  85 ALFPH-------LSVFDNVAFGL-----RLRKVKEDDvKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEP 152
Cdd:PRK10575  88 AYLPQqlpaaegMTVRELVAIGRypwhgALGRFGAAD-REKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDS 166

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515998033 153 DLLLFDEPLSNLDANLRVNMRVEIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNIEQLDAPSTIFKYPTTE 228
Cdd:PRK10575 167 RCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLE 242
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
3-166 2.09e-14

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 74.23  E-value: 2.09e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   3 LLTLDRVSVAYDNQL-ILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVN--KRNFGF 79
Cdd:PRK13657 334 AVEFDDVSFSYDNSRqGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRAslRRNIAV 413

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  80 VFQSYALFPHlSVFDNVAFGlrlrkvKEDDVKRRVMTMLDTVSLGGFEKRFP-------GE----LSGGQRQRVAIARAL 148
Cdd:PRK13657 414 VFQDAGLFNR-SIEDNIRVG------RPDATDEEMRAAAERAQAHDFIERKPdgydtvvGErgrqLSGGERQRLAIARAL 486

                        170
                 ....*....|....*...
gi 515998033 149 VIEPDLLLFDEPLSNLDA 166
Cdd:PRK13657 487 LKDPPILILDEATSALDV 504
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
 18-195 2.81e-14

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


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 71.14  E-value: 2.81e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  18 ILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQgtflfgDKDYTRVPVNkrNFGfvfqsyalfPHLSVFDNVA 97
Cdd:COG2401   45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTP------VAGCVDVPDN--QFG---------REASLIDAIG 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  98 fglrlrkvKEDDVKrRVMTMLDTVSLGG--FEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLSNLDAnlRVNMRV- 174
Cdd:COG2401  108 --------RKGDFK-DAVELLNAVGLSDavLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDR--QTAKRVa 176

                        170       180
                 ....*....|....*....|..
gi 515998033 175 -EIRRIQQELGITTVYVSHDQE 195
Cdd:COG2401  177 rNLQKLARRAGITLVVATHHYD 198
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
19-193 3.09e-14

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 73.69  E-value: 3.09e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  19 LQDFDLQLERGQL-----LSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDK----------DYTrVPV------NKRNF 77
Cdd:PRK13409 350 LGDFSLEVEGGEIyegevIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKisykpqyikpDYD-GTVedllrsITDDL 428

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  78 GfvfQSYalfphlsVFDNVAFGLRLRKVKEDDVKrrvmtmldtvslggfekrfpgELSGGQRQRVAIARALVIEPDLLLF 157
Cdd:PRK13409 429 G---SSY-------YKSEIIKPLQLERLLDKNVK---------------------DLSGGELQRVAIAACLSRDADLYLL 477

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 515998033 158 DEPLSNLDANLRVNMRVEIRRIQQELGITTVYVSHD 193
Cdd:PRK13409 478 DEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHD 513
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
4-165 3.92e-14

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 73.13  E-value: 3.92e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   4 LTLDRVSVAYD--NQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFL---FGDKDYTRVpvNKRN-F 77
Cdd:PRK11176 342 IEFRNVTFTYPgkEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILldgHDLRDYTLA--SLRNqV 419

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  78 GFVFQSYALFpHLSVFDNVAFGLRLRKVKEDDVKRRVMT--M---------LDTVSlggfekrfpGE----LSGGQRQRV 142
Cdd:PRK11176 420 ALVSQNVHLF-NDTIANNIAYARTEQYSREQIEEAARMAyaMdfinkmdngLDTVI---------GEngvlLSGGQRQRI 489

                        170       180
                 ....*....|....*....|...
gi 515998033 143 AIARALVIEPDLLLFDEPLSNLD 165
Cdd:PRK11176 490 AIARALLRDSPILILDEATSALD 512
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
20-215 5.18e-14

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 72.89  E-value: 5.18e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  20 QDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGT-FLFGDKDYTRVPVN--KRNFGFVFQSY---ALFPHLSVF 93
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEiRLNGKDISPRSPLDavKKGMAYITESRrdnGFFPNFSIA 359

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  94 DNVAFGLRLRK---------VKEDDVKRRVMTMLDTVSL--GGFEKRFpGELSGGQRQRVAIARALVIEPDLLLFDEPLS 162
Cdd:PRK09700 360 QNMAISRSLKDggykgamglFHEVDEQRTAENQRELLALkcHSVNQNI-TELSGGNQQKVLISKWLCCCPEVIIFDEPTR 438

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 515998033 163 NLDanlrVNMRVEIRRIQQEL---GITTVYVSHDQEECFSISDQVAIMNKGNIEQL 215
Cdd:PRK09700 439 GID----VGAKAEIYKVMRQLaddGKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
 6-195 5.58e-14

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 73.06  E-value: 5.58e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   6 LDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGdkdyTRVPVNkrnfgfVFQSY- 84
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCG----TKLEVA------YFDQHr 391

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  85 -ALFPHLSVFDNVAFGlrLRKVKEDDVKRRVMTMLDTVSLGGFEKRFP-GELSGGQRQRVAIARALVIEPDLLLFDEPLS 162
Cdd:PRK11147 392 aELDPEKTVMDNLAEG--KQEVMVNGRPRHVLGYLQDFLFHPKRAMTPvKALSGGERNRLLLARLFLKPSNLLILDEPTN 469

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 515998033 163 NLDanlrvnmrVEIRRIQQEL-----GiTTVYVSHDQE 195
Cdd:PRK11147 470 DLD--------VETLELLEELldsyqG-TVLLVSHDRQ 498
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
 18-165 6.87e-14

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: 71.04  E-value: 6.87e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  18 ILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFlfgdKDYTRVpvnkrnfGFVFQSYALFPHlSVFDNVA 97
Cdd:cd03291   52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI----KHSGRI-------SFSSQFSWIMPG-TIKENII 119

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515998033  98 FGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGE----LSGGQRQRVAIARALVIEPDLLLFDEPLSNLD 165
Cdd:cd03291  120 FGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFGYLD 191
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
 18-165 9.40e-14

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: 72.64  E-value: 9.40e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033    18 ILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFlfgdKDYTRVpvnkrnfGFVFQSYALFPHlSVFDNVA 97
Cdd:TIGR01271  441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI----KHSGRI-------SFSPQTSWIMPG-TIKDNII 508

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515998033    98 FGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGE----LSGGQRQRVAIARALVIEPDLLLFDEPLSNLD 165
Cdd:TIGR01271  509 FGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFTHLD 580
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
 1-225 1.28e-13

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 70.54  E-value: 1.28e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   1 MALLTLDRVSVAY-DNQLILQDFD---LQLERGQLLSLLGPSGCGKTTTLRLIAGFLE------AKQgtFLFGDKDYTRV 70
Cdd:PRK11022   1 MALLNVDKLSVHFgDESAPFRAVDrisYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDypgrvmAEK--LEFNGQDLQRI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  71 PVNKR------NFGFVFQS--YALFPHLSVFDNVAFGLrlrKVKEDDVKR----RVMTMLDTVSLGGFEKR---FPGELS 135
Cdd:PRK11022  79 SEKERrnlvgaEVAMIFQDpmTSLNPCYTVGFQIMEAI---KVHQGGNKKtrrqRAIDLLNQVGIPDPASRldvYPHQLS 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033 136 GGQRQRVAIARALVIEPDLLLFDEPLSNLDANLRVNMRVEIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNIEQL 215
Cdd:PRK11022 156 GGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVET 235

                        250
                 ....*....|
gi 515998033 216 DAPSTIFKYP 225
Cdd:PRK11022 236 GKAHDIFRAP 245
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
 5-166 1.31e-13

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


Pssm-ID: 274744 [Multi-domain]  Cd Length: 552  Bit Score: 71.50  E-value: 1.31e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033    5 TLDRVSVAYD-NQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFleakqgtflfgDKDYT--RVPVNKRNFGFVF 81
Cdd:TIGR03719   6 TMNRVSKVVPpKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV-----------DKDFNgeARPQPGIKVGYLP 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   82 QSYALFPHLSVFDNVAFGLRlrkVKEDDVKR-----------------------RVMTMLDTVSLGGFEKRF-------- 130
Cdd:TIGR03719  75 QEPQLDPTKTVRENVEEGVA---EIKDALDRfneisakyaepdadfdklaaeqaELQEIIDAADAWDLDSQLeiamdalr 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 515998033  131 --PGE-----LSGGQRQRVAIARALVIEPDLLLFDEPLSNLDA 166
Cdd:TIGR03719 152 cpPWDadvtkLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDA 194
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
 19-240 1.43e-13

