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Conserved domains on  [gi|914601027|ref|WP_050596687|]
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ABC transporter ATP-binding protein [Mesorhizobium ciceri]

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 ...
 20-373 5.65e-176

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


:

Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 493.08  E-value: 5.65e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  20 PAIEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQRDIGLVF 99
Cdd:COG3842    4 PALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGMVF 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 100 QSYALFPNMTVAGNIAFSLAVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPL 179
Cdd:COG3842   84 QDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEPL 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 180 AALDRKLREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELYRQPANRFVAGFLGAANLFH 259
Cdd:COG3842  164 SALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGEANLLP 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 260 GIIAREGNGAVLAldGGTRLPLAGDYP-SLGRRATMLVRPERVNLQPatEAPANRFciDCHVADVVYQGEIVRYAVEAPP 338
Cdd:COG3842  244 GTVLGDEGGGVRT--GGRTLEVPADAGlAAGGPVTVAIRPEDIRLSP--EGPENGL--PGTVEDVVFLGSHVRYRVRLGD 317

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 914601027 339 VGPVIASCQ-HVVPRFSPGDRACFSWRPEDAWLIQD 373
Cdd:COG3842  318 GQELVVRVPnRAALPLEPGDRVGLSWDPEDVVVLPA 353
 
Name Accession Description Interval E-value
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
 20-373 5.65e-176

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 493.08  E-value: 5.65e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  20 PAIEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQRDIGLVF 99
Cdd:COG3842    4 PALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGMVF 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 100 QSYALFPNMTVAGNIAFSLAVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPL 179
Cdd:COG3842   84 QDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEPL 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 180 AALDRKLREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELYRQPANRFVAGFLGAANLFH 259
Cdd:COG3842  164 SALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGEANLLP 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 260 GIIAREGNGAVLAldGGTRLPLAGDYP-SLGRRATMLVRPERVNLQPatEAPANRFciDCHVADVVYQGEIVRYAVEAPP 338
Cdd:COG3842  244 GTVLGDEGGGVRT--GGRTLEVPADAGlAAGGPVTVAIRPEDIRLSP--EGPENGL--PGTVEDVVFLGSHVRYRVRLGD 317

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 914601027 339 VGPVIASCQ-HVVPRFSPGDRACFSWRPEDAWLIQD 373
Cdd:COG3842  318 GQELVVRVPnRAALPLEPGDRVGLSWDPEDVVVLPA 353
PhnT2 TIGR03265
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ...
 19-337 1.41e-129

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: 375.53  E-value: 1.41e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   19 RPAIEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQRDIGLV 98
Cdd:TIGR03265   2 SPYLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYGIV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   99 FQSYALFPNMTVAGNIAFSLAVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEP 178
Cdd:TIGR03265  82 FQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  179 LAALDRKLREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELYRQPANRFVAGFLGAANLF 258
Cdd:TIGR03265 162 LSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVGEVNWL 241

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 914601027  259 HGiiAREGNGAVLAldGGTRLPLAGDYPSLGRRATMLVRPERVNLQPATEApANRfcIDCHVADVVYQGEIVRYAVEAP 337
Cdd:TIGR03265 242 PG--TRGGGSRARV--GGLTLACAPGLAQPGASVRLAVRPEDIRVSPAGNA-ANL--LLARVEDMEFLGAFYRLRLRLE 313
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
 22-253 5.34e-129

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: 369.64  E-value: 5.34e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  22 IEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQRDIGLVFQS 101
Cdd:cd03300    1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 102 YALFPNMTVAGNIAFSLAVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAA 181
Cdd:cd03300   81 YALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 914601027 182 LDRKLREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELYRQPANRFVAGFLG 253
Cdd:cd03300  161 LDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
14-335 4.74e-127

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 370.05  E-value: 4.74e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  14 APVSRRPAIEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQR 93
Cdd:PRK09452   7 QPSSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENR 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  94 DIGLVFQSYALFPNMTVAGNIAFSLAVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLL 173
Cdd:PRK09452  87 HVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVL 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 174 LLDEPLAALDRKLREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELYRQPANRFVAGFLG 253
Cdd:PRK09452 167 LLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIG 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 254 AANLFHG-IIAREGNGAVLALDGGTRLPLAGDYP-SLGRRATMLVRPERVNLQPATEAPANRFCIDcHVADVVYQGEIVR 331
Cdd:PRK09452 247 EINIFDAtVIERLDEQRVRANVEGRECNIYVNFAvEPGQKLHVLLRPEDLRVEEINDDEHAEGLIG-YVRERNYKGMTLD 325


                 ....
gi 914601027 332 YAVE 335
Cdd:PRK09452 326 SVVE 329
tungstate_WtpC NF040840
tungstate ABC transporter ATP-binding protein WtpC;
22-331 9.43e-97

tungstate ABC transporter ATP-binding protein WtpC;


Pssm-ID: 468779 [Multi-domain]  Cd Length: 347  Bit Score: 291.59  E-value: 9.43e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  22 IEVSGLSKHFGTVcAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQRDIGLVFQS 101
Cdd:NF040840   2 IRIENLSKDWKEF-KLRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIAYVYQN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 102 YALFPNMTVAGNIAFSLAVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAA 181
Cdd:NF040840  81 YMLFPHKTVFENIAFGLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 182 LDRKLREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELYRQPANRFVAGFLGAANLFHGI 261
Cdd:NF040840 161 LDVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVGFENIIEGV 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 914601027 262 IAREGNGAVLALdGGTRLPLAGDYPSlgrRATMLVRPERVNL--QPATEAPANRFciDCHVADVVYQGEIVR 331
Cdd:NF040840 241 AEKGGEGTILDT-GNIKIELPEEKKG---KVRIGIRPEDITIstEKVKTSARNEF--KGKVEEIEDLGPLVK 306
ABC_ATP_DarD NF038007
darobactin export ABC transporter ATP-binding protein;
36-228 1.14e-52

darobactin export ABC transporter ATP-binding protein;


Pssm-ID: 411600 [Multi-domain]  Cd Length: 218  Bit Score: 174.14  E-value: 1.14e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  36 AVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQRD------IGLVFQSYALFPNMT 109
Cdd:NF038007  20 VLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSYSQKIilrrelIGYIFQSFNLIPHLS 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 110 VAGNIAFSLAVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAALDRKLREE 189
Cdd:NF038007 100 IFDNVALPLKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNPALLLADEPTGNLDSKNARA 179

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 914601027 190 VRLELRRLQGTlGVTTVLVTHdQDEAMSMSDRIAVLAQG 228
Cdd:NF038007 180 VLQQLKYINQK-GTTIIMVTH-SDEASTYGNRIINMKDG 216
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 37-180 3.21e-49

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: 162.82  E-value: 3.21e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   37 VSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTH--VPPAQRDIGLVFQSYALFPNMTVAGNI 114
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDdeRKSLRKEIGYVFQDPQLFPRLTVRENL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  115 AFSLAVRGISRRDAKERVEWAIELVRLNGLEHRK----PSQLSGGQQQRVAIARALVFGPKLLLLDEPLA 180
Cdd:pfam00005  81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
31-225 1.34e-34

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 126.19  E-value: 1.34e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  31 FGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGsrdvthvppAQRDIGLVFQSYAL---FPn 107
Cdd:NF040873   2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRA---------GGARVAYVPQRSEVpdsLP- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 108 MTVAGNIAFSL-AVRGISRR---DAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAALD 183
Cdd:NF040873  72 LTVRDLVAMGRwARRGLWRRltrDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 914601027 184 RKLREEVRLELRRLQGTlGVTTVLVTHDQDEAMSmSDRIAVL 225
Cdd:NF040873 152 AESRERIIALLAEEHAR-GATVVVVTHDLELVRR-ADPCVLL 191
GguA NF040905
sugar ABC transporter ATP-binding protein;
23-228 5.57e-21

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 94.09  E-value: 5.57e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  23 EVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGlIQPTG---GRIVI--------GSRDVTHvppa 91
Cdd:NF040905   3 EMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG-VYPHGsyeGEILFdgevcrfkDIRDSEA---- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  92 qRDIGLVFQSYALFPNMTVAGNIaF---SLAVRG-ISRRDAKERvewAIELVRLNGLE---HRKPSQLSGGQQQRVAIAR 164
Cdd:NF040905  78 -LGIVIIHQELALIPYLSIAENI-FlgnERAKRGvIDWNETNRR---ARELLAKVGLDespDTLVTDIGVGKQQLVEIAK 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 914601027 165 ALVFGPKLLLLDEPLAALD----RKLREEVrLELRRlQgtlGVTTVLVTHDQDEAMSMSDRIAVLAQG 228
Cdd:NF040905 153 ALSKDVKLLILDEPTAALNeedsAALLDLL-LELKA-Q---GITSIIISHKLNEIRRVADSITVLRDG 215
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
19-246 1.49e-20

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 91.72  E-value: 1.49e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  19 RPAIEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLlGLVAGLIQPTGGR-------IVIGSRDVTHVPPA 91
Cdd:NF000106  11 RNAVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RG-ALPAHV*GPDAGRrpwrf*tWCANRRALRRTIG* 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  92 QRDIGL-VFQSYALFPNMTVAGNIAfslavrGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGP 170
Cdd:NF000106  90 HRPVR*gRRESFSGRENLYMIGR*L------DLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRP 163

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 914601027 171 KLLLLDEPLAALDRKLREEVRLELRRLQGTlGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELYRQPANR 246
Cdd:NF000106 164 AVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVGGR 238
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
20-242 1.05e-17

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 84.79  E-value: 1.05e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  20 PAIEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRI-----VIGSRDVThvppAQRD 94
Cdd:NF033858 265 PAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAwlfgqPVDAGDIA----TRRR 340

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  95 IGLVFQSYALFPNMTVAGNIAfsLAVR--GISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKL 172
Cdd:NF033858 341 VGYMSQAFSLYGELTVRQNLE--LHARlfHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPEL 418

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 914601027 173 LLLDEPLAALDRKLRE---EVRLELRRLQgtlGVTTVLVTHDQDEAMSmSDRIA------VLAQgviqqlGSPGELYRQ 242
Cdd:NF033858 419 LILDEPTSGVDPVARDmfwRLLIELSRED---GVTIFISTHFMNEAER-CDRISlmhagrVLAS------DTPAALVAA 487
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
21-178 1.73e-15

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 78.24  E-value: 1.73e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  21 AIEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGL--IQpTGGRIVIGS--RDVTHVPPAQRDI- 95
Cdd:NF033858   1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGArkIQ-QGRVEVLGGdmADARHRRAVCPRIa 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  96 ----GLvfqSYALFPNMTVAGNIAFSLAVRGISRRDAKERVEwaiELVRLNGLE---HRKPSQLSGGQQQRVAIARALVF 168
Cdd:NF033858  80 ympqGL---GKNLYPTLSVFENLDFFGRLFGQDAAERRRRID---ELLRATGLApfaDRPAGKLSGGMKQKLGLCCALIH 153

                        170
                 ....*....|
gi 914601027 169 GPKLLLLDEP 178
Cdd:NF033858 154 DPDLLILDEP 163
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 47-224 1.11e-12

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: 65.09  E-value: 1.11e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027    47 GEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIgsrdvthvppaqrdiglvfqsyalfpnmtVAGniafslavrgisrr 126
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIY-----------------------------IDG-------------- 38

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   127 dakERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAALDRKLREEVRLELRRLQGTL----- 201
Cdd:smart00382  39 ---EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLlksek 115

                          170       180
                   ....*....|....*....|...
gi 914601027   202 GVTTVLVTHDQDEAMSMSDRIAV 224
Cdd:smart00382 116 NLTVILTTNDEKDLGPALLRRRF 138
GguA NF040905
sugar ABC transporter ATP-binding protein;
37-244 2.76e-05

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 45.94  E-value: 2.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  37 VSDVDLTVAEGEFLSILGPSGSGKSTL----LGLVAGliQPTGGRIVIGSR--DVTHVPPAQrDIGLVF-----QSYALF 105
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTELamsvFGRSYG--RNISGTVFKDGKevDVSTVSDAI-DAGLAYvtedrKGYGLN 352

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 106 PNMTVAGNIafSLA-VRGISRR---DAKERVEWAIELVRlnGLEHRKPS------QLSGGQQQRVAIARALVFGPKLLLL 175
Cdd:NF040905 353 LIDDIKRNI--TLAnLGKVSRRgviDENEEIKVAEEYRK--KMNIKTPSvfqkvgNLSGGNQQKVVLSKWLFTDPDVLIL 428

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 914601027 176 DEPLAALDRKLREEVRLELRRL--QGTlGVttVLVTHDQDEAMSMSDRIAVLAQGVIQqlgspGELYRQPA 244
Cdd:NF040905 429 DEPTRGIDVGAKYEIYTIINELaaEGK-GV--IVISSELPELLGMCDRIYVMNEGRIT-----GELPREEA 491
 
Name Accession Description Interval E-value
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
 20-373 5.65e-176

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 493.08  E-value: 5.65e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  20 PAIEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQRDIGLVF 99
Cdd:COG3842    4 PALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGMVF 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 100 QSYALFPNMTVAGNIAFSLAVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPL 179
Cdd:COG3842   84 QDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEPL 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 180 AALDRKLREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELYRQPANRFVAGFLGAANLFH 259
Cdd:COG3842  164 SALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGEANLLP 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 260 GIIAREGNGAVLAldGGTRLPLAGDYP-SLGRRATMLVRPERVNLQPatEAPANRFciDCHVADVVYQGEIVRYAVEAPP 338
Cdd:COG3842  244 GTVLGDEGGGVRT--GGRTLEVPADAGlAAGGPVTVAIRPEDIRLSP--EGPENGL--PGTVEDVVFLGSHVRYRVRLGD 317