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: 71.90  E-value: 1.43e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033    19 LQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFgdkdytrvpvnKRNFGFVFQSyALFPHLSVFDNVAF 98
Cdd:TIGR00957  654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHM-----------KGSVAYVPQQ-AWIQNDSLRENILF 721

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033    99 GLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGE----LSGGQRQRVAIARALVIEPDLLLFDEPLSNLDANLRVNMRV 174
Cdd:TIGR00957  722 GKALNEKYYQQVLEACALLPDLEILPSGDRTEIGEkgvnLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFE 801

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515998033   175 EIRRIQQEL-GITTVYVSHdqeecfSIS-----DQVAIMNKGNIEQLDApstifkYPttEFVARFIGFNNFL 240
Cdd:TIGR00957  802 HVIGPEGVLkNKTRILVTH------GISylpqvDVIIVMSGGKISEMGS------YQ--ELLQRDGAFAEFL 859
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 26-207 1.95e-13

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: 71.35  E-value: 1.95e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  26 LERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGtflfgdkDYTRVP----VNKRnfgfvFQSYALFPHLS---------- 91
Cdd:COG1245   96 PKKGKVTGILGPNGIGKSTALKILSGELKPNLG-------DYDEEPswdeVLKR-----FRGTELQDYFKklangeikva 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  92 -----------VFDNVAFGLrLRKVKEDDVKRRVMTMLDtvsLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEP 160
Cdd:COG1245  164 hkpqyvdlipkVFKGTVREL-LEKVDERGKLDELAEKLG---LENILDRDISELSGGELQRVAIAAALLRDADFYFFDEP 239

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 515998033 161 LSNLDANLRVNMRVEIRRIQQElGITTVYVSHDQEECFSISDQVAIM 207
Cdd:COG1245  240 SSYLDIYQRLNVARLIRELAEE-GKYVLVVEHDLAILDYLADYVHIL 285
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
4-192 2.40e-13

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


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 70.90  E-value: 2.40e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   4 LTLDRVSVAY-DNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKdytrvPVNKRNFGFVFQ 82
Cdd:PRK10790 341 IDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGR-----PLSSLSHSVLRQ 415

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  83 SYALF---PHL---SVFDNVAFGlrlRKVKEDdvkrRVMTMLDTVSLGGFEKRFP-------GE----LSGGQRQRVAIA 145
Cdd:PRK10790 416 GVAMVqqdPVVladTFLANVTLG---RDISEE----QVWQALETVQLAELARSLPdglytplGEqgnnLSVGQKQLLALA 488

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 515998033 146 RALVIEPDLLLFDEPLSNLDANLRvnmrveiRRIQQELGI-----TTVYVSH 192
Cdd:PRK10790 489 RVLVQTPQILILDEATANIDSGTE-------QAIQQALAAvrehtTLVVIAH 533
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
 29-193 2.81e-13

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: 68.93  E-value: 2.81e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  29 GQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLfGDKDYTRVPVNKRnfGFVFQSY------------------ALFPHl 90
Cdd:cd03236   26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGKFD-DPPDWDEILDEFR--GSELQNYftkllegdvkvivkpqyvDLIPK- 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  91 SVFDNVafGLRLRKVKEDDVKRRVMtmlDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLSNLDANLRV 170
Cdd:cd03236  102 AVKGKV--GELLKKKDERGKLDELV---DQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRL 176

                        170       180
                 ....*....|....*....|...
gi 515998033 171 NMRVEIRRIQQElGITTVYVSHD 193
Cdd:cd03236  177 NAARLIRELAED-DNYVLVVEHD 198
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
 1-165 3.61e-13

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 70.36  E-value: 3.61e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   1 MALLTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLF-GDKDYTRV----PVNKR 75
Cdd:PRK11147   1 MSLISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYeQDLIVARLqqdpPRNVE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  76 NfgfvfqsyalfphlSVFDNVAFGLR------------LRKVKEDDVKR------RVMTMLDTVSLGGFEKRFP------ 131
Cdd:PRK11147  81 G--------------TVYDFVAEGIEeqaeylkryhdiSHLVETDPSEKnlnelaKLQEQLDHHNLWQLENRINevlaql 146

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 515998033 132 --------GELSGGQRQRVAIARALVIEPDLLLFDEPLSNLD 165
Cdd:PRK11147 147 gldpdaalSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD 188
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
26-193 3.95e-13

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 70.22  E-value: 3.95e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  26 LERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFlfgDKDYTRVPVNKRNFGFVFQSYalFPHLS-------------- 91
Cdd:PRK13409  96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDY---EEEPSWDEVLKRFRGTELQNY--FKKLYngeikvvhkpqyvd 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  92 ----VFDNVAFGLrLRKVKEDDVKRRVMTMLDtvsLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLSNLDAN 167
Cdd:PRK13409 171 lipkVFKGKVREL-LKKVDERGKLDEVVERLG---LENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIR 246

                        170       180
                 ....*....|....*....|....*.
gi 515998033 168 LRVNMRVEIRRIQQelGITTVYVSHD 193
Cdd:PRK13409 247 QRLNVARLIRELAE--GKYVLVVEHD 270
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
 19-192 4.39e-13

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: 67.74  E-value: 4.39e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  19 LQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPV------NKRNFGFVFQSYALFpHLSV 92
Cdd:cd03290   17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFeatrsrNRYSVAYAAQKPWLL-NATV 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  93 FDNVAFGLRLRKvkeddvkRRVMTMLDTVSLGGFEKRFP-------GE----LSGGQRQRVAIARALVIEPDLLLFDEPL 161
Cdd:cd03290   96 EENITFGSPFNK-------QRYKAVTDACSLQPDIDLLPfgdqteiGErginLSGGQRQRICVARALYQNTNIVFLDDPF 168

                        170       180       190
                 ....*....|....*....|....*....|..
gi 515998033 162 SNLDANLRVN-MRVEIRRIQQELGITTVYVSH 192
Cdd:cd03290  169 SALDIHLSDHlMQEGILKFLQDDKRTLVLVTH 200
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
 4-195 4.68e-13

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 69.92  E-value: 4.68e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   4 LTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDkdytrvpvnKRNFGFVFQ- 82
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSE---------NANIGYYAQd 390

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  83 SYALFPH-LSVFDNVAfglRLRKVKEDDVKRRvmTMLDTVSLGGFE-KRFPGELSGGQRQRVAIARALVIEPDLLLFDEP 160
Cdd:PRK15064 391 HAYDFENdLTLFDWMS---QWRQEGDDEQAVR--GTLGRLLFSQDDiKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEP 465

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 515998033 161 LSNLDanlrvnMRvEIRRIQQELGI---TTVYVSHDQE 195
Cdd:PRK15064 466 TNHMD------ME-SIESLNMALEKyegTLIFVSHDRE 496
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
 19-210 8.60e-13

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 68.99  E-value: 8.60e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  19 LQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKdytrvPVNKRN--------FGFVFQSYALFPHL 90
Cdd:PRK10982  14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGK-----EIDFKSskealengISMVHQELNLVLQR 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  91 SVFDNVAFGLRLRK---VKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLSNLDAN 167
Cdd:PRK10982  89 SVMDNMWLGRYPTKgmfVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEK 168

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 515998033 168 lRVNMRVEIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKG 210
Cdd:PRK10982 169 -EVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDG 210
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
 18-218 1.46e-12

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: 65.90  E-value: 1.46e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  18 ILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVNK--RNFGFVFQSYALFP-----HL 90
Cdd:cd03369   23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDlrSSLTIIPQDPTLFSgtirsNL 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  91 SVFDnvafglrlrkvKEDDVKrrVMTMLdTVSLGGFEkrfpgeLSGGQRQRVAIARALVIEPDLLLFDEPLSNLDanlrV 170
Cdd:cd03369  103 DPFD-----------EYSDEE--IYGAL-RVSEGGLN------LSQGQRQLLCLARALLKRPRVLVLDEATASID----Y 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 515998033 171 NMRVEIRRIQQEL--GITTVYVSHDQEecfSIS--DQVAIMNKGNIEQLDAP 218
Cdd:cd03369  159 ATDALIQKTIREEftNSTILTIAHRLR---TIIdyDKILVMDAGEVKEYDHP 207
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
 75-208 1.84e-12

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 68.52  E-value: 1.84e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   75 RN-FGFVFQSYALFpHLSVFDNVAFGlrlrkvKEDDVKRRVMTMLDTVSLGGFEKRFPGE-----------LSGGQRQRV 142
Cdd:PTZ00265 1295 RNlFSIVSQEPMLF-NMSIYENIKFG------KEDATREDVKRACKFAAIDEFIESLPNKydtnvgpygksLSGGQKQRI 1367

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515998033  143 AIARALVIEPDLLLFDEPLSNLDANLRVNMRVEIRRIQQELGITTVYVSHdQEECFSISDQVAIMN 208
Cdd:PTZ00265 1368 AIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH-RIASIKRSDKIVVFN 1432
hmuV PRK13547
heme ABC transporter ATP-binding protein;
3-236 1.90e-12

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 66.77  E-value: 1.90e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   3 LLTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFL---EAKQGTFLFGDKDYTRVPV------- 72
Cdd:PRK13547   1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtggGAPRGARVTGDVTLNGEPLaaidapr 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  73 -----------NKRNFGFVFQSYAL---FPHlsvfdnvAFGLRLRKVKEDDVKRRVMTMLDTVSLGGfekRFPGELSGGQ 138
Cdd:PRK13547  81 larlravlpqaAQPAFAFSAREIVLlgrYPH-------ARRAGALTHRDGEIAWQALALAGATALVG---RDVTTLSGGE 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033 139 RQRVAIARAL---------VIEPDLLLFDEPLSNLDANLRVNMRVEIRRIQQELGITTVYVSHDQEECFSISDQVAIMNK 209
Cdd:PRK13547 151 LARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLAD 230

                        250       260
                 ....*....|....*....|....*..
gi 515998033 210 GNIEQLDAPSTIFkypTTEFVARFIGF 236
Cdd:PRK13547 231 GAIVAHGAPADVL---TPAHIARCYGF 254
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
 21-212 3.01e-12

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 67.34  E-value: 3.01e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  21 DFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTF-LFGDKDYTRVPVNKRNFGFVFQSY-----ALFPHLSVFD 94
Cdd:PRK10762 270 DVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVtLDGHEVVTRSPQDGLANGIVYISEdrkrdGLVLGMSVKE 349

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  95 NVA---------FGLRLRKVKEddvkrrVMTMLDTVSLggFEKRFP------GELSGGQRQRVAIARALVIEPDLLLFDE 159
Cdd:PRK10762 350 NMSltalryfsrAGGSLKHADE------QQAVSDFIRL--FNIKTPsmeqaiGLLSGGNQQKVAIARGLMTRPKVLILDE 421

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 515998033 160 PLSNLDANLRVNMRVEIRRIQQElGITTVYVSHDQEECFSISDQVAIMNKGNI 212
Cdd:PRK10762 422 PTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGRI 473
SufC COG0396
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ...
 4-165 4.42e-12

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


Pssm-ID: 440165 [Multi-domain]  Cd Length: 245  Bit Score: 65.09  E-value: 4.42e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   4 LTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGF--LEAKQGTFLFGDKDYTRVPVNKR---NFG 78
Cdd:COG0396    1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDILELSPDERaraGIF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  79 FVFQSYALFPHLSVFD--NVAFG-LRLRKVKEDDVKRRVMTMLDTVSLG-GFEKRFPGE-LSGGQRQRVAIARALVIEPD 153
Cdd:COG0396   81 LAFQYPVEIPGVSVSNflRTALNaRRGEELSAREFLKLLKEKMKELGLDeDFLDRYVNEgFSGGEKKRNEILQMLLLEPK 160

                        170
                 ....*....|..
gi 515998033 154 LLLFDEPLSNLD 165
Cdd:COG0396  161 LAILDETDSGLD 172
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
 19-193 5.75e-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: 64.74  E-value: 5.75e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  19 LQDFDLQLE-----RGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGtflfgDKDYTRVPVnkrnfgfvfqSY------ALF 87
Cdd:cd03237   10 LGEFTLEVEggsisESEVIGILGPNGIGKTTFIKMLAGVLKPDEG-----DIEIELDTV----------SYkpqyikADY 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  88 PhlSVFDNVAFGLRLRKVKEDDVKRRVMTMLDTVSLggFEKRFPgELSGGQRQRVAIARALVIEPDLLLFDEPLSNLDAN 167
Cdd:cd03237   75 E--GTVRDLLSSITKDFYTHPYFKTEIAKPLQIEQI--LDREVP-ELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVE 149

                        170       180
                 ....*....|....*....|....*.
gi 515998033 168 LRVNMRVEIRRIQQELGITTVYVSHD 193
Cdd:cd03237  150 QRLMASKVIRRFAENNEKTAFVVEHD 175
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
 21-213 6.14e-12

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


Pssm-ID: 131681 [Multi-domain]  Cd Length: 500  Bit Score: 66.39  E-value: 6.14e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   21 DFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAK-QGTFLFGDKdytrvPVNKRN-FGFVFQSYALFPH--------- 89
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGK-----PVDIRNpAQAIRAGIAMVPEdrkrhgivp 352

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   90 ---------LSVFDNVAFGLRLRKVKEDDVKRRVMTMLdtvSLGGFEKRFP-GELSGGQRQRVAIARALVIEPDLLLFDE 159
Cdd:TIGR02633 353 ilgvgknitLSVLKSFCFKMRIDAAAELQIIGSAIQRL---KVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDE 429

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 515998033  160 PLSNLDanlrVNMRVEIRRIQQEL---GITTVYVSHDQEECFSISDQVAIMNKGNIE 213
Cdd:TIGR02633 430 PTRGVD----VGAKYEIYKLINQLaqeGVAIIVVSSELAEVLGLSDRVLVIGEGKLK 482
PRK10522 PRK10522
multidrug transporter membrane component/ATP-binding component; Provisional
 4-216 9.59e-12

multidrug transporter membrane component/ATP-binding component; Provisional


Pssm-ID: 236707 [Multi-domain]  Cd Length: 547  Bit Score: 65.76  E-value: 9.59e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   4 LTLDRVSVAY-DNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKdytrvPVNKRN------ 76
Cdd:PRK10522 323 LELRNVTFAYqDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGK-----PVTAEQpedyrk 397

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  77 -FGFVFQSYALFPHLsvfdnvafglrLRKVKEDDVKRRVMTMLDTVSLGgfEK-RFPGE------LSGGQRQRVAIARAL 148
Cdd:PRK10522 398 lFSAVFTDFHLFDQL-----------LGPEGKPANPALVEKWLERLKMA--HKlELEDGrisnlkLSKGQKKRLALLLAL 464

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515998033 149 VIEPDLLLFDEPLSNLDANLRVNMRVEIRRIQQELGITTVYVSHDqEECFSISDQVAIMNKGNIEQLD 216
Cdd:PRK10522 465 AEERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQLSELT 531
ABCG_PDR_domain2 cd03232
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...
 9-166 1.24e-11

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


Pssm-ID: 213199 [Multi-domain]  Cd Length: 192  Bit Score: 63.03  E-value: 1.24e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   9 VSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAK--QGTFLF----GDKDYTRVpvnkrnFGFVFQ 82
Cdd:cd03232   13 VPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILIngrpLDKNFQRS------TGYVEQ 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  83 SYALFPHLSVFDNVAFGLRLRkvkeddvkrrvmtmldtvslggfekrfpgELSGGQRQRVAIARALVIEPDLLLFDEPLS 162
Cdd:cd03232   87 QDVHSPNLTVREALRFSALLR-----------------------------GLSVEQRKRLTIGVELAAKPSILFLDEPTS 137