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 914601027 339 VGPVIASCQ-HVVPRFSPGDRACFSWRPEDAWLIQD 373
Cdd:COG3842  318 GQELVVRVPnRAALPLEPGDRVGLSWDPEDVVVLPA 353
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
 21-370 3.22e-149

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


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 425.26  E-value: 3.22e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  21 AIEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQRDIGLVFQ 100
Cdd:COG3839    3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIAMVFQ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 101 SYALFPNMTVAGNIAFSLAVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLA 180
Cdd:COG3839   83 SYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLS 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 181 ALDRKLREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELYRQPANRFVAGFLG--AANLF 258
Cdd:COG3839  163 NLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGFIGspPMNLL 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 259 HGIIarEGNGAVLaldGGTRLPLAGDYPSL-GRRATMLVRPERVNLqpateAPANRFCIDCHVADVVYQGEIVRYAVEAP 337
Cdd:COG3839  243 PGTV--EGGGVRL---GGVRLPLPAALAAAaGGEVTLGIRPEHLRL-----ADEGDGGLEATVEVVEPLGSETLVHVRLG 312

                        330       340       350
                 ....*....|....*....|....*....|...
gi 914601027 338 PvGPVIASCQHVVpRFSPGDRACFSWRPEDAWL 370
Cdd:COG3839  313 G-QELVARVPGDT-RLRPGDTVRLAFDPERLHL 343
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
 22-370 1.87e-131

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


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 380.26  E-value: 1.87e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  22 IEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDV-THVPPAQRDIGLVFQ 100
Cdd:COG1118    3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLfTNLPPRERRVGFVFQ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 101 SYALFPNMTVAGNIAFSLAVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLA 180
Cdd:COG1118   83 HYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFG 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 181 ALDRKLREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELYRQPANRFVAGFLGAANLFHG 260
Cdd:COG1118  163 ALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLGCVNVLRG 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 261 IIAregnGAVLALDGgtrLPLAGDYPSLGRRATMLVRPERVNLQPATEAPAnrfCIDCHVADVVYQGEIVRYAVEAPPVG 340
Cdd:COG1118  243 RVI----GGQLEADG---LTLPVAEPLPDGPAVAGVRPHDIEVSREPEGEN---TFPATVARVSELGPEVRVELKLEDGE 312

                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 914601027 341 PVIASCQhvVPR-------FSPGDRACFSWRPEDAWL 370
Cdd:COG1118  313 GQPLEAE--VTKeawaelgLAPGDPVYLRPRPARVFL 347
PhnT2 TIGR03265
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ...
 19-337 1.41e-129

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: 375.53  E-value: 1.41e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   19 RPAIEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQRDIGLV 98
Cdd:TIGR03265   2 SPYLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYGIV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   99 FQSYALFPNMTVAGNIAFSLAVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEP 178
Cdd:TIGR03265  82 FQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  179 LAALDRKLREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELYRQPANRFVAGFLGAANLF 258
Cdd:TIGR03265 162 LSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVGEVNWL 241

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 914601027  259 HGiiAREGNGAVLAldGGTRLPLAGDYPSLGRRATMLVRPERVNLQPATEApANRfcIDCHVADVVYQGEIVRYAVEAP 337
Cdd:TIGR03265 242 PG--TRGGGSRARV--GGLTLACAPGLAQPGASVRLAVRPEDIRVSPAGNA-ANL--LLARVEDMEFLGAFYRLRLRLE 313
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
 22-253 5.34e-129

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: 369.64  E-value: 5.34e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  22 IEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQRDIGLVFQS 101
Cdd:cd03300    1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 102 YALFPNMTVAGNIAFSLAVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAA 181
Cdd:cd03300   81 YALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 914601027 182 LDRKLREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELYRQPANRFVAGFLG 253
Cdd:cd03300  161 LDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
14-335 4.74e-127

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 370.05  E-value: 4.74e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  14 APVSRRPAIEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQR 93
Cdd:PRK09452   7 QPSSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENR 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  94 DIGLVFQSYALFPNMTVAGNIAFSLAVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLL 173
Cdd:PRK09452  87 HVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVL 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 174 LLDEPLAALDRKLREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELYRQPANRFVAGFLG 253
Cdd:PRK09452 167 LLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIG 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 254 AANLFHG-IIAREGNGAVLALDGGTRLPLAGDYP-SLGRRATMLVRPERVNLQPATEAPANRFCIDcHVADVVYQGEIVR 331
Cdd:PRK09452 247 EINIFDAtVIERLDEQRVRANVEGRECNIYVNFAvEPGQKLHVLLRPEDLRVEEINDDEHAEGLIG-YVRERNYKGMTLD 325


                 ....
gi 914601027 332 YAVE 335
Cdd:PRK09452 326 SVVE 329
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
 22-234 2.33e-112

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: 326.40  E-value: 2.33e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  22 IEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQRDIGLVFQS 101
Cdd:cd03259    1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVFQD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 102 YALFPNMTVAGNIAFSLAVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAA 181
Cdd:cd03259   81 YALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 914601027 182 LDRKLREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLG 234
Cdd:cd03259  161 LDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
potA TIGR01187
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ...
 52-365 2.62e-112

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: 330.61  E-value: 2.62e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   52 ILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQRDIGLVFQSYALFPNMTVAGNIAFSLAVRGISRRDAKER 131
Cdd:TIGR01187   1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  132 VEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAALDRKLREEVRLELRRLQGTLGVTTVLVTHD 211
Cdd:TIGR01187  81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  212 QDEAMSMSDRIAVLAQGVIQQLGSPGELYRQPANRFVAGFLGAANLFHG-IIAREGNGAVLALDGGTRLPLAGDYPSLG- 289
Cdd:TIGR01187 161 QEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVFEAtVIERKSEQVVLAGVEGRRCDIYTDVPVEKd 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  290 RRATMLVRPERVNLQpaTEAPANRF-CIDCHVADVVYQGEIVRYAVEAPPVGPVIASCQ----HVVPRFSPGDRACFSWR 364
Cdd:TIGR01187 241 QPLHVVLRPEKIVIE--EEDEANSSnAIIGHVIDITYLGMTLEVHVRLETGQKVLVSEFfnedDPHMSPSIGDRVGLTWH 318


                  .
gi 914601027  365 P 365
Cdd:TIGR01187 319 P 319
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
 22-234 2.27e-109

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: 318.82  E-value: 2.27e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  22 IEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQRDIGLVFQS 101
Cdd:cd03301    1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVFQN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 102 YALFPNMTVAGNIAFSLAVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAA 181
Cdd:cd03301   81 YALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 914601027 182 LDRKLREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLG 234
Cdd:cd03301  161 LDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
21-311 2.26e-107

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


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 319.10  E-value: 2.26e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  21 AIEVSGLSKHF-GTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQRDIGLVF 99
Cdd:PRK11650   3 GLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDIAMVF 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 100 QSYALFPNMTVAGNIAFSLAVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPL 179
Cdd:PRK11650  83 QNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPL 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 180 AALDRKLREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELYRQPANRFVAGFLG--AANL 257
Cdd:PRK11650 163 SNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASFIGspAMNL 242

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 914601027 258 FHGIIarEGNGAVLALDGGTRLPLAGDYP-SLGRRATMLVRPErvNLQPATEAPA 311
Cdd:PRK11650 243 LDGRV--SADGAAFELAGGIALPLGGGYRqYAGRKLTLGIRPE--HIALSSAEGG 293
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
 21-254 1.79e-104

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: 307.34  E-value: 1.79e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  21 AIEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQRDIGLVFQ 100
Cdd:cd03296    2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFVFQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 101 SYALFPNMTVAGNIAFSLAVRGISRR----DAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLD 176
Cdd:cd03296   82 HYALFRHMTVFDNVAFGLRVKPRSERppeaEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLD 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 914601027 177 EPLAALDRKLREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELYRQPANRFVAGFLGA 254
Cdd:cd03296  162 EPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFLGE 239
3a0106s01 TIGR00968
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
 22-256 1.39e-100

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


Pssm-ID: 130041 [Multi-domain]  Cd Length: 237  Bit Score: 297.48  E-value: 1.39e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   22 IEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQRDIGLVFQS 101
Cdd:TIGR00968   1 IEIANISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARDRKIGFVFQH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  102 YALFPNMTVAGNIAFSLAVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAA 181
Cdd:TIGR00968  81 YALFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGA 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 914601027  182 LDRKLREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELYRQPANRFVAGFLGAAN 256
Cdd:TIGR00968 161 LDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLGEVN 235
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
22-327 2.24e-100

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 301.25  E-value: 2.24e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  22 IEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQRDIGLVFQS 101
Cdd:PRK11432   7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMVFQS 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 102 YALFPNMTVAGNIAFSLAVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAA 181
Cdd:PRK11432  87 YALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSN 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 182 LDRKLREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELYRQPANRFVAGFLGAANLFHGi 261
Cdd:PRK11432 167 LDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMGDANIFPA- 245

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 914601027 262 iaREGNGAVLAldGGTRLPLAGDYPSLGRRATMLV--RPERVNLQpATEAPANRfcidCHVADVVYQG 327
Cdd:PRK11432 246 --TLSGDYVDI--YGYRLPRPAAFAFNLPDGECTVgvRPEAITLS-EQGEESQR----CTIKHVAYMG 304
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
 17-228 5.74e-97

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


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 288.91  E-value: 5.74e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  17 SRRPAIEVSGLSKHF----GTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPaq 92
Cdd:COG1116    3 AAAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP-- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  93 rDIGLVFQSYALFPNMTVAGNIAFSLAVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKL 172
Cdd:COG1116   81 -DRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEV 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 914601027 173 LLLDEPLAALDRKLREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQG 228
Cdd:COG1116  160 LLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSAR 215
tungstate_WtpC NF040840
tungstate ABC transporter ATP-binding protein WtpC;
22-331 9.43e-97

tungstate ABC transporter ATP-binding protein WtpC;


Pssm-ID: 468779 [Multi-domain]  Cd Length: 347  Bit Score: 291.59  E-value: 9.43e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  22 IEVSGLSKHFGTVcAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQRDIGLVFQS 101
Cdd:NF040840   2 IRIENLSKDWKEF-KLRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIAYVYQN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 102 YALFPNMTVAGNIAFSLAVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAA 181
Cdd:NF040840  81 YMLFPHKTVFENIAFGLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 182 LDRKLREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELYRQPANRFVAGFLGAANLFHGI 261
Cdd:NF040840 161 LDVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVGFENIIEGV 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 914601027 262 IAREGNGAVLALdGGTRLPLAGDYPSlgrRATMLVRPERVNL--QPATEAPANRFciDCHVADVVYQGEIVR 331
Cdd:NF040840 241 AEKGGEGTILDT-GNIKIELPEEKKG---KVRIGIRPEDITIstEKVKTSARNEF--KGKVEEIEDLGPLVK 306
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
19-334 4.05e-95

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 288.66  E-value: 4.05e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  19 RPAIEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQRDIGLV 98
Cdd:PRK11607  17 TPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMM 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  99 FQSYALFPNMTVAGNIAFSLAVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEP 178
Cdd:PRK11607  97 FQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEP 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 179 LAALDRKLREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELYRQPANRFVAGFLGAANLF 258
Cdd:PRK11607 177 MGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNVF 256

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 259 HGIIAREGNGAVLALDGGTRLPLAGDYPSL---GRRATMLVRPERVNLqpATEAPANRFCIDC-HVADVVYQGEIVRYAV 334
Cdd:PRK11607 257 EGVLKERQEDGLVIDSPGLVHPLKVDADASvvdNVPVHVALRPEKIML--CEEPPADGCNFAVgEVIHIAYLGDLSIYHV 334
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
26-329 2.06e-92

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 281.53  E-value: 2.06e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  26 GLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQRDIGLVFQSYALF 105
Cdd:PRK11000   8 NVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGMVFQSYALY 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 106 PNMTVAGNIAFSLAVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAALDRK 185
Cdd:PRK11000  88 PHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAA 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 186 LREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELYRQPANRFVAGFLGAAN---LFHGII 262
Cdd:PRK11000 168 LRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGSPKmnfLPVKVT 247

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 914601027 263 AREGNGAVLALDGGTR--LPLAGDYPSLGRRATMLVRPERVnlqpateapanrfcIDCHVADVVYQGEI 329
Cdd:PRK11000 248 ATAIEQVQVELPNRQQvwLPVEGRGVQVGANMSLGIRPEHL--------------LPSDIADVTLEGEV 302
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
 22-225 1.96e-91

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: 273.58  E-value: 1.96e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  22 IEVSGLSKHFGT----VCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPaqrDIGL 97
Cdd:cd03293    1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP---DRGY 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  98 VFQSYALFPNMTVAGNIAFSLAVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDE 177
Cdd:cd03293   78 VFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDE 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 914601027 178 PLAALDRKLREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVL 225
Cdd:cd03293  158 PFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
21-310 5.98e-90

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 274.65  E-value: 5.98e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  21 AIEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQRDIGLVFQ 100
Cdd:PRK10851   2 SIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVFQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 101 SYALFPNMTVAGNIAFSLAVrgISRRD------AKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLL 174
Cdd:PRK10851  82 HYALFRHMTVFDNIAFGLTV--LPRRErpnaaaIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 175 LDEPLAALDRKLREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELYRQPANRFVAGFLGA 254
Cdd:PRK10851 160 LDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMGE 239

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 914601027 255 ANLFHGIIaregNGAVLALdGGTRLPLAGDyPSLGRRATMLVRPERVNL--QPATEAP 310
Cdd:PRK10851 240 VNRLQGTI----RGGQFHV-GAHRWPLGYT-PAYQGPVDLFLRPWEVDIsrRTSLDSP 291
OpuBA COG1125
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ...
 22-254 8.28e-90

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


Pssm-ID: 440742 [Multi-domain]  Cd Length: 306  Bit Score: 272.35  E-value: 8.28e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  22 IEVSGLSKHF--GTVcAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQ--RDIGL 97
Cdd:COG1125    2 IEFENVTKRYpdGTV-AVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVElrRRIGY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  98 VFQSYALFPNMTVAGNIAFSLAVRGISRRDAKERVEwaiELVRLNGLE-----HRKPSQLSGGQQQRVAIARALVFGPKL 172
Cdd:COG1125   81 VIQQIGLFPHMTVAENIATVPRLLGWDKERIRARVD---ELLELVGLDpeeyrDRYPHELSGGQQQRVGVARALAADPPI 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 173 LLLDEPLAALDRKLREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELYRQPANRFVAGFL 252
Cdd:COG1125  158 LLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADFV 237


                 ..
gi 914601027 253 GA 254
Cdd:COG1125  238 GA 239
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
 22-257 6.86e-87

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: 262.66  E-value: 6.86e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  22 IEVSGLSKHFGTVcAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQRDIGLVFQS 101
Cdd:cd03299    1 LKVENLSKDWKEF-KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVPQN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 102 YALFPNMTVAGNIAFSLAVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAA 181
Cdd:cd03299   80 YALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSA 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 914601027 182 LDRKLREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELYRQPANRFVAGFLGAANL 257
Cdd:cd03299  160 LDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLGFNNI 235
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
20-230 2.76e-86

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 260.75  E-value: 2.76e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  20 PAIEVSGLSKHFGT----VCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQRD- 94
Cdd:COG1136    3 PLLELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELAr 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  95 -----IGLVFQSYALFPNMTVAGNIAFSLAVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFG 169
Cdd:COG1136   83 lrrrhIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNR 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 914601027 170 PKLLLLDEPLAALDRKLREEVRLELRRLQGTLGVTTVLVTHDQdEAMSMSDRIAVLAQGVI 230
Cdd:COG1136  163 PKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDP-ELAARADRVIRLRDGRI 222
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
 22-258 3.55e-83

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: 253.38  E-value: 3.55e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  22 IEVSGLSKHFGTV-CAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQ--RDIGLV 98
Cdd:cd03295    1 IEFENVTKRYGGGkKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElrRKIGYV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  99 FQSYALFPNMTVAGNIAFSLAVRGISRRDAKERVEWAIELVRL--NGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLD 176
Cdd:cd03295   81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 177 EPLAALDRKLREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELYRQPANRFVAGFLGAAN 256
Cdd:cd03295  161 EPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVGADR 240


                 ..
gi 914601027 257 LF 258
Cdd:cd03295  241 LL 242
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
 27-251 1.99e-82

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: 252.18  E-value: 1.99e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  27 LSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQ------RDIGLVFQ 100
Cdd:cd03294   30 ILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElrelrrKKISMVFQ 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 101 SYALFPNMTVAGNIAFSLAVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLA 180
Cdd:cd03294  110 SFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFS 189

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 914601027 181 ALDRKLREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELYRQPANRFVAGF 251
Cdd:cd03294  190 ALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREF 260
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
 17-252 1.01e-81

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: 249.51  E-value: 1.01e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  17 SRRPAIEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQRD-- 94
Cdd:COG1127    1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYel 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  95 ---IGLVFQSYALFPNMTVAGNIAFSL-AVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGP 170
Cdd:COG1127   81 rrrIGMLFQGGALFDSLTVFENVAFPLrEHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 171 KLLLLDEPLAALDRKLREEV-RLeLRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELyRQPANRFVA 249
Cdd:COG1127  161 EILLYDEPTAGLDPITSAVIdEL-IRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEEL-LASDDPWVR 238


                 ...
gi 914601027 250 GFL 252
Cdd:COG1127  239 QFL 241
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
 22-230 1.25e-79

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: 243.17  E-value: 1.25e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  22 IEVSGLSKHFG----TVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQRD--- 94
Cdd:cd03255    1 IELKNLSKTYGgggeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafr 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  95 ---IGLVFQSYALFPNMTVAGNIAFSLAVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPK 171
Cdd:cd03255   81 rrhIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 914601027 172 LLLLDEPLAALDRKLREEVRLELRRLQGTLGVTTVLVTHDQDEAmSMSDRIAVLAQGVI 230
Cdd:cd03255  161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
22-242 1.10e-77

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 238.81  E-value: 1.10e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  22 IEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPP-AQRDIGLVFQ 100
Cdd:COG1131    1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAeVRRRIGYVPQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 101 SYALFPNMTVAGNIAFSLAVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLA 180
Cdd:COG1131   81 EPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 914601027 181 ALDRKLREEVRLELRRLQGTlGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELYRQ 242
Cdd:COG1131  161 GLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKAR 221
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
 22-253 4.57e-77

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


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 237.58  E-value: 4.57e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  22 IEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVT----HVPPAQRDIGL 97
Cdd:COG1126    2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTdskkDINKLRRKVGM 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  98 VFQSYALFPNMTVAGNIAfsLA---VRGISRRDAKERvewAIELVRLNGLEHRK---PSQLSGGQQQRVAIARALVFGPK 171
Cdd:COG1126   82 VFQQFNLFPHLTVLENVT--LApikVKKMSKAEAEER---AMELLERVGLADKAdayPAQLSGGQQQRVAIARALAMEPK 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 172 LLLLDEPLAALDRKLREEVrLE-LRRLQGTlGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELYRQPANRFVAG 250
Cdd:COG1126  157 VMLFDEPTSALDPELVGEV-LDvMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTRA 234


                 ...
gi 914601027 251 FLG 253
Cdd:COG1126  235 FLS 237
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
 14-243 5.43e-74

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: 238.26  E-value: 5.43e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  14 APVSRRPAIEVSGLSKHF-----GTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHV 88
Cdd:COG1123  253 AAAAAEPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKL 332

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  89 PPAQ-----RDIGLVFQ--SYALFPNMTVAGNIAFSLAVRGI-SRRDAKERVEWAIELVRLN-GLEHRKPSQLSGGQQQR 159
Cdd:COG1123  333 SRRSlrelrRRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLPpDLADRYPHELSGGQRQR 412

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 160 VAIARALVFGPKLLLLDEPLAALDRKLREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGEL 239
Cdd:COG1123  413 VAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEV 492


                 ....
gi 914601027 240 YRQP 243
Cdd:COG1123  493 FANP 496
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
41-254 5.85e-74

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 229.26  E-value: 5.85e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  41 DLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQRDIGLVFQSYALFPNMTVAGNIAFSLAV 120
Cdd:COG3840   19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSMLFQENNLFPHLTVAQNIGLGLRP 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 121 RGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAALDRKLREEVRLELRRLQGT 200
Cdd:COG3840   99 GLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRE 178

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 914601027 201 LGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELYRQPANRFVAGFLGA 254
Cdd:COG3840  179 RGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYLGI 232
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
22-273 2.34e-73

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 231.51  E-value: 2.34e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  22 IEVSGLSKHF----GTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQ----- 92
Cdd:COG1135    2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElraar 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  93 RDIGLVFQSYALFPNMTVAGNIAFSLAVRGISRRDAKERVEwaiELVRLNGLEHRK---PSQLSGGQQQRVAIARALVFG 169
Cdd:COG1135   82 RKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVA---ELLELVGLSDKAdayPSQLSGGQKQRVGIARALANN 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 170 PKLLLLDEPLAALDRKLREEVrLEL-RRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELYRQPANRFV 248
Cdd:COG1135  159 PKVLLCDEATSALDPETTRSI-LDLlKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSELT 237

                        250       260       270
                 ....*....|....*....|....*....|..
gi 914601027 249 AGFLG-------AANLFHGIIAREGNGAVLAL 273
Cdd:COG1135  238 RRFLPtvlndelPEELLARLREAAGGGRLVRL 269
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
 22-251 2.56e-73

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: 227.77  E-value: 2.56e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  22 IEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQ-----RDIG 96
Cdd:cd03261    1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrlrRRMG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  97 LVFQSYALFPNMTVAGNIAFSLAVRGI-SRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLL 175
Cdd:cd03261   81 MLFQSGALFDSLTVFENVAFPLREHTRlSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 914601027 176 DEPLAALDRKLREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELyRQPANRFVAGF 251
Cdd:cd03261  161 DEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL-RASDDPLVRQF 235
proV TIGR01186
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ...
 29-257 2.12e-72

glycine betaine/L-proline transport ATP binding subunit; This model describes 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 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. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 130254 [Multi-domain]  Cd Length: 363  Bit Score: 229.74  E-value: 2.12e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   29 KHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQ------RDIGLVFQSY 102
Cdd:TIGR01186   1 KKTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVElrevrrKKIGMVFQQF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  103 ALFPNMTVAGNIAFSLAVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAAL 182
Cdd:TIGR01186  81 ALFPHMTILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSAL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 914601027  183 DRKLREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELYRQPANRFVAGFLGAANL 257
Cdd:TIGR01186 161 DPLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGKVDL 235
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
 22-243 3.36e-72

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: 224.90  E-value: 3.36e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  22 IEVSGLS-KHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQ--RDIGLV 98
Cdd:COG1122    1 IELENLSfSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElrRKVGLV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  99 FQS--YALFpNMTVAGNIAFSLAVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLD 176
Cdd:COG1122   81 FQNpdDQLF-APTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLD 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 914601027 177 EPLAALDRKLREEVRLELRRLQGTlGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELYRQP 243
Cdd:COG1122  160 EPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDY 225
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
 22-228 1.22e-70

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: 218.98  E-value: 1.22e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  22 IEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVT----HVPPAQRDIGL 97
Cdd:cd03229    1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTdledELPPLRRRIGM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  98 VFQSYALFPNMTVAGNIAFSLavrgisrrdakervewaielvrlnglehrkpsqlSGGQQQRVAIARALVFGPKLLLLDE 177
Cdd:cd03229   81 VFQDFALFPHLTVLENIALGL----------------------------------SGGQQQRVALARALAMDPDVLLLDE 126

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 914601027 178 PLAALDRKLREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQG 228
Cdd:cd03229  127 PTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
22-238 2.04e-70

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 219.92  E-value: 2.04e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  22 IEVSGLSKHFGT-VCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQ-----RDI 95
Cdd:COG2884    2 IRFENVSKRYPGgREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipylrRRI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  96 GLVFQSYALFPNMTVAGNIAFSLAVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLL 175
Cdd:COG2884   82 GVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLA 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 914601027 176 DEPLAALDRKLREEV-RL--ELRRlqgtLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGE 238
Cdd:COG2884  162 DEPTGNLDPETSWEImELleEINR----RGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEARGV 223
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
 22-243 4.71e-70

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: 219.37  E-value: 4.71e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  22 IEVSGLSKHFGT----VCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPP-----AQ 92
Cdd:cd03258    2 IELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGkelrkAR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  93 RDIGLVFQSYALFPNMTVAGNIAFSLAVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKL 172
Cdd:cd03258   82 RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 914601027 173 LLLDEPLAALDRKLREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELYRQP 243
Cdd:cd03258  162 LLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANP 232
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
 39-312 1.45e-69

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: 222.28  E-value: 1.45e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  39 DVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIG------SRDVTHVPPAQRDIGLVFQSYALFPNMTVAG 112
Cdd:COG4148   17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGgevlqdSARGIFLPPHRRRIGYVFQEARLFPHLSVRG 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 113 NIAFslAVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAALDRKLREEVRL 192
Cdd:COG4148   97 NLLY--GRKRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILP 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 193 ELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELYRQPANRFVAGFLGAANLFHGIIAR---EGNGA 269
Cdd:COG4148  175 YLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAGGEEAGSVLEATVAAhdpDYGLT 254

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 914601027 270 VLALDGGT-RLPLAGDypSLGRRATMLVRPERVNLqpATEAPAN 312
Cdd:COG4148  255 RLALGGGRlWVPRLDL--PPGTRVRVRIRARDVSL--ALEPPEG 294
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
 39-234 2.55e-69

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: 216.78  E-value: 2.55e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  39 DVDLTVaEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIG------SRDVTHVPPAQRDIGLVFQSYALFPNMTVAG 112
Cdd:cd03297   16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNgtvlfdSRKKINLPPQQRKIGLVFQQYALFPHLNVRE 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 113 NIAFSLavRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAALDRKLREEVRL 192
Cdd:cd03297   95 NLAFGL--KRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLP 172

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 914601027 193 ELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLG 234
Cdd:cd03297  173 ELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
 22-230 1.86e-68