                 ....
gi 515998033 163 NLDA 166
Cdd:cd03232  138 GLDS 141
PTZ00243 PTZ00243
ABC transporter; Provisional
 18-213 1.58e-11

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 65.57  E-value: 1.58e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   18 ILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLfgdkdytrvpvNKRNFGFVFQSyALFPHLSVFDNVA 97
Cdd:PTZ00243  675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW-----------AERSIAYVPQQ-AWIMNATVRGNIL 742

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   98 FGLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGE----LSGGQRQRVAIARALVIEPDLLLFDEPLSNLDANLRvnmr 173
Cdd:PTZ00243  743 FFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEkgvnLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVG---- 818

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 515998033  174 veiRRIQQEL------GITTVYVSHdQEECFSISDQVAIMNKGNIE 213
Cdd:PTZ00243  819 ---ERVVEECflgalaGKTRVLATH-QVHVVPRADYVVALGDGRVE 860
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
 2-196 2.08e-11

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 64.65  E-value: 2.08e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   2 ALLTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGflEAKQG----TFLFGDK------------ 65
Cdd:PRK10938 259 PRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG--DHPQGysndLTLFGRRrgsgetiwdikk 336

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  66 -----------DYtRVPVNKRNF---GFvFQSYALFPHLSvfDnvafglRLRKVkeddvkrrVMTMLDTVSLGGFEKRFP 131
Cdd:PRK10938 337 higyvssslhlDY-RVSTSVRNVilsGF-FDSIGIYQAVS--D------RQQKL--------AQQWLDILGIDKRTADAP 398

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033 132 -GELSGGQRQRVAIARALVIEPDLLLFDEPLSNLDAnlrVNmRVEIRRIQQEL---GITT-VYVSHDQEE 196
Cdd:PRK10938 399 fHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDP---LN-RQLVRRFVDVLiseGETQlLFVSHHAED 464
PLN03232 PLN03232
ABC transporter C family member; Provisional
 19-294 2.08e-11

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 65.38  E-value: 2.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   19 LQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLfgdkdytrvpVNKRNFGFVFQSYALFpHLSVFDNVAF 98
Cdd:PLN03232  633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSV----------VIRGSVAYVPQVSWIF-NATVRENILF 701

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   99 GlrlrkvkEDDVKRRVMTMLDTVSLGGFEKRFPGE-----------LSGGQRQRVAIARALVIEPDLLLFDEPLSNLDAN 167
Cdd:PLN03232  702 G-------SDFESERYWRAIDVTALQHDLDLLPGRdlteigergvnISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAH 774

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  168 lrVNMRVEIRRIQQEL-GITTVYVShDQEECFSISDQV------AIMNKGNIEQLDAPSTIFKYPttefvarfigFNNFL 240
Cdd:PLN03232  775 --VAHQVFDSCMKDELkGKTRVLVT-NQLHFLPLMDRIilvsegMIKEEGTFAELSKSGSLFKKL----------MENAG 841

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 515998033  241 SFDERTEEGERIRlNTGDLSFSVVRNQGTVQPGARQGAIRPDDLVIRTEGNETG 294
Cdd:PLN03232  842 KMDATQEVNTNDE-NILKLGPTVTIDVSERNLGSTKQGKRGRSVLVKQEERETG 894
PLN03130 PLN03130
ABC transporter C family member; Provisional
 19-223 3.17e-11

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 64.76  E-value: 3.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   19 LQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLfgdkdytrvpVNKRNFGFVFQSYALFpHLSVFDNVAF 98
Cdd:PLN03130  633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASV----------VIRGTVAYVPQVSWIF-NATVRDNILF 701

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   99 GLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGE----LSGGQRQRVAIARALVIEPDLLLFDEPLSNLDANlrVNMRV 174
Cdd:PLN03130  702 GSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGErgvnISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAH--VGRQV 779

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 515998033  175 EIRRIQQELGITTVYVSHDQEECFSISDQV------AIMNKGNIEQLDAPSTIFK 223
Cdd:PLN03130  780 FDKCIKDELRGKTRVLVTNQLHFLSQVDRIilvhegMIKEEGTYEELSNNGPLFQ 834
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
 9-169 3.68e-11

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 63.98  E-value: 3.68e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   9 VSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKdytrVPVnkrnfGFVFQSY-ALF 87
Cdd:PRK11819 330 LSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGET----VKL-----AYVDQSRdALD 400

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  88 PHLSVFDNVAFGlrlrkvkeddvkrrvmtmLDTVSLGGFE-------KRF----------PGELSGGQRQRVAIARALVI 150
Cdd:PRK11819 401 PNKTVWEEISGG------------------LDIIKVGNREipsrayvGRFnfkggdqqkkVGVLSGGERNRLHLAKTLKQ 462

                        170       180
                 ....*....|....*....|
gi 515998033 151 EPDLLLFDEPLSNLDAN-LR 169
Cdd:PRK11819 463 GGNVLLLDEPTNDLDVEtLR 482
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
 11-210 4.18e-11

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 62.26  E-value: 4.18e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  11 VAYDNQLIlqDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKqGTFLFGDKDYTRVPVNK--RNFGFVFQSYALFP 88
Cdd:PRK03695   6 VAVSTRLG--PLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGS-GSIQFAGQPLEAWSAAElaRHRAYLSQQQTPPF 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  89 HLSVFDNVAFGLRlRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARA-LVIEPD------LLLFDEPL 161
Cdd:PRK03695  83 AMPVFQYLTLHQP-DKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVvLQVWPDinpagqLLLLDEPM 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 515998033 162 SNLDANLRVNMRVEIRRIQQeLGITTVYVSHDQEECFSISDQVAIMNKG 210
Cdd:PRK03695 162 NSLDVAQQAALDRLLSELCQ-QGIAVVMSSHDLNHTLRHADRVWLLKQG 209
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
 29-210 5.11e-11

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 63.48  E-value: 5.11e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  29 GQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDytrvpvnkRNF-----------GFVFQSYALFPHLSVFDNVA 97
Cdd:PRK10762  30 GRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKE--------VTFngpkssqeagiGIIHQELNLIPQLTIAENIF 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  98 FGL----RLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLSNL-DANLRVNM 172
Cdd:PRK10762 102 LGRefvnRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTETESLF 181

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 515998033 173 RVeIRRIQ-QELGIttVYVSHDQEECFSISDQVAIMNKG 210
Cdd:PRK10762 182 RV-IRELKsQGRGI--VYISHRLKEIFEICDDVTVFRDG 217
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
 21-212 1.06e-10

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 62.76  E-value: 1.06e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  21 DFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYT-RVPVNKRNFGFVF-----QSYALFPHLSVFD 94
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINaLSTAQRLARGLVYlpedrQSSGLYLDAPLAW 360

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  95 NVA------FGLRLRKVKEDDVKRRVMTMLDtVSLGGFEKRFpGELSGGQRQRVAIARALVIEPDLLLFDEPLSNLDANL 168
Cdd:PRK15439 361 NVCalthnrRGFWIKPARENAVLERYRRALN-IKFNHAEQAA-RTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSA 438

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 515998033 169 RVNMRVEIRRIQQElGITTVYVSHDQEECFSISDQVAIMNKGNI 212
Cdd:PRK15439 439 RNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEI 481
PLN03140 PLN03140
ABC transporter G family member; Provisional
 11-210 1.83e-10

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 62.56  E-value: 1.83e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   11 VAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGfleAKQGTFLFGDKDYTRVPVNKRNF----GFVFQSYAL 86
Cdd:PLN03140  888 VTEDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG---RKTGGYIEGDIRISGFPKKQETFarisGYCEQNDIH 964

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   87 FPHLSVFDNVAFG--LRLRKVKEDDVKRR----VMTMLDTVSLGGFEKRFPG--ELSGGQRQRVAIARALVIEPDLLLFD 158
Cdd:PLN03140  965 SPQVTVRESLIYSafLRLPKEVSKEEKMMfvdeVMELVELDNLKDAIVGLPGvtGLSTEQRKRLTIAVELVANPSIIFMD 1044