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: 214.70  E-value: 1.86e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  22 IEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPA----QRDIGL 97
Cdd:cd03262    1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinelRQKVGM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  98 VFQSYALFPNMTVAGNIAFSL-AVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLD 176
Cdd:cd03262   81 VFQQFNLFPHLTVLENITLAPiKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 914601027 177 EPLAALDRKLREEVRLELRRLQGTlGVTTVLVTHDQDEAMSMSDRIAVLAQGVI 230
Cdd:cd03262  161 EPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
 23-228 5.34e-66

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: 208.09  E-value: 5.34e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  23 EVSGLSKHFGT--VCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQ--RDIGLV 98
Cdd:cd03225    1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKElrRKVGLV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  99 FQsyalFP-----NMTVAGNIAFSLAVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLL 173
Cdd:cd03225   81 FQ----NPddqffGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 914601027 174 LLDEPLAALDRKLREEVRLELRRLQgTLGVTTVLVTHDQDEAMSMSDRIAVLAQG 228
Cdd:cd03225  157 LLDEPTAGLDPAGRRELLELLKKLK-AEGKTIIIVTHDLDLLLELADRVIVLEDG 210
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...
 19-244 1.11e-65

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: 209.12  E-value: 1.11e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  19 RPAIEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQR-DIGL 97
Cdd:COG0411    2 DPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIaRLGI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  98 V--FQSYALFPNMTVAGNIA---------------FSLAVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRV 160
Cdd:COG0411   82 ArtFQNPRLFPELTVLENVLvaaharlgrgllaalLRLPRARREEREARERAEELLERVGLADRADEPAGNLSYGQQRRL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 161 AIARALVFGPKLLLLDEPLAALDRKLREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELY 240
Cdd:COG0411  162 EIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEVR 241


                 ....
gi 914601027 241 RQPA 244
Cdd:COG0411  242 ADPR 245
PhnC COG3638
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ...
 20-239 1.86e-65

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


Pssm-ID: 442855 [Multi-domain]  Cd Length: 249  Bit Score: 207.99  E-value: 1.86e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  20 PAIEVSGLSKHF-GTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQ-----R 93
Cdd:COG3638    1 PMLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAlrrlrR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  94 DIGLVFQSYALFPNMTVAGN--------IAFSLAVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARA 165
Cdd:COG3638   81 RIGMIFQQFNLVPRLSVLTNvlagrlgrTSTWRSLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARA 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 914601027 166 LVFGPKLLLLDEPLAALDRKLREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGEL 239
Cdd:COG3638  161 LVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL 234
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
 19-244 4.55e-64

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: 212.46  E-value: 4.55e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  19 RPAIEVSGLSKHF--GTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTG---GRIVIGSRDVTHVPPAQR 93
Cdd:COG1123    2 TPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  94 --DIGLVFQS--YALFPnMTVAGNIAFSLAVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFG 169
Cdd:COG1123   82 grRIGMVFQDpmTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALD 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 914601027 170 PKLLLLDEPLAALDRKLREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELYRQPA 244
Cdd:COG1123  161 PDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
 22-242 1.19e-63

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: 203.17  E-value: 1.19e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  22 IEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPP-AQRDIGLVFQ 100
Cdd:COG4555    2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPReARRQIGVLPD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 101 SYALFPNMTVAGNIAFSLAVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLA 180
Cdd:COG4555   82 ERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTN 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 914601027 181 ALDRKLREEVRLELRRLqGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELYRQ 242
Cdd:COG4555  162 GLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREE 222
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
 22-244 1.24e-63

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: 203.05  E-value: 1.24e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  22 IEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPP---AQRDIGLV 98
Cdd:cd03219    1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPheiARLGIGRT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  99 FQSYALFPNMTVAGNI----------AFSLAVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVF 168
Cdd:cd03219   81 FQIPRLFPELTVLENVmvaaqartgsGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALAT 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 914601027 169 GPKLLLLDEPLAALDRKLREEVRLELRRLQgTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELYRQPA 244
Cdd:cd03219  161 DPKLLLLDEPAAGLNPEETEELAELIRELR-ERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPR 235
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
 21-260 5.48e-63

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: 201.57  E-value: 5.48e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  21 AIEVSGLSKHFGT----VCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQ--RD 94
Cdd:COG1124    1 MLEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAfrRR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  95 IGLVFQSY--ALFPNMTVAGNIAFSLAVRGISRRDakERVEWAIELVRLN-GLEHRKPSQLSGGQQQRVAIARALVFGPK 171
Cdd:COG1124   81 VQMVFQDPyaSLHPRHTVDRILAEPLRIHGLPDRE--ERIAELLEQVGLPpSFLDRYPHQLSGGQRQRVAIARALILEPE 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 172 LLLLDEPLAALDRKLREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELYRQPANRFVAGF 251
Cdd:COG1124  159 LLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHPYTREL 238


                 ....*....
gi 914601027 252 LGAANLFHG 260
Cdd:COG1124  239 LAASLAFER 247
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
 22-234 3.92e-62

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: 198.88  E-value: 3.92e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  22 IEVSGLSKHF----GTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQR---- 93
Cdd:cd03257    2 LEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirr 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  94 -DIGLVFQSY--ALFPNMTVAGNIAFSLAVRGISRRDAKERVEWAIELVRLNGLE---HRKPSQLSGGQQQRVAIARALV 167
Cdd:cd03257   82 kEIQMVFQDPmsSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEevlNRYPHELSGGQRQRVAIARALA 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 914601027 168 FGPKLLLLDEPLAALDRKLREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLG 234
Cdd:cd03257  162 LNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
ECF_ATPase_2 TIGR04521
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
 36-243 7.25e-61

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: 197.29  E-value: 7.25e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   36 AVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTH-----VPPAQRDIGLVFQ--SYALFPNm 108
Cdd:TIGR04521  20 ALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAkkkkkLKDLRKKVGLVFQfpEHQLFEE- 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  109 TVAGNIAFSLAVRGISRRDAKERVEWAIELVrlnGLE----HRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAALDR 184
Cdd:TIGR04521  99 TVYKDIAFGPKNLGLSEEEAEERVKEALELV---GLDeeylERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDP 175

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 914601027  185 KLREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELYRQP 243
Cdd:TIGR04521 176 KGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDV 234
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
 21-239 1.53e-60

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: 195.65  E-value: 1.53e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  21 AIEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQ--RDIGLV 98
Cdd:COG1120    1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRElaRRIAYV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  99 FQSYALFPNMTVA-----GNIAFSLAVRGISRRDaKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLL 173
Cdd:COG1120   81 PQEPPAPFGLTVRelvalGRYPHLGLFGRPSAED-REAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLL 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 914601027 174 LLDEPLAALDRKLREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGEL 239
Cdd:COG1120  160 LLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
22-252 2.62e-60

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 194.54  E-value: 2.62e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  22 IEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQRDI----GL 97
Cdd:PRK09493   2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIrqeaGM 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  98 VFQSYALFPNMTVAGNIAFS-LAVRGISRRDAKERvewAIELVRLNGLEHRK---PSQLSGGQQQRVAIARALVFGPKLL 173
Cdd:PRK09493  82 VFQQFYLFPHLTALENVMFGpLRVRGASKEEAEKQ---ARELLAKVGLAERAhhyPSELSGGQQQRVAIARALAVKPKLM 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 914601027 174 LLDEPLAALDRKLREEVrLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELYRQPANRFVAGFL 252
Cdd:PRK09493 159 LFDEPTSALDPELRHEV-LKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFL 236
ECF_ATPase_1 TIGR04520
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
 22-242 5.60e-60

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: 194.57  E-value: 5.60e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   22 IEVSGLSKHF--GTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIG---SRDVTHVPPAQRDIG 96
Cdd:TIGR04520   1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDgldTLDEENLWEIRKKVG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   97 LVFQSyalfP-----NMTVAGNIAFSLAVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPK 171
Cdd:TIGR04520  81 MVFQN----PdnqfvGATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPD 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 914601027  172 LLLLDEPLAALDRKLREEVRLELRRLQGTLGVTTVLVTHDQDEAMsMSDRIAVLAQGVIQQLGSPGELYRQ 242
Cdd:TIGR04520 157 IIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAV-LADRVIVMNKGKIVAEGTPREIFSQ 226
TauB COG4525
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
19-250 5.80e-60

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


Pssm-ID: 443596 [Multi-domain]  Cd Length: 262  Bit Score: 194.31  E-value: 5.80e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  19 RPAIEVSGLSKHFG----TVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHvPPAQRd 94
Cdd:COG4525    1 MSMLTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG-PGADR- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  95 iGLVFQSYALFPNMTVAGNIAFSLAVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLL 174
Cdd:COG4525   79 -GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 175 LDEPLAALDRKLREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAqgviqqlGSPGELYRQP----ANRFVAG 250
Cdd:COG4525  158 MDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMS-------PGPGRIVERLeldfSRRFLAG 230
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
 15-232 7.72e-59

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: 190.34  E-value: 7.72e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  15 PVSRRPAIEVSGLSKHF----GTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPP 90
Cdd:COG4181    2 SSSSAPIIELRGLTKTVgtgaGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  91 AQR------DIGLVFQSYALFPNMTVAGNIAFSLAVRGisRRDAKERVEWAIELVrlnGLEHR---KPSQLSGGQQQRVA 161
Cdd:COG4181   82 DARarlrarHVGFVFQSFQLLPTLTALENVMLPLELAG--RRDARARARALLERV---GLGHRldhYPAQLSGGEQQRVA 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 914601027 162 IARALVFGPKLLLLDEPLAALDRKLREEVRLELRRLQGTLGVTTVLVTHDQDEAmSMSDRIAVLAQGVIQQ 232
Cdd:COG4181  157 LARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALA-ARCDRVLRLRAGRLVE 226
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
 17-244 8.38e-59

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


Pssm-ID: 443658 [Multi-domain]  Cd Length: 329  Bit Score: 193.41  E-value: 8.38e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  17 SRRPAIEVSGLSKHF-----------GTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDV 85
Cdd:COG4608    3 MAEPLLEVRDLKKHFpvrgglfgrtvGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  86 THVPPAQ-----RDIGLVFQ-SYA-LFPNMTVAGNIAFSLAVRGI-SRRDAKERVEWAIELVRLNGlEH--RKPSQLSGG 155
Cdd:COG4608   83 TGLSGRElrplrRRMQMVFQdPYAsLNPRMTVGDIIAEPLRIHGLaSKAERRERVAELLELVGLRP-EHadRYPHEFSGG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 156 QQQRVAIARALVFGPKLLLLDEPLAALDRKLREEVRLELRRLQGTLGVTTVLVTHDqdeaMSM----SDRIAVLAQGVIQ 231
Cdd:COG4608  162 QRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHD----LSVvrhiSDRVAVMYLGKIV 237

                        250
                 ....*....|...
gi 914601027 232 QLGSPGELYRQPA 244
Cdd:COG4608  238 EIAPRDELYARPL 250
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
 22-239 8.52e-59

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: 190.02  E-value: 8.52e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  22 IEVSGLSKHFGTVC--AVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDV-THVPPAQRDIGLV 98
Cdd:cd03263    1 LQIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIrTDRKAARQSLGYC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  99 FQSYALFPNMTVAGNIAFSLAVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEP 178
Cdd:cd03263   81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 914601027 179 LAALDRKLREEVRLELRRLQGtlGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGEL 239
Cdd:cd03263  161 TSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
 20-244 4.97e-58

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 188.76  E-value: 4.97e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  20 PAIEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHvppAQRDIGLVF 99
Cdd:COG1121    5 PAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR---ARRRIGYVP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 100 QSYAL---FPnMTVA-----GNIAFSLAVRGISRRDaKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPK 171
Cdd:COG1121   82 QRAEVdwdFP-ITVRdvvlmGRYGRRGLFRRPSRAD-REAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPD 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 914601027 172 LLLLDEPLAALDRKLREEV-RLeLRRLQGTlGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQlGSPGELYRQPA 244
Cdd:COG1121  160 LLLLDEPFAGVDAATEEALyEL-LRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRGLVAH-GPPEEVLTPEN 230
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
 22-248 9.27e-58

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 191.17  E-value: 9.27e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  22 IEVSGLSKHF----GTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPP-----AQ 92
Cdd:PRK11153   2 IELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEkelrkAR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  93 RDIGLVFQSYALFPNMTVAGNIAFSLAVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKL 172
Cdd:PRK11153  82 RQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 173 LLLDEPLAALDRKLREEVrLEL-RRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELYRQP----ANRF 247
Cdd:PRK11153 162 LLCDEATSALDPATTRSI-LELlKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPkhplTREF 240


                 .
gi 914601027 248 V 248
Cdd:PRK11153 241 I 241
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
 22-239 4.14e-57

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: 185.72  E-value: 4.14e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  22 IEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPP---AQRDIGLV 98
Cdd:cd03224    1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPherARAGIGYV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  99 FQSYALFPNMTVAGNIAfsLAVRGISRRDAKERVEWAIELV-RLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDE 177
Cdd:cd03224   81 PEGRRIFPELTVEENLL--LGAYARRRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDE 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 914601027 178 PLAALDRKLREEVRLELRRLQGTlGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGEL 239
Cdd:cd03224  159 PSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
 22-244 8.45e-57