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 515998033  159 EPLSNLDAN-LRVNMRVEirRIQQELGITTVYVSHDQE-ECFSISDQVAIMNKG 210
Cdd:PLN03140 1045 EPTSGLDARaAAIVMRTV--RNTVDTGRTVVCTIHQPSiDIFEAFDELLLMKRG 1096
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
 3-216 2.00e-10

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 62.11  E-value: 2.00e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   3 LLTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGdKDYTRVPVNKRNFGFVFQ 82
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLA-KGIKLGYFAQHQLEFLRA 390

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  83 SYALFPHLSvfdnvafglRLRKvKEDDVKRRVMtmldtvsLGGFEkrFPGE--------LSGGQRQRVAIARALVIEPDL 154
Cdd:PRK10636 391 DESPLQHLA---------RLAP-QELEQKLRDY-------LGGFG--FQGDkvteetrrFSGGEKARLVLALIVWQRPNL 451

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515998033 155 LLFDEPLSNLDanlrVNMRVEIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNIEQLD 216
Cdd:PRK10636 452 LLLDEPTNHLD----LDMRQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVEPFD 509
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
 15-210 2.66e-10

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 61.28  E-value: 2.66e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  15 NQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTF-LFGDKDYTRVPVNKRNFGFVF-----QSYALFP 88
Cdd:PRK10982 260 RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTItLHGKKINNHNANEAINHGFALvteerRSTGIYA 339

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  89 HLSV-FDNV---------AFGLRLRKVKEDDVKRRVMTM-LDTVSlggfEKRFPGELSGGQRQRVAIARALVIEPDLLLF 157
Cdd:PRK10982 340 YLDIgFNSLisnirnyknKVGLLDNSRMKSDTQWVIDSMrVKTPG----HRTQIGSLSGGNQQKVIIGRWLLTQPEILML 415

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 515998033 158 DEPLSNLDanlrVNMRVEIRRIQQEL-----GIttVYVSHDQEECFSISDQVAIMNKG 210
Cdd:PRK10982 416 DEPTRGID----VGAKFEIYQLIAELakkdkGI--IIISSEMPELLGITDRILVMSNG 467
PvdE COG4615
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...
 4-219 3.03e-10

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: 61.35  E-value: 3.03e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   4 LTLDRVSVAY-----DNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKdytrvPVNKRN-- 76
Cdd:COG4615  328 LELRGVTYRYpgedgDEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQ-----PVTADNre 402

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  77 -----FGFVFQSYALFPHLSVFDNVAfglrlrkvkEDDVKRRVMTMLD-----TVSLGGFEKRfpgELSGGQRQRVAIAR 146
Cdd:COG4615  403 ayrqlFSAVFSDFHLFDRLLGLDGEA---------DPARARELLERLEldhkvSVEDGRFSTT---DLSQGQRKRLALLV 470

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515998033 147 ALVIEPDLLLFDEPLSNLDANLRvnmRVEIRRIQQEL---GITTVYVSHDqEECFSISDQVAIMNKGNIEQLDAPS 219
Cdd:COG4615  471 ALLEDRPILVFDEWAADQDPEFR---RVFYTELLPELkarGKTVIAISHD-DRYFDLADRVLKMDYGKLVELTGPA 542
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
 7-218 3.67e-10

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: 59.04  E-value: 3.67e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   7 DRVSVAY--DNQLILQDFDLQLERGQLLSLLGPSGCGKTTT----LRLIagflEAKQGTFLFGDKDYTRVPVNK--RNFG 78
Cdd:cd03244    6 KNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLllalFRLV----ELSSGSILIDGVDISKIGLHDlrSRIS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  79 FVFQSYALFPHlSVFDNVA-FGLR--------LRKVKeddVKRRVMTM---LDT-VSLGGfekrfpGELSGGQRQRVAIA 145
Cdd:cd03244   82 IIPQDPVLFSG-TIRSNLDpFGEYsdeelwqaLERVG---LKEFVESLpggLDTvVEEGG------ENLSVGQRQLLCLA 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033 146 RALVIEPDLLLFDEPLSNLDanlrvnMRVEiRRIQQEL-----GITTVYVSHDQEecfSI--SDQVAIMNKGNIEQLDAP 218
Cdd:cd03244  152 RALLRKSKILVLDEATASVD------PETD-ALIQKTIreafkDCTVLTIAHRLD---TIidSDRILVLDKGRVVEFDSP 221
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
 9-166 6.01e-10

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


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 60.89  E-value: 6.01e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033     9 VSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAkqGTFLFGDKDYTRVPVNK---RNFGFVFQSYA 85
Cdd:TIGR00956  769 VKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTT--GVITGGDRLVNGRPLDSsfqRSIGYVQQQDL 846

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033    86 LFPHLSVFDNVAFGLRLRKVKE------DDVKRRVMTMLDTVSLGGFEKRFPGE-LSGGQRQRVAIARALVIEPDLLLF- 157
Cdd:TIGR00956  847 HLPTSTVRESLRFSAYLRQPKSvsksekMEYVEEVIKLLEMESYADAVVGVPGEgLNVEQRKRLTIGVELVAKPKLLLFl 926


                   ....*....
gi 515998033   158 DEPLSNLDA 166
Cdd:TIGR00956  927 DEPTSGLDS 935
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
 26-212 2.01e-09

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 58.79  E-value: 2.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  26 LERGQLLSLLGPSGCGKTTTLRLIAG-FLEAKQGT-FLFGDKDYTR------------VPVNKRNFGFVFQ-SYALFPHL 90
Cdd:PRK13549 285 LRRGEILGIAGLVGAGRTELVQCLFGaYPGRWEGEiFIDGKPVKIRnpqqaiaqgiamVPEDRKRDGIVPVmGVGKNITL 364

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  91 SVFDNVAFGLRLRKVKEDDVKRRVMTMLdTVSLGGFEKRFpGELSGGQRQRVAIARALVIEPDLLLFDEPLSNLDanlrV 170
Cdd:PRK13549 365 AALDRFTGGSRIDDAAELKTILESIQRL-KVKTASPELAI-ARLSGGNQQKAVLAKCLLLNPKILILDEPTRGID----V 438

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 515998033 171 NMRVEIRRIQQEL---GITTVYVSHDQEECFSISDQVAIMNKGNI 212
Cdd:PRK13549 439 GAKYEIYKLINQLvqqGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 28-196 2.21e-09

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: 55.46  E-value: 2.21e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033    28 RGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDytrvpvnkrnfgfvfqsyalfphlsvfdnvafglrlrkvke 107
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGE----------------------------------------- 39

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   108 ddvkrRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLSNLDANLRVNMRVEIR-----RIQQE 182
Cdd:smart00382  40 -----DILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrlllLLKSE 114

                          170
                   ....*....|....
gi 515998033   183 LGITTVYVSHDQEE 196
Cdd:smart00382 115 KNLTVILTTNDEKD 128
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
 5-166 2.23e-09

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 58.59  E-value: 2.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   5 TLDRVSVAYD-NQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFleakqgtflfgDKDYT--RVPVNKRNFGFVF 81
Cdd:PRK11819   8 TMNRVSKVVPpKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV-----------DKEFEgeARPAPGIKVGYLP 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  82 QSYALFPHLSVFDNVAFGLRLRKVK------------EDDVKR--------RVMTMLDTVSLGGFEKRF----------P 131
Cdd:PRK11819  77 QEPQLDPEKTVRENVEEGVAEVKAAldrfneiyaayaEPDADFdalaaeqgELQEIIDAADAWDLDSQLeiamdalrcpP 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 515998033 132 GE-----LSGGQRQRVAIARALVIEPDLLLFDEPLSNLDA 166
Cdd:PRK11819 157 WDakvtkLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA 196
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
 18-210 4.09e-09

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


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 58.20  E-value: 4.09e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033    18 ILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIA----GFLEAKQGTFLFgdKDYTRVPVNKRNFGFVFQSYAL---FPHL 90
Cdd:TIGR00956   76 ILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITY--DGITPEEIKKHYRGDVVYNAETdvhFPHL 153

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033    91 SVFDNVAFGLRLRKV--------KEDDVKRRVMTMLDTVSLG-------GFEkrFPGELSGGQRQRVAIARALVIEPDLL 155
Cdd:TIGR00956  154 TVGETLDFAARCKTPqnrpdgvsREEYAKHIADVYMATYGLShtrntkvGND--FVRGVSGGERKRVSIAEASLGGAKIQ 231

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 515998033   156 LFDEPLSNLDANLRVNMrVEIRRIQQELGITTVYVSHDQ--EECFSISDQVAIMNKG 210
Cdd:TIGR00956  232 CWDNATRGLDSATALEF-IRALKTSANILDTTPLVAIYQcsQDAYELFDKVIVLYEG 287
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
 26-206 1.02e-08

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: 54.12  E-value: 1.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  26 LERGQLLSLLGPSGCGKTTTLRLIAGFLEAKqgtflfGDKDYtrvpvnkrnfgfvfqsyalfphlsvFDNVAFGLRLRKV 105
Cdd:cd03222   22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPN------GDNDE-------------------------WDGITPVYKPQYI 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033 106 KeddvkrrvmtmldtvslggfekrfpgeLSGGQRQRVAIARALVIEPDLLLFDEPLSNLDANLRVNMRVEIRRIQQELGI 185
Cdd:cd03222   71 D---------------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKK 123

                        170       180
                 ....*....|....*....|.
gi 515998033 186 TTVYVSHDQEECFSISDQVAI 206
Cdd:cd03222  124 TALVVEHDLAVLDYLSDRIHV 144
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
20-212 1.44e-08

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 56.07  E-value: 1.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  20 QDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGT-FLFGDKDYTRVPVNKRNFGFVF-----QSYALFPHLSVF 93
Cdd:PRK11288 270 EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQvYLDGKPIDIRSPRDAIRAGIMLcpedrKAEGIIPVHSVA 349

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  94 DNVA---------FGLRLRKVKEDDVKRRVMTMLDTVSLGGfeKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLSNL 164
Cdd:PRK11288 350 DNINisarrhhlrAGCLINNRWEAENADRFIRSLNIKTPSR--EQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGI 427

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 515998033 165 DanlrVNMRVEIRRIQQEL---GITTVYVSHDQEECFSISDQVAIMNKGNI 212
Cdd:PRK11288 428 D----VGAKHEIYNVIYELaaqGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
 18-192 1.60e-08

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 56.58  E-value: 1.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   18 ILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRvPVN----KRNFGFVFQSYALFPHlSVF 93
Cdd:PTZ00265  400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLK-DINlkwwRSKIGVVSQDPLLFSN-SIK 477

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   94 DNVAFGLRLRK--------VKED-----------------------------------DVKRRVMTMLDT--------VS 122
Cdd:PTZ00265  478 NNIKYSLYSLKdlealsnyYNEDgndsqenknkrnscrakcagdlndmsnttdsneliEMRKNYQTIKDSevvdvskkVL 557

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  123 LGGFEKRFP-----------GELSGGQRQRVAIARALVIEPDLLLFDEPLSNLDANLRVNMRVEIRRIQQELGITTVYVS 191
Cdd:PTZ00265  558 IHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIA 637


                  .
gi 515998033  192 H 192
Cdd:PTZ00265  638 H 638
3a01203 TIGR00954
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...
 15-192 1.80e-08

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


Pssm-ID: 273360 [Multi-domain]  Cd Length: 659  Bit Score: 55.91  E-value: 1.80e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   15 NQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFlfgdkdytRVPVNKRNFgFVFQSyalfPHLSV-- 92
Cdd:TIGR00954 464 GDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRL--------TKPAKGKLF-YVPQR----PYMTLgt 530

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   93 -FDNVAFGLRLRKVKEDDVKRRVM-TMLDTVSLGGFEKRFPG---------ELSGGQRQRVAIARALVIEPDLLLFDEPL 161
Cdd:TIGR00954 531 lRDQIIYPDSSEDMKRRGLSDKDLeQILDNVQLTHILEREGGwsavqdwmdVLSGGEKQRIAMARLFYHKPQFAILDECT 610

                         170       180       190
                  ....*....|....*....|....*....|.
gi 515998033  162 SNLDanlrVNMRVEIRRIQQELGITTVYVSH 192
Cdd:TIGR00954 611 SAVS----VDVEGYMYRLCREFGITLFSVSH 637
PLN03073 PLN03073
ABC transporter F family; Provisional
 101-165 6.70e-08

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 54.10  E-value: 6.70e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515998033 101 RLRKVKEDDVKRRVMTMLDTVSLGG-FEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLSNLD 165
Cdd:PLN03073 311 RLELIDAYTAEARAASILAGLSFTPeMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
TOBE_2 pfam08402
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the ...
 278-351 9.98e-08

TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the C-terminal strand of each domain is supplied by the partner. Probably involved in the recognition of small ligands such as molybdenum and sulphate. Found in ABC transporters immediately after the ATPase domain. In this family a strong RPE motif is found at the presumed N-terminus of the domain.


Pssm-ID: 462465 [Multi-domain]  Cd Length: 73  Bit Score: 48.77  E-value: 9.98e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515998033  278 AIRPDDLVIrtegnETGENELPGVIKVSTYLGRSYQYVVETAKGNFTANQ---EMDTPYLSGQRVTLHFPADKMVLV 351
Cdd:pfam08402   2 AIRPEKIRL-----AAAANGLSGTVTDVEYLGDHTRYHVELAGGEELVVRvpnAHARPPAPGDRVGLGWDPEDAHVL 73
SapD COG4170
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
6-207 1.58e-07

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


Pssm-ID: 443330 [Multi-domain]  Cd Length: 331  Bit Score: 52.22  E-value: 1.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   6 LDRVSvaydnqlilqdfdLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAK-QGT---FLFGDKDYTRVPVNKR------ 75
Cdd:COG4170   23 VDRVS-------------LTLNEGEIRGLVGESGSGKSLIAKAICGITKDNwHVTadrFRWNGIDLLKLSPRERrkiigr 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  76 NFGFVFQ--SYALFPHLSVFDNVAFGLRLRKVK------EDDVKRRVMTMLDTVSLGGFE---KRFPGELSGGQRQRVAI 144
Cdd:COG4170   90 EIAMIFQepSSCLDPSAKIGDQLIEAIPSWTFKgkwwqrFKWRKKRAIELLHRVGIKDHKdimNSYPHELTEGECQKVMI 169

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515998033 145 ARALVIEPDLLLFDEPLSNLDANLRVNMRVEIRRIQQELGITTVYVSHDQEECFSISDQVAIM 207
Cdd:COG4170  170 AMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVL 232
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
101-212 1.97e-07

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 52.04  E-value: 1.97e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033 101 RLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLSNLDANLRVNMRVEIRRIQ 180
Cdd:NF000106 112 R*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMV 191

                         90       100       110
                 ....*....|....*....|....*....|..
gi 515998033 181 QElGITTVYVSHDQEECFSISDQVAIMNKGNI 212
Cdd:NF000106 192 RD-GATVLLTTQYMEEAEQLAHELTVIDRGRV 222
PRK15093 PRK15093
peptide ABC transporter ATP-binding protein SapD;
6-207 2.01e-07

peptide ABC transporter ATP-binding protein SapD;


Pssm-ID: 185049 [Multi-domain]  Cd Length: 330  Bit Score: 52.11  E-value: 2.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   6 LDRVSvaydnqlilqdfdLQLERGQLLSLLGPSGCGKTTTLRLIAGF----LEAKQGTFLFGDKDYTRVPVNKR------ 75
Cdd:PRK15093  23 VDRVS-------------MTLTEGEIRGLVGESGSGKSLIAKAICGVtkdnWRVTADRMRFDDIDLLRLSPRERrklvgh 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  76 NFGFVFQ--SYALFPHLSVFDNVA---------------FGLRlrkvkeddvKRRVMTMLDTVSLGGFE---KRFPGELS 135
Cdd:PRK15093  90 NVSMIFQepQSCLDPSERVGRQLMqnipgwtykgrwwqrFGWR---------KRRAIELLHRVGIKDHKdamRSFPYELT 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515998033 136 GGQRQRVAIARALVIEPDLLLFDEPLSNLDANLRVNMRVEIRRIQQELGITTVYVSHDQEECFSISDQVAIM 207
Cdd:PRK15093 161 EGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVL 232
PLN03232 PLN03232
ABC transporter C family member; Provisional
 32-229 2.57e-07