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: 187.95  E-value: 8.45e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  22 IEVSGLSKHF----GTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQP---TGGRIVIGSRDVTHVPPAQ-- 92
Cdd:COG0444    2 LEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKElr 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  93 ----RDIGLVFQ-SY-ALFPNMTVAGNIAFSLAV-RGISRRDAKERVEWAIELVRLNGLEHRK---PSQLSGGQQQRVAI 162
Cdd:COG0444   82 kirgREIQMIFQdPMtSLNPVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLPDPERRLdryPHELSGGMRQRVMI 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 163 ARALVFGPKLLLLDEPLAALDRKLREEVrLEL-RRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELYR 241
Cdd:COG0444  162 ARALALEPKLLIADEPTTALDVTIQAQI-LNLlKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELFE 240


                 ...
gi 914601027 242 QPA 244
Cdd:COG0444  241 NPR 243
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
 22-239 1.04e-56

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: 185.46  E-value: 1.04e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  22 IEVSGLSKHFGT-VCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPP-----AQRDI 95
Cdd:cd03256    1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGkalrqLRRQI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  96 GLVFQSYALFPNMTVAGNI-----AFSLAVRGISRRDAKERVEWAIEL---VRLNGLEHRKPSQLSGGQQQRVAIARALV 167
Cdd:cd03256   81 GMIFQQFNLIERLSVLENVlsgrlGRRSTWRSLFGLFPKEEKQRALAAlerVGLLDKAYQRADQLSGGQQQRVAIARALM 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 914601027 168 FGPKLLLLDEPLAALDRKLREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGEL 239
Cdd:cd03256  161 QQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
 23-238 1.47e-56

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


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 183.84  E-value: 1.47e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  23 EVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQP---TGGRIVIGSRDVTHVPPAQRDIGLVF 99
Cdd:COG4136    3 SLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAEQRRIGILF 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 100 QSYALFPNMTVAGNIAFSLAvRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPL 179
Cdd:COG4136   83 QDDLLFPHLSVGENLAFALP-PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPF 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 180 AALDRKLREEVR-LELRRLQgTLGVTTVLVTHDQDEAmsmsdriavLAQGVIQQLGSPGE 238
Cdd:COG4136  162 SKLDAALRAQFReFVFEQIR-QRGIPALLVTHDEEDA---------PAAGRVLDLGNWQH 211
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
 39-234 4.11e-56

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: 183.44  E-value: 4.11e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   39 DVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPaqrDIGLVFQSYALFPNMTVAGNIAFSL 118
Cdd:TIGR01184   3 GVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGP---DRMVVFQNYSLLPWLTVRENIALAV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  119 --AVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAALDRKLREEVRLELRR 196
Cdd:TIGR01184  80 drVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQ 159

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 914601027  197 LQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLG 234
Cdd:TIGR01184 160 IWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIG 197
ABC_phnC TIGR02315
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ...
 22-246 2.25e-55

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: 182.11  E-value: 2.25e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   22 IEVSGLSKHFGT-VCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVP-----PAQRDI 95
Cdd:TIGR02315   2 LEVENLSKVYPNgKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRgkklrKLRRRI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   96 GLVFQSYALFPNMTVAGNI-----AFSLAVRGISRRDAKERVEWAIELVRLNGLE---HRKPSQLSGGQQQRVAIARALV 167
Cdd:TIGR02315  82 GMIFQHYNLIERLTVLENVlhgrlGYKPTWRSLLGRFSEEDKERALSALERVGLAdkaYQRADQLSGGQQQRVAIARALA 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 914601027  168 FGPKLLLLDEPLAALDRKLREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELYRQPANR 246
Cdd:TIGR02315 162 QQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDDEVLRH 240
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
22-230 1.04e-54

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 178.86  E-value: 1.04e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  22 IEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQ--RDIGLVF 99
Cdd:COG4619    1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwrRQVAYVP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 100 QSYALFPNmTVAGNIAFSLAVRGisRRDAKERVEWAIELVRLN-GLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEP 178
Cdd:COG4619   81 QEPALWGG-TVRDNLPFPFQLRE--RKFDRERALELLERLGLPpDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEP 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 914601027 179 LAALDRKLREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVI 230
Cdd:COG4619  158 TSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
 22-239 8.29e-54

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: 177.18  E-value: 8.29e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  22 IEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVP-PAQRDIGLVFQ 100
Cdd:cd03265    1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPrEVRRRIGIVFQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 101 SYALFPNMTVAGNIAFSLAVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLA 180
Cdd:cd03265   81 DLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 914601027 181 ALDRKLREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGEL 239
Cdd:cd03265  161 GLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
 22-230 1.50e-53

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: 174.89  E-value: 1.50e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  22 IEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDV-THVPPAQRDIGLVFQ 100
Cdd:cd03230    1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIkKEPEEVKRRIGYLPE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 101 SYALFPNMTVAGNIafslavrgisrrdakervewaielvrlnglehrkpsQLSGGQQQRVAIARALVFGPKLLLLDEPLA 180
Cdd:cd03230   81 EPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTS 124

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 914601027 181 ALDRKLREEVRLELRRLQGTlGVTTVLVTHDQDEAMSMSDRIAVLAQGVI 230
Cdd:cd03230  125 GLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
 27-336 1.70e-53

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: 180.69  E-value: 1.70e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   27 LSKHFGTVCAvsDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIG------SRDVTHVPPAQRDIGLVFQ 100
Cdd:TIGR02142   5 FSKRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNgrtlfdSRKGIFLPPEKRRIGYVFQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  101 SYALFPNMTVAGNIAFslavrGISRRDAKERVEWAIELVRLNGLEH---RKPSQLSGGQQQRVAIARALVFGPKLLLLDE 177
Cdd:TIGR02142  83 EARLFPHLSVRGNLRY-----GMKRARPSERRISFERVIELLGIGHllgRLPGRLSGGEKQRVAIGRALLSSPRLLLMDE 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  178 PLAALDRKLREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELYRQPANRFVAgFLGAANL 257
Cdd:TIGR02142 158 PLAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPWLA-REDQGSL 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  258 FHGIIAR--EGNG-AVLALDGGtRLPLAGDYPSLGRRATMLVRPERVNL-QPATEAPANRFCIDCHVADvVYQGEIVRYA 333
Cdd:TIGR02142 237 IEGVVAEhdQHYGlTALRLGGG-HLWVPENLGPTGARLRLRVPARDVSLaLQKPEATSIRNILPARVVE-IEDSDIGRVG 314


                  ...
gi 914601027  334 VEA 336
Cdd:TIGR02142 315 VVL 317
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
 22-239 4.45e-53

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: 175.45  E-value: 4.45e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  22 IEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLI-----QPTGGRIVIGSRDVTHVPPA----Q 92
Cdd:cd03260    1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYDLDVDvlelR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  93 RDIGLVFQSYALFPnMTVAGNIAFSLAVRGISRRDA-KERVEWAIELVRLNGLEHRK--PSQLSGGQQQRVAIARALVFG 169
Cdd:cd03260   81 RRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEElDERVEEALRKAALWDEVKDRlhALGLSGGQQQRLCLARALANE 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 170 PKLLLLDEPLAALDRKLREEVRLELRRLQGTlgVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGEL 239
Cdd:cd03260  160 PEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
36-242 5.20e-53

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 177.13  E-value: 5.20e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  36 AVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTH--VPPAQRDIGLVFQSY-ALFPNMTVAG 112
Cdd:PRK13635  22 ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEetVWDVRRQVGMVFQNPdNQFVGATVQD 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 113 NIAFSLAVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAALDRKLREEVRL 192
Cdd:PRK13635 102 DVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLE 181

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 914601027 193 ELRRLQGTLGVTTVLVTHDQDEAMSmSDRIAVLAQGVIQQLGSPGELYRQ 242
Cdd:PRK13635 182 TVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFKS 230
FtsE TIGR02673
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ...
 22-228 5.64e-53

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: 174.74  E-value: 5.64e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   22 IEVSGLSKHFGTVC-AVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTH-----VPPAQRDI 95
Cdd:TIGR02673   2 IEFHNVSKAYPGGVaALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRlrgrqLPLLRRRI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   96 GLVFQSYALFPNMTVAGNIAFSLAVRGISRRDAKERVEWAIELVrlnGLEHRK---PSQLSGGQQQRVAIARALVFGPKL 172
Cdd:TIGR02673  82 GVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQV---GLEHKAdafPEQLSGGEQQRVAIARAIVNSPPL 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 914601027  173 LLLDEPLAALDRKLREEVRLELRRLQgTLGVTTVLVTHDQDEAMSMSDRIAVLAQG 228
Cdd:TIGR02673 159 LLADEPTGNLDPDLSERILDLLKRLN-KRGTTVIVATHDLSLVDRVAHRVIILDDG 213
ABC_ATP_DarD NF038007
darobactin export ABC transporter ATP-binding protein;
36-228 1.14e-52

darobactin export ABC transporter ATP-binding protein;


Pssm-ID: 411600 [Multi-domain]  Cd Length: 218  Bit Score: 174.14  E-value: 1.14e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  36 AVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQRD------IGLVFQSYALFPNMT 109
Cdd:NF038007  20 VLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSYSQKIilrrelIGYIFQSFNLIPHLS 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 110 VAGNIAFSLAVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAALDRKLREE 189
Cdd:NF038007 100 IFDNVALPLKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNPALLLADEPTGNLDSKNARA 179

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 914601027 190 VRLELRRLQGTlGVTTVLVTHdQDEAMSMSDRIAVLAQG 228
Cdd:NF038007 180 VLQQLKYINQK-GTTIIMVTH-SDEASTYGNRIINMKDG 216
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
 39-230 1.80e-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: 173.45  E-value: 1.80e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  39 DVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQRDIGLVFQSYALFPNMTVAGNIAFSL 118
Cdd:cd03298   16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQENNLFAHLTVEQNVGLGL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 119 AVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAALDRKLREEVRLELRRLQ 198
Cdd:cd03298   96 SPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLH 175

                        170       180       190
                 ....*....|....*....|....*....|..
gi 914601027 199 GTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVI 230
Cdd:cd03298  176 AETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
 21-252 2.88e-52

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 174.05  E-value: 2.88e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  21 AIEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSR--DVTHVPPAQ------ 92
Cdd:PRK11124   2 SIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSKTPSDKairelr 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  93 RDIGLVFQSYALFPNMTVAGN-IAFSLAVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPK 171
Cdd:PRK11124  82 RNVGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQ 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 172 LLLLDEPLAALDRKLREEVRLELRRLQGTlGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSpGELYRQPANRFVAGF 251
Cdd:PRK11124 162 VLLFDEPTAALDPEITAQIVSIIRELAET-GITQVIVTHEVEVARKTASRVVYMENGHIVEQGD-ASCFTQPQTEAFKNY 239


                 .
gi 914601027 252 L 252
Cdd:PRK11124 240 L 240
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
21-252 2.87e-51

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


Pssm-ID: 443326 [Multi-domain]  Cd Length: 242  Bit Score: 171.35  E-value: 2.87e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  21 AIEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSR--DVTHVPPAQ------ 92
Cdd:COG4161    2 SIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfDFSQKPSEKairllr 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  93 RDIGLVFQSYALFPNMTVAGN-IAFSLAVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPK 171
Cdd:COG4161   82 QKVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQ 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 172 LLLLDEPLAALDRKLREEVRLELRRLQGTlGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSpGELYRQPANRFVAGF 251
Cdd:COG4161  162 VLLFDEPTAALDPEITAQVVEIIRELSQT-GITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD-ASHFTQPQTEAFAHY 239


                 .
gi 914601027 252 L 252
Cdd:COG4161  240 L 240
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
16-257 4.41e-51

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


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 175.61  E-value: 4.41e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  16 VSRRPAIEVSGLSkhfgtvCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQ--- 92
Cdd:PRK10070  29 LSKEQILEKTGLS------LGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAElre 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  93 ---RDIGLVFQSYALFPNMTVAGNIAFSLAVRGISrrdAKERVEWAIELVRLNGLE---HRKPSQLSGGQQQRVAIARAL 166
Cdd:PRK10070 103 vrrKKIAMVFQSFALMPHMTVLDNTAFGMELAGIN---AEERREKALDALRQVGLEnyaHSYPDELSGGMRQRVGLARAL 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 167 VFGPKLLLLDEPLAALDRKLREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELYRQPANR 246
Cdd:PRK10070 180 AINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPAND 259

                        250
                 ....*....|.
gi 914601027 247 FVAGFLGAANL 257
Cdd:PRK10070 260 YVRTFFRGVDI 270
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
 20-244 6.16e-51

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: 170.16  E-value: 6.16e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  20 PAIEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPP---AQRDIG 96
Cdd:COG0410    2 PMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPhriARLGIG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  97 LVFQSYALFPNMTVAGNIAFSLAVRGiSRRDAKERVEWAIELV-RLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLL 175
Cdd:COG0410   82 YVPEGRRIFPSLTVEENLLLGAYARR-DRAEVRADLERVYELFpRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 914601027 176 DEPLAALDRKLREEVRLELRRLQGTlGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELYRQPA 244
Cdd:COG0410  161 DEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPE 228
HisP COG4598
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
15-252 9.46e-51

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


Pssm-ID: 443652 [Multi-domain]  Cd Length: 259  Bit Score: 170.37  E-value: 9.46e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  15 PVSRRPAIEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVP----- 89
Cdd:COG4598    2 TDTAPPALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPdrdge 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  90 --PAQRD--------IGLVFQSYALFPNMTVAGNIAFS-LAVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQ 158
Cdd:COG4598   82 lvPADRRqlqrirtrLGMVFQSFNLWSHMTVLENVIEApVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQ 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 159 RVAIARALVFGPKLLLLDEPLAALDRKLREEVrleLRRLQGtL---GVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGS 235
Cdd:COG4598  162 RAAIARALAMEPEVMLFDEPTSALDPELVGEV---LKVMRD-LaeeGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGP 237