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 52.67  E-value: 2.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   32 LSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVN--KRNFGFVFQSYALFPHLSVFDNVAFGLR-------- 101
Cdd:PLN03232 1265 VGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTdlRRVLSIIPQSPVLFSGTVRFNIDPFSEHndadlwea 1344

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  102 LRKVKEDDVKRRVMTMLDT-VSLGGfekrfpGELSGGQRQRVAIARALVIEPDLLLFDEPLSNLDanLRVNMRVEiRRIQ 180
Cdd:PLN03232 1345 LERAHIKDVIDRNPFGLDAeVSEGG------ENFSVGQRQLLSLARALLRRSKILVLDEATASVD--VRTDSLIQ-RTIR 1415

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 515998033  181 QELGITTVYVSHDQEECFSISDQVAIMNKGNIEQLDAPSTIFKYPTTEF 229
Cdd:PLN03232 1416 EEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAF 1464
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
 36-195 1.03e-06

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


Pssm-ID: 213207 [Multi-domain]  Cd Length: 204  Bit Score: 48.76  E-value: 1.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  36 GPSGCGKTTTLRLI--AGFLEAKQGT-FLFGDKDYTRVPVNKRNFGFVFQS-----YALFPHLSVFDNVAFglrlrkVKE 107
Cdd:cd03240   29 GQNGAGKTTIIEALkyALTGELPPNSkGGAHDPKLIREGEVRAQVKLAFENangkkYTITRSLAILENVIF------CHQ 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033 108 DDVKRRVMTMLDTvslggfekrfpgeLSGGQRQ------RVAIARALVIEPDLLLFDEPLSNLDA-NLRVNMRVEIRRIQ 180
Cdd:cd03240  103 GESNWPLLDMRGR-------------CSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEeNIEESLAEIIEERK 169

                        170
                 ....*....|....*
gi 515998033 181 QELGITTVYVSHDQE 195
Cdd:cd03240  170 SQKNFQLIVITHDEE 184
GguA NF040905
sugar ABC transporter ATP-binding protein;
19-217 1.22e-06

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 50.17  E-value: 1.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  19 LQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAkqGTFLfGDKDYTRVPVNKRN------FGFVF--QSYALFPHL 90
Cdd:NF040905  17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPH--GSYE-GEILFDGEVCRFKDirdseaLGIVIihQELALIPYL 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  91 SVFDNVAFGLRLRK---VKEDDVKRRVMTMLDTVSLggfeKRFPGELSG----GQRQRVAIARALVIEPDLLLFDEPLSN 163
Cdd:NF040905  94 SIAENIFLGNERAKrgvIDWNETNRRARELLAKVGL----DESPDTLVTdigvGKQQLVEIAKALSKDVKLLILDEPTAA 169

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 515998033 164 LD----ANLrVNMRVEIRriqqELGITTVYVSHDQEECFSISDQVAIMNKGN-IEQLDA 217
Cdd:NF040905 170 LNeedsAAL-LDLLLELK----AQGITSIIISHKLNEIRRVADSITVLRDGRtIETLDC 223
PLN03073 PLN03073
ABC transporter F family; Provisional
 32-165 1.65e-06

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 49.86  E-value: 1.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  32 LSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKdyTRVPVNKRNF--GFVFQSYALFPHLSVFDNVAfglrlrkvkedd 109
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISGELQPSSGTVFRSAK--VRMAVFSQHHvdGLDLSSNPLLYMMRCFPGVP------------ 603

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 515998033 110 vKRRVMTMLDTVSLGGFEKRFPG-ELSGGQRQRVAIARALVIEPDLLLFDEPLSNLD 165
Cdd:PLN03073 604 -EQKLRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
ABCC_SUR2 cd03288
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...
 4-222 1.99e-06

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: 48.37  E-value: 1.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   4 LTLDRVSVAYDNQL--ILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVN--KRNFGF 79
Cdd:cd03288   20 IKIHDLCVRYENNLkpVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHtlRSRLSI 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  80 VFQSYALFPhlsvfDNVAFGLRLRKVKEDDvkrRVMTMLDTVSLGGFEKRFPGEL-----------SGGQRQRVAIARAL 148
Cdd:cd03288  100 ILQDPILFS-----GSIRFNLDPECKCTDD---RLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAF 171

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515998033 149 VIEPDLLLFDEPLSNLD-ANLRVNMRVEIRRIQQElgiTTVYVSHDQEECFSiSDQVAIMNKGNIEQLDAPSTIF 222
Cdd:cd03288  172 VRKSSILIMDEATASIDmATENILQKVVMTAFADR---TVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLL 242
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
 29-224 1.99e-06

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 49.40  E-value: 1.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  29 GQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLF--------------------------GDKDYTRVP-----VNKRNF 77
Cdd:PRK10636  27 GQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFpgnwqlawvnqetpalpqpaleyvidGDREYRQLEaqlhdANERND 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  78 GFVFQSyalfphlsvfdnvAFGlRLRKVKEDDVKRRVMTMLDTVslgGFEK----RFPGELSGGQRQRVAIARALVIEPD 153
Cdd:PRK10636 107 GHAIAT-------------IHG-KLDAIDAWTIRSRAASLLHGL---GFSNeqleRPVSDFSGGWRMRLNLAQALICRSD 169

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515998033 154 LLLFDEPLSNLDANLRVNMRVEIRRIQQelgiTTVYVSHDQEECFSISDQVAimnkgNIEQldapSTIFKY 224
Cdd:PRK10636 170 LLLLDEPTNHLDLDAVIWLEKWLKSYQG----TLILISHDRDFLDPIVDKII-----HIEQ----QSLFEY 227
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
 4-217 3.01e-06

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: 47.93  E-value: 3.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   4 LTLDRVSVAY--DNQLILQDFDLQLERGQLLSLLGPSGCGKTTtlrLIAGFLE--AKQGTFLFGDKDYTRVPVNK--RNF 77
Cdd:cd03289    3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKST---LLSAFLRllNTEGDIQIDGVSWNSVPLQKwrKAF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  78 GFVFQSYALFPHLSVFDNVAFGlrlrKVKEDDVKRrvmtMLDTVSLGGFEKRFPGEL-----------SGGQRQRVAIAR 146
Cdd:cd03289   80 GVIPQKVFIFSGTFRKNLDPYG----KWSDEEIWK----VAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLAR 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515998033 147 ALVIEPDLLLFDEPLSNLDAnlrVNMRVEIRRIQQELGITTVYVSHDQEECFSISDQVAIMNKGNIEQLDA 217
Cdd:cd03289  152 SVLSKAKILLLDEPSAHLDP---ITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDS 219
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
 14-223 4.05e-06

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: 48.79  E-value: 4.05e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033    14 DNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRVPVNKRNFgfvfqSYALFPHlsvf 93
Cdd:TIGR00957 1297 DLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRF-----KITIIPQ---- 1367

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033    94 DNVAFGLRLR-------KVKEDDVkrrvMTMLDTVSLGGFEKRFP----------GE-LSGGQRQRVAIARALVIEPDLL 155
Cdd:TIGR00957 1368 DPVLFSGSLRmnldpfsQYSDEEV----WWALELAHLKTFVSALPdkldhecaegGEnLSVGQRQLVCLARALLRKTKIL 1443

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   156 LFDEPLSNLDANLRVNMRVEIRriQQELGITTVYVSHDQEecfSISD--QVAIMNKGNIEQLDAPSTIFK 223
Cdd:TIGR00957 1444 VLDEATAAVDLETDNLIQSTIR--TQFEDCTVLTIAHRLN---TIMDytRVIVLDKGEVAEFGAPSNLLQ 1508
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
 34-193 6.61e-06

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 47.58  E-value: 6.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  34 LLGPSGCGKTTTLRLIAGFLEAKQGTflfgdkdyTRVPVNKRnFGFVFQSYALFPHLSVFDNVAFG-LRLRKVKEDdvKR 112
Cdd:PRK15064  32 LIGANGCGKSTFMKILGGDLEPSAGN--------VSLDPNER-LGKLRQDQFAFEEFTVLDTVIMGhTELWEVKQE--RD 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033 113 RV-----MTMLDTVSLGGFEKRFpGELSG------------------------------GQRQRVAIARALVIEPDLLLF 157
Cdd:PRK15064 101 RIyalpeMSEEDGMKVADLEVKF-AEMDGytaearagelllgvgipeeqhyglmsevapGWKLRVLLAQALFSNPDILLL 179

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 515998033 158 DEPLSNLDANlrvnmrvEIRRIQQEL---GITTVYVSHD 193
Cdd:PRK15064 180 DEPTNNLDIN-------TIRWLEDVLnerNSTMIIISHD 211
ycf16 CHL00131
sulfate ABC transporter protein; Validated
 3-165 7.34e-06

sulfate ABC transporter protein; Validated


Pssm-ID: 214372 [Multi-domain]  Cd Length: 252  Bit Score: 46.56  E-value: 7.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   3 LLTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAK--QGTFLFGDKDYTRVPVNKRNfgfv 80
Cdd:CHL00131   7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKilEGDILFKGESILDLEPEERA---- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  81 fqsyalfpHLSVF------------DNVAFgLRL-----RKVKEDDVK------RRVMTMLDTVSLGG-FEKRFPGE-LS 135
Cdd:CHL00131  83 --------HLGIFlafqypieipgvSNADF-LRLaynskRKFQGLPELdpleflEIINEKLKLVGMDPsFLSRNVNEgFS 153

                        170       180       190
                 ....*....|....*....|....*....|
gi 515998033 136 GGQRQRVAIARALVIEPDLLLFDEPLSNLD 165
Cdd:CHL00131 154 GGEKKRNEILQMALLDSELAILDETDSGLD 183
PRK13546 PRK13546
teichoic acids export ABC transporter ATP-binding subunit TagH;
19-214 1.25e-05

teichoic acids export ABC transporter ATP-binding subunit TagH;


Pssm-ID: 184131 [Multi-domain]  Cd Length: 264  Bit Score: 45.96  E-value: 1.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  19 LQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFlfgdKDYTRVPVNKRNFGfvfqsyaLFPHLSVFDNVAF 98
Cdd:PRK13546  40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV----DRNGEVSVIAISAG-------LSGQLTGIENIEF 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  99 GLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLSNLDANLRVNMRVEIRR 178
Cdd:PRK13546 109 KMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYE 188

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 515998033 179 IqQELGITTVYVSHDQEECFSISDQVAIMNKGNIEQ 214
Cdd:PRK13546 189 F-KEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKD 223
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
 127-207 1.63e-05

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 46.55  E-value: 1.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033 127 EKRFPgELSGGQRQRVAIARALVIEPDLLLFDEPLSNLDANLRVNMRVEIRRIQQElGITTVYVSHDQEECFSISDQVAI 206
Cdd:PRK10938 130 DRRFK-YLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGV 207


                 .
gi 515998033 207 M 207
Cdd:PRK10938 208 L 208
sufC PRK09580
cysteine desulfurase ATPase component; Reviewed
 3-165 2.04e-05

cysteine desulfurase ATPase component; Reviewed


Pssm-ID: 181965 [Multi-domain]  Cd Length: 248  Bit Score: 45.55  E-value: 2.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033   3 LLTLDRVSVAYDNQLILQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGF--LEAKQGTFLFGDKDYTRVPVNKRNFGFV 80
Cdd:PRK09580   1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEDRAGEGI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  81 F-------------------------QSYALFPHLSVFDNVAF---GLRLRKVKEDDVKRRVMTmldtvslgGFekrfpg 132
Cdd:PRK09580  81 FmafqypveipgvsnqfflqtalnavRSYRGQEPLDRFDFQDLmeeKIALLKMPEDLLTRSVNV--------GF------ 146

                        170       180       190
                 ....*....|....*....|....*....|...
gi 515998033 133 elSGGQRQRVAIARALVIEPDLLLFDEPLSNLD 165
Cdd:PRK09580 147 --SGGEKKRNDILQMAVLEPELCILDESDSGLD 177
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
 19-210 3.92e-05

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


Pssm-ID: 213205 [Multi-domain]  Cd Length: 176  Bit Score: 43.85  E-value: 3.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  19 LQDFDLQLERGQLLSLLGPSGCGKTTTLRliAGFLEAKQGTFLFGDKDYTRVPVnkrnfgfvfqsyalfphlsvfdnvaf 98
Cdd:cd03238   11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVN--EGLYASGKARLISFLPKFSRNKL-------------------------- 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  99 glrlrkVKEDDVKRRVMTMLDTVSLGgfekRFPGELSGGQRQRVAIARALV--IEPDLLLFDEPLSNLDANLRVNMRVEI 176
Cdd:cd03238   63 ------IFIDQLQFLIDVGLGYLTLG----QKLSTLSGGELQRVKLASELFsePPGTLFILDEPSTGLHQQDINQLLEVI 132

                        170       180       190
                 ....*....|....*....|....*....|....
gi 515998033 177 RRIQQeLGITTVYVSHDqEECFSISDQVAIMNKG 210
Cdd:cd03238  133 KGLID-LGNTVILIEHN-LDVLSSADWIIDFGPG 164
GguA NF040905
sugar ABC transporter ATP-binding protein;
132-212 8.53e-05

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 44.40  E-value: 8.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033 132 GELSGGQRQRVAIARALVIEPDLLLFDEPLSNLDanlrVNMRVEIRRIQQEL---GITTVYVSHDQEECFSISDQVAIMN 208
Cdd:NF040905 403 GNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGID----VGAKYEIYTIINELaaeGKGVIVISSELPELLGMCDRIYVMN 478


                 ....
gi 515998033 209 KGNI 212
Cdd:NF040905 479 EGRI 482
tagH PRK13545
teichoic acids export protein ATP-binding subunit; Provisional
 19-192 6.20e-04

teichoic acids export protein ATP-binding subunit; Provisional


Pssm-ID: 184130 [Multi-domain]  Cd Length: 549  Bit Score: 41.41  E-value: 6.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  19 LQDFDLQLERGQLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFgdkdytrvpvnKRNFGFVFQSYALFPHLSVFDNVAF 98
Cdd:PRK13545  40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDI-----------KGSAALIAISSGLNGQLTGIENIEL 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515998033  99 GLRLRKVKEDDVKRRVMTMLDTVSLGGFEKRFPGELSGGQRQRVAIARALVIEPDLLLFDEPLSNLDANLrVNMRVEIRR 178
Cdd:PRK13545 109 KGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTF-TKKCLDKMN 187

                        170
                 ....*....|....
gi 515998033 179 IQQELGITTVYVSH 192
Cdd:PRK13545 188 EFKEQGKTIFFISH 201
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 26-56 1.63e-03

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 40.07  E-value: 1.63e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 515998033  26 LERGQLLSLL--GPSGCGKTTTLRLIAGFLEAK 56
Cdd:PRK13342  31 IEAGRLSSMIlwGPPGTGKTTLARIIAGATDAP 63
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 34-61 2.85e-03

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 37.90  E-value: 2.85e-03
                         10        20
                 ....*....|....*....|....*...
gi 515998033  34 LLGPSGCGKTTTLRLIAGFLEAKQGTFL 61
Cdd:cd00009   24 LYGPPGTGKTTLARAIANELFRPGAPFL 51
flhF PRK11889
flagellar biosynthesis protein FlhF;
30-70 3.04e-03

flagellar biosynthesis protein FlhF;


Pssm-ID: 183360 [Multi-domain]  Cd Length: 436  Bit Score: 39.28  E-value: 3.04e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 515998033  30 QLLSLLGPSGCGKTTTLRLIAGFLEAKQGTFLFGDKDYTRV 70
Cdd:PRK11889 242 QTIALIGPTGVGKTTTLAKMAWQFHGKKKTVGFITTDHSRI 282
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
 26-51 9.34e-03

Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, recombination and repair];


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 37.73  E-value: 9.34e-03
                         10        20
                 ....*....|....*....|....*...
gi 515998033  26 LERGQLLSLL--GPSGCGKTTTLRLIAG 51
Cdd:COG2256   44 IEAGRLSSMIlwGPPGTGKTTLARLIAN 71
 
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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