                        250
                 ....*....|....*..
gi 914601027 236 PGELYRQPANRFVAGFL 252
Cdd:COG4598  238 PAEVFGNPKSERLRQFL 254
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
 36-244 1.48e-50

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 170.97  E-value: 1.48e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  36 AVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVT------HVPPAQRDIGLVFQsyalFPNM- 108
Cdd:PRK13634  22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkknkKLKPLRKKVGIVFQ----FPEHq 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 109 ----TVAGNIAFSLAVRGISRRDAKERVEWAIELVRLN-GLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAALD 183
Cdd:PRK13634  98 lfeeTVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPeELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLD 177

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 914601027 184 RKLREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELYRQPA 244
Cdd:PRK13634 178 PKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
 22-230 1.92e-50

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: 168.36  E-value: 1.92e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  22 IEVSGLSKHF-GTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTH-----VPPAQRDI 95
Cdd:cd03292    1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDlrgraIPYLRRKI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  96 GLVFQSYALFPNMTVAGNIAFSLAVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLL 175
Cdd:cd03292   81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 914601027 176 DEPLAALDRKLREEVrLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVI 230
Cdd:cd03292  161 DEPTGNLDPDTTWEI-MNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 22-230 2.63e-50

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


Pssm-ID: 440718 [Multi-domain]  Cd Length: 264  Bit Score: 169.50  E-value: 2.63e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  22 IEVSGLSKHF--GTV---CAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQR--D 94
Cdd:COG1101    2 LELKNLSKTFnpGTVnekRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRakY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  95 IGLVFQSYAL--FPNMTVAGNIAFSLA---VRGISRRDAKERVEWAIELVRL--NGLEHR---KPSQLSGGQQQRVAIAR 164
Cdd:COG1101   82 IGRVFQDPMMgtAPSMTIEENLALAYRrgkRRGLRRGLTKKRRELFRELLATlgLGLENRldtKVGLLSGGQRQALSLLM 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 914601027 165 ALVFGPKLLLLDEPLAALDRKLREEVrLEL-RRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVI 230
Cdd:COG1101  162 ATLTKPKLLLLDEHTAALDPKTAALV-LELtEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRI 227
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
 23-230 3.07e-50

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: 167.71  E-value: 3.07e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  23 EVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVppaQRDIGLVFQSY 102
Cdd:cd03235    1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE---RKRIGYVPQRR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 103 AL---FPnMTVA-----GNIAFSLAVRGISRRDaKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLL 174
Cdd:cd03235   78 SIdrdFP-ISVRdvvlmGLYGHKGLFRRLSKAD-KAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLL 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 914601027 175 LDEPLAALDRKLREE-VRLeLRRLQGtLGVTTVLVTHDQDEAMSMSDRIAVLAQGVI 230
Cdd:cd03235  156 LDEPFAGVDPKTQEDiYEL-LRELRR-EGMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
21-250 1.43e-49

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 167.18  E-value: 1.43e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  21 AIEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHvPPAQRdiGLVFQ 100
Cdd:PRK11248   1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG-PGAER--GVVFQ 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 101 SYALFPNMTVAGNIAFSLAVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLA 180
Cdd:PRK11248  78 NEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFG 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 914601027 181 ALDRKLREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGviqqlgsPGE-LYRQPAN---RFVAG 250
Cdd:PRK11248 158 ALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG-------PGRvVERLPLNfarRFVAG 224
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
 23-234 2.46e-49

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: 164.15  E-value: 2.46e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  23 EVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQ--RDIGLVFQ 100
Cdd:cd03214    1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKElaRKIAYVPQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 101 syalfpnmtvagniafslavrgisrrdakervewAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLA 180
Cdd:cd03214   81 ----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTS 126

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 914601027 181 ALDRKLREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLG 234
Cdd:cd03214  127 HLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 37-180 3.21e-49

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: 162.82  E-value: 3.21e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   37 VSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTH--VPPAQRDIGLVFQSYALFPNMTVAGNI 114
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDdeRKSLRKEIGYVFQDPQLFPRLTVRENL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  115 AFSLAVRGISRRDAKERVEWAIELVRLNGLEHRK----PSQLSGGQQQRVAIARALVFGPKLLLLDEPLA 180
Cdd:pfam00005  81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
 20-215 4.68e-49

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: 164.19  E-value: 4.68e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  20 PAIEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPA-QRDIGLV 98
Cdd:COG4133    1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDyRRRLAYL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  99 FQSYALFPNMTVAGNIAFSLAVRGisRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEP 178
Cdd:COG4133   81 GHADGLKPELTVRENLRFWAALYG--LRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEP 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 914601027 179 LAALDRK----LREEVRLELRRlqgtlGVTTVLVTHDQDEA 215
Cdd:COG4133  159 FTALDAAgvalLAELIAAHLAR-----GGAVLLTTHQPLEL 194
cbiO PRK13637
energy-coupling factor transporter ATPase;
36-242 6.14e-49

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 166.76  E-value: 6.14e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  36 AVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQRDI----GLVFQ--SYALFPNmT 109
Cdd:PRK13637  22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDIrkkvGLVFQypEYQLFEE-T 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 110 VAGNIAFSLAVRGISRRDAKERVEWAIELVRL--NGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAALDRKLR 187
Cdd:PRK13637 101 IEKDIAFGPINLGLSEEEIENRVKRAMNIVGLdyEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGR 180

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 914601027 188 EEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELYRQ 242
Cdd:PRK13637 181 DEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKE 235
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
 22-234 1.11e-48

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: 163.52  E-value: 1.11e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  22 IEVSGLSKHFGTVCAVSDVDLTVAEGeFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQRD-IGLVFQ 100
Cdd:cd03264    1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRrIGYLPQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 101 SYALFPNMTVAGNIAFSLAVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLA 180
Cdd:cd03264   80 EFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 914601027 181 ALDrklrEEVRLELRRLQGTLG--VTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLG 234
Cdd:cd03264  160 GLD----PEERIRFRNLLSELGedRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
thiQ TIGR01277
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ...
 41-234 1.53e-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: 163.49  E-value: 1.53e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   41 DLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQRDIGLVFQSYALFPNMTVAGNIAFSLAV 120
Cdd:TIGR01277  18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSMLFQENNLFAHLTVRQNIGLGLHP 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  121 RGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAALDRKLREEVRLELRRLQGT 200
Cdd:TIGR01277  98 GLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLCSE 177

                         170       180       190
                  ....*....|....*....|....*....|....
gi 914601027  201 LGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLG 234
Cdd:TIGR01277 178 RQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
 4-239 2.13e-48

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: 173.87  E-value: 2.13e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   4 HQLTSERDTLAPVSRRP----AIEVSGLSKHFG--TVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGR 77
Cdd:COG2274  452 LDLPPEREEGRSKLSLPrlkgDIELENVSFRYPgdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGR 531

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  78 IVIGSRDVTHVPPAQ--RDIGLVFQSYALFpNMTVAGNIAFslavrgiSRRDA-KERVEWAIELVRL--------NGLEH 146
Cdd:COG2274  532 ILIDGIDLRQIDPASlrRQIGVVLQDVFLF-SGTIRENITL-------GDPDAtDEEIIEAARLAGLhdfiealpMGYDT 603

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 147 R---KPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAALDRKLREEVRLELRRLQGtlGVTTVLVTHDqDEAMSMSDRIA 223
Cdd:COG2274  604 VvgeGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHR-LSTIRLADRII 680

                        250
                 ....*....|....*.
gi 914601027 224 VLAQGVIQQLGSPGEL 239
Cdd:COG2274  681 VLDKGRIVEDGTHEEL 696
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
41-239 4.32e-48

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 162.83  E-value: 4.32e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  41 DLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQRDIGLVFQSYALFPNMTVAGNIAFSLAV 120
Cdd:PRK10771  19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQENNLFSHLTVAQNIGLGLNP 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 121 RGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAALDRKLREEVRLELRRLQGT 200
Cdd:PRK10771  99 GLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQE 178

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 914601027 201 LGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGEL 239
Cdd:PRK10771 179 RQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
 22-246 5.32e-48

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: 162.33  E-value: 5.32e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  22 IEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPP---AQRDIGLV 98
Cdd:cd03218    1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMhkrARLGIGYL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  99 FQSYALFPNMTVAGNIAFSLAVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEP 178
Cdd:cd03218   81 PQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 179 LAALDRKLREEVRLELRRL-QGTLGvttVLVT-HDQDEAMSMSDRIAVLAQGVIQQLGSPGELYRQPANR 246
Cdd:cd03218  161 FAGVDPIAVQDIQKIIKILkDRGIG---VLITdHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVR 227
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
 14-242 1.06e-47

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: 169.94  E-value: 1.06e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  14 APVSRRPAIEVSGLS-KHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPA- 91
Cdd:COG4988  329 LPAAGPPSIELEDVSfSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPAs 408

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  92 -QRDIGLVFQSYALFPnMTVAGNIAFslavrgiSRRDA-KERVEWAIELVRL--------NGLEHR---KPSQLSGGQQQ 158
Cdd:COG4988  409 wRRQIAWVPQNPYLFA-GTIRENLRL-------GRPDAsDEELEAALEAAGLdefvaalpDGLDTPlgeGGRGLSGGQAQ 480

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 159 RVAIARALVFGPKLLLLDEPLAALDRKLREEVRLELRRLQGtlGVTTVLVTHDQDEAMSMsDRIAVLAQGVIQQLGSPGE 238
Cdd:COG4988  481 RLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLAQA-DRILVLDDGRIVEQGTHEE 557


                 ....
gi 914601027 239 LYRQ 242
Cdd:COG4988  558 LLAK 561
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
 20-228 1.67e-47

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 168.28  E-value: 1.67e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  20 PAIEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQ---RDIG 96
Cdd:COG3845    4 PALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDaiaLGIG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  97 LVFQSYALFPNMTVAGNIAFSLAVRG---ISRRDAKERVEwaiELVRLNGLE---HRKPSQLSGGQQQRVAIARALVFGP 170
Cdd:COG3845   84 MVHQHFMLVPNLTVAENIVLGLEPTKggrLDRKAARARIR---ELSERYGLDvdpDAKVEDLSVGEQQRVEILKALYRGA 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 914601027 171 KLLLLDEPLAALDRKLREEVRLELRRLQGTlGVTTVLVTHDQDEAMSMSDRIAVLAQG 228
Cdd:COG3845  161 RILILDEPTAVLTPQEADELFEILRRLAAE-GKSIIFITHKLREVMAIADRVTVLRRG 217
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
 22-230 2.47e-47

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: 160.23  E-value: 2.47e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  22 IEVSGLSKHF----GTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVP-PAQRDIG 96
Cdd:cd03266    2 ITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPaEARRRLG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  97 LVFQSYALFPNMTVAGNIAFSLAVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLD 176
Cdd:cd03266   82 FVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 914601027 177 EPLAALD----RKLREEVRlELRRlqgtLGVTTVLVTHDQDEAMSMSDRIAVLAQGVI 230
Cdd:cd03266  162 EPTTGLDvmatRALREFIR-QLRA----LGKCILFSTHIMQEVERLCDRVVVLHRGRV 214
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
 14-243 1.72e-46

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: 166.01  E-value: 1.72e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  14 APVSRRPAIEVSGLSKHF-----------GTVCAVSDVDLTVAEGEFLSILGPSGSGKSTL----LGLVagliqPTGGRI 78
Cdd:COG4172  268 VPPDAPPLLEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLglalLRLI-----PSEGEI 342

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  79 VIGSRDVTHVPPAQ-----RDIGLVFQS-YA-LFPNMTVAGNIAFSLAV--RGISRRDAKERVEWAIELVRLN-GLEHRK 148
Cdd:COG4172  343 RFDGQDLDGLSRRAlrplrRRMQVVFQDpFGsLSPRMTVGQIIAEGLRVhgPGLSAAERRARVAEALEEVGLDpAARHRY 422

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 149 PSQLSGGQQQRVAIARALVFGPKLLLLDEPLAALDRKLREEVrLEL-RRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQ 227
Cdd:COG4172  423 PHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQI-LDLlRDLQREHGLAYLFISHDLAVVRALAHRVMVMKD 501

                        250
                 ....*....|....*.
gi 914601027 228 GVIQQLGSPGELYRQP 243
Cdd:COG4172  502 GKVVEQGPTEQVFDAP 517
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
 23-228 2.40e-46

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: 155.48  E-value: 2.40e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  23 EVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQ--RDIGLVFQ 100
Cdd:cd00267    1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEElrRRIGYVPQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 101 syalfpnmtvagniafslavrgisrrdakervewaielvrlnglehrkpsqLSGGQQQRVAIARALVFGPKLLLLDEPLA 180
Cdd:cd00267   81 ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 914601027 181 ALDRKLREEVRLELRRLQGTlGVTTVLVTHDQDEAMSMSDRIAVLAQG 228
Cdd:cd00267  110 GLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDG 156
L_ocin_972_ABC TIGR03608
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ...
 24-222 3.31e-46

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: 157.01  E-value: 3.31e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   24 VSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQ-----RD-IGL 97
Cdd:TIGR03608   1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKaskfrREkLGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   98 VFQSYALFPNMTVAGNIAFSLAVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDE 177
Cdd:TIGR03608  81 LFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADE 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 914601027  178 PLAALDRKLREEVrLELRRLQGTLGVTTVLVTHDQdEAMSMSDRI 222
Cdd:TIGR03608 161 PTGSLDPKNRDEV-LDLLLELNDEGKTIIIVTHDP-EVAKQADRV 203
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
20-225 8.63e-46

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 163.65  E-value: 8.63e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  20 PAIEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPP--AQRD-IG 96
Cdd:COG1129    3 PLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPrdAQAAgIA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  97 LVFQSYALFPNMTVAGNIAFSLAVRGISRRDAKERVEWAIELVRLNGLE---HRKPSQLSGGQQQRVAIARALVFGPKLL 173
Cdd:COG1129   83 IIHQELNLVPNLSVAENIFLGREPRRGGLIDWRAMRRRARELLARLGLDidpDTPVGDLSVAQQQLVEIARALSRDARVL 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 914601027 174 LLDEPLAALDRKlreEVR--LEL-RRLQGTlGVTTVLVTHDQDEAMSMSDRIAVL 225
Cdd:COG1129  163 ILDEPTASLTER---EVErlFRIiRRLKAQ-GVAIIYISHRLDEVFEIADRVTVL 213
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
 12-246 1.11e-45

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


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 157.12  E-value: 1.11e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  12 TLAPVSRRPAIEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLL-------GLVAGliQPTGGRIVIGSRD 84
Cdd:COG1117    2 TAPASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLrclnrmnDLIPG--ARVEGEILLDGED 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  85 V--THVPPAQ--RDIGLVFQSYALFPnMTVAGNIAFSLAVRGI-SRRDAKERVEWAIELV--------RLngleHRKPSQ 151
Cdd:COG1117   80 IydPDVDVVElrRRVGMVFQKPNPFP-KSIYDNVAYGLRLHGIkSKSELDEIVEESLRKAalwdevkdRL----KKSALG 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 152 LSGGQQQRVAIARALVFGPKLLLLDEPLAALD----RKLrEEVRLELRRlqgtlGVTTVLVTHDQDEAMSMSDRIAVLAQ 227
Cdd:COG1117  155 LSGGQQQRLCIARALAVEPEVLLMDEPTSALDpistAKI-EELILELKK-----DYTIVIVTHNMQQAARVSDYTAFFYL 228

                        250
                 ....*....|....*....
gi 914601027 228 GVIQQLGSPGELYRQPANR 246
Cdd:COG1117  229 GELVEFGPTEQIFTNPKDK 247
cbiO PRK13650
energy-coupling factor transporter ATPase;
37-240 1.29e-45

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 157.59  E-value: 1.29e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  37 VSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVT--HVPPAQRDIGLVFQSY-ALFPNMTVAGN 113
Cdd:PRK13650  23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTeeNVWDIRHKIGMVFQNPdNQFVGATVEDD 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 114 IAFSLAVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAALDRKLREEVRLE 193
Cdd:PRK13650 103 VAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKT 182

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 914601027 194 LRRLQGTLGVTTVLVTHDQDEaMSMSDRIAVLAQGVIQQLGSPGELY 240
Cdd:PRK13650 183 IKGIRDDYQMTVISITHDLDE-VALSDRVLVMKNGQVESTSTPRELF 228
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
 24-230 1.67e-45

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 156.76  E-value: 1.67e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  24 VSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHvppAQRDIGLVFQSYA 103
Cdd:PRK11247  15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAE---AREDTRLMFQDAR 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 104 LFPNMTVAGNIAfsLAVRGISRRDAKErvewAIELVrlnGLEHRK---PSQLSGGQQQRVAIARALVFGPKLLLLDEPLA 180
Cdd:PRK11247  92 LLPWKKVIDNVG--LGLKGQWRDAALQ----ALAAV---GLADRAnewPAALSGGQKQRVALARALIHRPGLLLLDEPLG 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 914601027 181 ALDRKLREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVI 230
Cdd:PRK11247 163 ALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
 22-228 1.74e-45

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: 153.69  E-value: 1.74e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  22 IEVSGLSKHFGT--VCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPA--QRDIGL 97
Cdd:cd03228    1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLEslRKNIAY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  98 VFQSYALFpNMTVAGNIafslavrgisrrdakervewaielvrlnglehrkpsqLSGGQQQRVAIARALVFGPKLLLLDE 177
Cdd:cd03228   81 VPQDPFLF-SGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDE 122

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 914601027 178 PLAALDRKLREEVRLELRRLQGtlGVTTVLVTHDqDEAMSMSDRIAVLAQG 228
Cdd:cd03228  123 ATSALDPETEALILEALRALAK--GKTVIVIAHR-LSTIRDADRIIVLDDG 170
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
 21-254 2.04e-45

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 156.45  E-value: 2.04e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  21 AIEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIG------SRDVTH----VPP 90
Cdd:PRK11264   3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGditidtARSLSQqkglIRQ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  91 AQRDIGLVFQSYALFPNMTVAGN-IAFSLAVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFG 169
Cdd:PRK11264  83 LRQHVGFVFQNFNLFPHRTVLENiIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMR 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 170 PKLLLLDEPLAALDRKLREEVRLELRRLqGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELYRQP----AN 245
Cdd:PRK11264 163 PEVILFDEPTSALDPELVGEVLNTIRQL-AQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPqqprTR 241


                 ....*....
gi 914601027 246 RFVAGFLGA 254
Cdd:PRK11264 242 QFLEKFLLQ 250
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
 22-243 6.47e-45

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


Pssm-ID: 440752 [Multi-domain]  Cd Length: 240  Bit Score: 154.80  E-value: 6.47e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  22 IEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPP---AQRDIGLV 98
Cdd:COG1137    4 LEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMhkrARLGIGYL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  99 FQSYALFPNMTVAGNIAFSLAVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEP 178
Cdd:COG1137   84 PQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEP 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 914601027 179 LAALDRKLREEVRLELRRL--QGtLGvttVLVT-HDQDEAMSMSDRIAVLAQGVIQQLGSPGELYRQP 243
Cdd:COG1137  164 FAGVDPIAVADIQKIIRHLkeRG-IG---VLITdHNVRETLGICDRAYIISEGKVLAEGTPEEILNNP 227
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
5-242 3.05e-44

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 160.72  E-value: 3.05e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   5 QLTSERDTLAPVSRRPAIEVSGLSkhF---GTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIG 81
Cdd:COG1132  323 EIPDPPGAVPLPPVRGEIEFENVS--FsypGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILID 400

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  82 SRDVTHVPPAQ--RDIGLVFQSYALFpNMTVAGNIAFslavrgiSRRDA-KERVEWAIELVRLNGLEHRKP--------- 149
Cdd:COG1132  401 GVDIRDLTLESlrRQIGVVPQDTFLF-SGTIRENIRY-------GRPDAtDEEVEEAAKAAQAHEFIEALPdgydtvvge 472

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 150 --SQLSGGQQQRVAIARALVFGPKLLLLDEPLAALDRKLREEVRLELRRLQGtlGVTTVLVTHdqdeamSMS-----DRI 222
Cdd:COG1132  473 rgVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAH------RLStirnaDRI 544

                        250       260
                 ....*....|....*....|
gi 914601027 223 AVLAQGVIQQLGSPGELYRQ 242
Cdd:COG1132  545 LVLDDGRIVEQGTHEELLAR 564
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 21-277 3.70e-44

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


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 154.50  E-value: 3.70e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  21 AIEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVThvPPAQRDIGlvfq 100
Cdd:COG4152    1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD--PEDRRRIG---- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 101 sY-----ALFPNMTVAGNIAFSLAVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLL 175
Cdd:COG4152   75 -YlpeerGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLIL 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 176 DEPLAALD----RKLREEVRlELRRlqgtLGVTTVLVTHDQDEAMSMSDRIAVLAQG--VIQqlGSPGELYRQ-PANRFV 248
Cdd:COG4152  154 DEPFSGLDpvnvELLKDVIR-ELAA----KGTTVIFSSHQMELVEELCDRIVIINKGrkVLS--GSVDEIRRQfGRNTLR 226

                        250       260       270
                 ....*....|....*....|....*....|....
gi 914601027 249 AGFLGAANLFHGI-----IAREGNGAVLALDGGT 277
Cdd:COG4152  227 LEADGDAGWLRALpgvtvVEEDGDGAELKLEDGA 260
heterocyst_DevA TIGR02982
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ...
 21-222 4.71e-44

ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.


Pssm-ID: 274374 [Multi-domain]  Cd Length: 220  Bit Score: 151.71  E-value: 4.71e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   21 AIEVSGLSKHFGTVCA----VSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQ---- 92
Cdd:TIGR02982   1 VISIRNLNHYYGHGSLrkqvLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQlvql 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   93 -RDIGLVFQSYALFPNMTVAGNIAFSLAV-RGISRRDAKERvewAIELVRLNGLEHR---KPSQLSGGQQQRVAIARALV 167
Cdd:TIGR02982  81 rRRIGYIFQAHNLLGFLTARQNVQMALELqPNLSYQEARER---ARAMLEAVGLGDHlnyYPHNLSGGQKQRVAIARALV 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 914601027  168 FGPKLLLLDEPLAALDRKLREEVRLELRRLQGTLGVTTVLVTHDqDEAMSMSDRI 222
Cdd:TIGR02982 158 HHPKLVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHD-NRILDVADRI 211
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
 22-230 5.44e-44

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: 151.22  E-value: 5.44e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  22 IEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQRDIGLVFQS 101
Cdd:cd03268    1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIEA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 102 YALFPNMTVAGNIAFSLAVRGISrrdaKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAA 181
Cdd:cd03268   81 PGFYPNLTARENLRLLARLLGIR----KKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNG 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 914601027 182 LDRKLREEVRLELRRLQGTlGVTTVLVTHDQDEAMSMSDRIAVLAQGVI 230
Cdd:cd03268  157 LDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKL 204
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
 7-244 7.40e-44

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: 159.55  E-value: 7.40e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   7 TSERDTLAPVSRRPAIEVSGLSKHF--GTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRD 84
Cdd:COG4987  319 VTEPAEPAPAPGGPSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVD 398

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  85 VTHVPPAQ--RDIGLVFQSYALFpNMTVAGNIAfsLAvrgisRRDAK-ERVEWAIELVRLNGLEHRKP-----------S 150
Cdd:COG4987  399 LRDLDEDDlrRRIAVVPQRPHLF-DTTLRENLR--LA-----RPDATdEELWAALERVGLGDWLAALPdgldtwlgeggR 470

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 151 QLSGGQQQRVAIARALVFGPKLLLLDEPLAALDRKLREEVRLELRRLQGtlGVTTVLVTHDQdEAMSMSDRIAVLAQGVI 230
Cdd:COG4987  471 RLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRL-AGLERMDRILVLEDGRI 547

                        250
                 ....*....|....
gi 914601027 231 QQLGSPGELYRQPA 244
Cdd:COG4987  548 VEQGTHEELLAQNG 561
3a0107s01c2 TIGR00972
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ...
 21-252 1.49e-43

phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]


Pssm-ID: 273372 [Multi-domain]  Cd Length: 247  Bit Score: 151.29  E-value: 1.49e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   21 AIEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLL-------GLVAGliQPTGGRIVIGSRDV----THVP 89
Cdd:TIGR00972   1 AIEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLrslnrmnDLVPG--VRIEGKVLFDGQDIydkkIDVV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   90 PAQRDIGLVFQSYALFPnMTVAGNIAFSLAVRGI-SRRDAKERVEWAIELV--------RLngleHRKPSQLSGGQQQRV 160
Cdd:TIGR00972  79 ELRRRVGMVFQKPNPFP-MSIYDNIAYGPRLHGIkDKKELDEIVEESLKKAalwdevkdRL----HDSALGLSGGQQQRL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  161 AIARALVFGPKLLLLDEPLAALDRKLREEVRLELRRLQGTLgvTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELY 240
Cdd:TIGR00972 154 CIARALAVEPEVLLLDEPTSALDPIATGKIEELIQELKKKY--TIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQIF 231

                         250
                  ....*....|..
gi 914601027  241 RQPANRFVAGFL 252
Cdd:TIGR00972 232 TNPKEKRTEDYI 243
LolD_lipo_ex TIGR02211
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ...
 40-228 1.78e-43

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: 150.19  E-value: 1.78e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   40 VDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQR------DIGLVFQSYALFPNMTVAGN 113
Cdd:TIGR02211  24 VSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERaklrnkKLGFIYQFHHLLPDFTALEN 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  114 IAFSLAVRGISRRDAKERvewAIELVRLNGLEHR---KPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAALDRKLRE-- 188
Cdd:TIGR02211 104 VAMPLLIGKKSVKEAKER---AYEMLEKVGLEHRinhRPSELSGGERQRVAIARALVNQPSLVLADEPTGNLDNNNAKii 180

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 914601027  189 -EVRLELRRLQGTlgvTTVLVTHDQDEAMSMsDRIAVLAQG 228
Cdd:TIGR02211 181 fDLMLELNRELNT---SFLVVTHDLELAKKL-DRVLEMKDG 217
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
 22-230 2.93e-43

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: 147.58  E-value: 2.93e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  22 IEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVthvppaqrdiglvfqs 101
Cdd:cd03216    1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEV---------------- 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 102 yalfpnmtvagniAFSlavrgiSRRDAKERvewAIELVrlnglehrkpSQLSGGQQQRVAIARALVFGPKLLLLDEPLAA 181
Cdd:cd03216   65 -------------SFA------SPRDARRA---GIAMV----------YQLSVGERQMVEIARALARNARLLILDEPTAA 112

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 914601027 182 LDRKLREEVRLELRRLQGTlGVTTVLVTHDQDEAMSMSDRIAVLAQGVI 230
Cdd:cd03216  113 LTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRV 160
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
 22-230 7.35e-43

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: 148.20  E-value: 7.35e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  22 IEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVThvPPAQRDIGLVFQS 101
Cdd:cd03269    1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD--IAARNRIGYLPEE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 102 YALFPNMTVAGNIAFSLAVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAA 181
Cdd:cd03269   79 RGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSG 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 914601027 182 LD---RKLREEVRLELRRlqgtLGVTTVLVTHDQDEAMSMSDRIAVLAQGVI 230
Cdd:cd03269  159 LDpvnVELLKDVIRELAR----AGKTVILSTHQMELVEELCDRVLLLNKGRA 206
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
 20-238 2.34e-42

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 148.38  E-value: 2.34e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  20 PAIEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQ--RDIGL 97
Cdd:PRK13548   1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElaRRRAV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  98 VFQSYAL-FPnMTVAGNIAFSLAVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALV------FGP 170
Cdd:PRK13548  81 LPQHSSLsFP-FTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPP 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 914601027 171 KLLLLDEPLAALDRKLREEV-RLeLRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGE 238
Cdd:PRK13548 160 RWLLLDEPTSALDLAHQHHVlRL-ARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAE 227
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
39-246 3.52e-42

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 150.79  E-value: 3.52e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  39 DVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSR---DV---THVPPAQRDIGLVFQSYALFPNMTVAG 112
Cdd:PRK11144  16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAekgICLPPEKRRIGYVFQDARLFPHYKVRG 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 113 NIAFslavrGISRRDAKErvewAIELVRLNGLEH---RKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAALDRKLREE 189
Cdd:PRK11144  96 NLRY-----GMAKSMVAQ----FDKIVALLGIEPlldRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRE 166

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 914601027 190 VRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELYRQPANR 246
Cdd:PRK11144 167 LLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSAMR 223
COG4559 COG4559
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
22-238 1.58e-41

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


Pssm-ID: 443620 [Multi-domain]  Cd Length: 258  Bit Score: 146.41  E-value: 1.58e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  22 IEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQ--RDIGLVF 99
Cdd:COG4559    2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWElaRRRAVLP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 100 QSYAL-FPnMTVAGNIAFSLAVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALV-------FGPK 171
Cdd:COG4559   82 QHSSLaFP-FTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdGGPR 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 914601027 172 LLLLDEPLAALD--------RKLREEVRlelrrlQGtLGVTTVLvtHDQDEAMSMSDRIAVLAQGVIQQLGSPGE 238
Cdd:COG4559  161 WLFLDEPTSALDlahqhavlRLARQLAR------RG-GGVVAVL--HDLNLAAQYADRILLLHQGRLVAQGTPEE 226
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
 20-244 2.93e-41

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: 151.76  E-value: 2.93e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  20 PAIEVSGLSKHFGT----VCAVSDVDLTVAEGEFLSILGPSGSGKS----TLLGLVAGLIQPTGGRIVIGSRDVTHVPPA 91
Cdd:COG4172    5 PLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSER 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  92 Q------RDIGLVFQ--SYALFPNMTVAGNIAFSLAV-RGISRRDAKERVEWAIELVRLNGLEHR---KPSQLSGGQQQR 159
Cdd:COG4172   85 ElrrirgNRIAMIFQepMTSLNPLHTIGKQIAEVLRLhRGLSGAAARARALELLERVGIPDPERRldaYPHQLSGGQRQR 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 160 VAIARALVFGPKLLLLDEPLAALDRKLREEVrLEL-RRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGE 238
Cdd:COG4172  165 VMIAMALANEPDLLIADEPTTALDVTVQAQI-LDLlKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAE 243


                 ....*.
gi 914601027 239 LYRQPA 244
Cdd:COG4172  244 LFAAPQ 249
CeuD COG4604
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ...
 22-239 3.55e-41

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


Pssm-ID: 443654 [Multi-domain]  Cd Length: 252  Bit Score: 145.23  E-value: 3.55e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  22 IEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQ--RDIGLVF 99
Cdd:COG4604    2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRElaKRLAILR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 100 QSYALFPNMTVAGNIAF-----SlavRG-ISRRDaKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLL 173
Cdd:COG4604   82 QENHINSRLTVRELVAFgrfpyS---KGrLTAED-REIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYV 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 914601027 174 LLDEPLAALDRKL-REEVRLeLRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGEL 239
Cdd:COG4604  158 LLDEPLNNLDMKHsVQMMKL-LRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI 223
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
 19-255 4.74e-41

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


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 145.13  E-value: 4.74e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  19 RPAIEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQ-RDIGL 97
Cdd:PRK11300   3 QPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQiARMGV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  98 V--FQSYALFPNMTVAGN-------------IAFSLAVRGISR--RDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRV 160
Cdd:PRK11300  83 VrtFQHVRLFREMTVIENllvaqhqqlktglFSGLLKTPAFRRaeSEALDRAATWLERVGLLEHANRQAGNLAYGQQRRL 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 161 AIARALVFGPKLLLLDEPLAALDRKLREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELY 240
Cdd:PRK11300 163 EIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIR 242

                        250
                 ....*....|....*
gi 914601027 241 RQPanRFVAGFLGAA 255
Cdd:PRK11300 243 NNP--DVIKAYLGEA 255
nickel_nikE TIGR02769
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ...
 22-246 1.01e-39

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: 141.87  E-value: 1.01e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   22 IEVSGLSKHFGT---------VCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQ 92
Cdd:TIGR02769   3 LEVRDVTHTYRTgglfgakqrAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   93 -----RDIGLVFQ-SYALF-PNMTVAGNIAFSLavRGISRRDAKERVEWAIELVRLNGLE----HRKPSQLSGGQQQRVA 161
Cdd:TIGR02769  83 rrafrRDVQLVFQdSPSAVnPRMTVRQIIGEPL--RHLTSLDESEQKARIAELLDMVGLRsedaDKLPRQLSGGQLQRIN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  162 IARALVFGPKLLLLDEPLAALDRKLREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGEL-- 239
Cdd:TIGR02769 161 IARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLls 240


                  ....*..
gi 914601027  240 YRQPANR 246
Cdd:TIGR02769 241 FKHPAGR 247
SapF COG4167
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
20-243 1.30e-39

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


Pssm-ID: 443328 [Multi-domain]  Cd Length: 265  Bit Score: 141.51  E-value: 1.30e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  20 PAIEVSGLSKHF---------GTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPP 90
Cdd:COG4167    3 ALLEVRNLSKTFkyrtglfrrQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDY 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  91 AQR--DIGLVFQ--SYALFPNMTVaGNIaFSLAVRGISRRDAKERVEWAIELVRLNGL--EHR--KPSQLSGGQQQRVAI 162
Cdd:COG4167   83 KYRckHIRMIFQdpNTSLNPRLNI-GQI-LEEPLRLNTDLTAEEREERIFATLRLVGLlpEHAnfYPHMLSSGQKQRVAL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 163 ARALVFGPKLLLLDEPLAALDRKLREE-VRLELrRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELYR 241
Cdd:COG4167  161 ARALILQPKIIIADEALAALDMSVRSQiINLML-ELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVFA 239


                 ..
gi 914601027 242 QP 243
Cdd:COG4167  240 NP 241
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
 18-239 1.37e-39

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 141.67  E-value: 1.37e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  18 RRPAIEVSGLSKHFGTV--CAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVT--HVPPAQR 93
Cdd:PRK13632   4 KSVMIKVENVSFSYPNSenNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISkeNLKEIRK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  94 DIGLVFQSY-ALFPNMTVAGNIAFSLAVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKL 172
Cdd:PRK13632  84 KIGIIFQNPdNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEI 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 914601027 173 LLLDEPLAALDRKLREEVRLELRRLQGTLGVTTVLVTHDQDEAMsMSDRIAVLAQGVIQQLGSPGEL 239
Cdd:PRK13632 164 IIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEI 229
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
22-255 2.36e-39

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 140.87  E-value: 2.36e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  22 IEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVppaqRD------- 94
Cdd:PRK10619   6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLV----RDkdgqlkv 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  95 ------------IGLVFQSYALFPNMTVAGNIAFS-LAVRGISRRDAKERVEWAIELVRLNGLEHRK-PSQLSGGQQQRV 160
Cdd:PRK10619  82 adknqlrllrtrLTMVFQHFNLWSHMTVLENVMEApIQVLGLSKQEARERAVKYLAKVGIDERAQGKyPVHLSGGQQQRV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 161 AIARALVFGPKLLLLDEPLAALDRKLREEVrleLRRLQ--GTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGE 238
Cdd:PRK10619 162 SIARALAMEPEVLLFDEPTSALDPELVGEV---LRIMQqlAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQ 238

                        250
                 ....*....|....*..
gi 914601027 239 LYRQPANRFVAGFLGAA 255
Cdd:PRK10619 239 LFGNPQSPRLQQFLKGS 255
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
36-242 3.91e-39

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 140.61  E-value: 3.91e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  36 AVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVI---GSRDVTHVPPAQRDIGLVFQSyalfP-NMTVA 111
Cdd:PRK13633  25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVdglDTSDEENLWDIRNKAGMVFQN----PdNQIVA 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 112 G----NIAFSLAVRGISRRDAKERVEWAIElvRLNGLEHRK--PSQLSGGQQQRVAIARALVFGPKLLLLDEPLAALDRK 185
Cdd:PRK13633 101 TiveeDVAFGPENLGIPPEEIRERVDESLK--KVGMYEYRRhaPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPS 178

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 914601027 186 LREEVRLELRRLQGTLGVTTVLVTHDQDEAMSmSDRIAVLAQGVIQQLGSPGELYRQ 242
Cdd:PRK13633 179 GRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKE 234
urea_trans_UrtE TIGR03410
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ...
 23-249 6.69e-39

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: 138.43  E-value: 6.69e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   23 EVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQR---DIGLVF 99
Cdd:TIGR03410   2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaraGIAYVP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  100 QSYALFPNMTVAGNIAFSLAVRGisrRDAKERVEWAIELVR-LNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEP 178
Cdd:TIGR03410  82 QGREIFPRLTVEENLLTGLAALP---RRSRKIPDEIYELFPvLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEP 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 914601027  179 LAALDRKLREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELYRQPANRFVA 249
Cdd:TIGR03410 159 TEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDELDEDKVRRYLA 229
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
 15-243 1.36e-38

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 140.61  E-value: 1.36e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  15 PVSRRPAIEVSGLSKHFG-------------TVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIG 81
Cdd:PRK15079   2 TEGKKVLLEVADLKVHFDikdgkqwfwqppkTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  82 SRDVTHVPPAQR-----DIGLVFQS--YALFPNMTVAGNIAFSLAVR--GISRRDAKERVEWAIELVRL-NGLEHRKPSQ 151
Cdd:PRK15079  82 GKDLLGMKDDEWravrsDIQMIFQDplASLNPRMTIGEIIAEPLRTYhpKLSRQEVKDRVKAMMLKVGLlPNLINRYPHE 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 152 LSGGQQQRVAIARALVFGPKLLLLDEPLAALDRKLREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQ 231
Cdd:PRK15079 162 FSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAV 241

                        250
                 ....*....|..
gi 914601027 232 QLGSPGELYRQP 243
Cdd:PRK15079 242 ELGTYDEVYHNP 253
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
 21-253 3.57e-37

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 134.97  E-value: 3.57e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  21 AIEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQ-----PTGGRIVIGSRDV--THVPP--A 91
Cdd:PRK14267   4 AIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIysPDVDPieV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  92 QRDIGLVFQSYALFPNMTVAGNIAFSLAVRGI--SRRDAKERVEWAIELVRL-NGLEHR---KPSQLSGGQQQRVAIARA 165
Cdd:PRK14267  84 RREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALwDEVKDRlndYPSNLSGGQRQRLVIARA 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 166 LVFGPKLLLLDEPLAALD----RKLrEEVRLELRRlqgtlGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELYR 241
Cdd:PRK14267 164 LAMKPKILLMDEPTANIDpvgtAKI-EELLFELKK-----EYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFE 237

                        250
                 ....*....|....*.
gi 914601027 242 QPAN----RFVAGFLG 253
Cdd:PRK14267 238 NPEHelteKYVTGALG 253
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
 20-225 7.46e-37

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: 139.73  E-value: 7.46e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   20 PAIEVSGLSKHF-GTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPA--QRDIG 96
Cdd:TIGR02857 320 SSLEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADswRDQIA 399

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   97 LVFQSYALFPNmTVAGNIAFslavrgiSRRDAKE-RVEWAIELVRLNGLEHRKP-----------SQLSGGQQQRVAIAR 164
Cdd:TIGR02857 400 WVPQHPFLFAG-TIAENIRL-------ARPDASDaEIREALERAGLDEFVAALPqgldtpigeggAGLSGGQAQRLALAR 471

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 914601027  165 ALVFGPKLLLLDEPLAALDRKLREEVRLELRRLQGtlGVTTVLVTHDqDEAMSMSDRIAVL 225
Cdd:TIGR02857 472 AFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHR-LALAALADRIVVL 529
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
22-246 1.19e-36

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 133.66  E-value: 1.19e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  22 IEVSGLSKHFGTVCAV---------SDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQ 92
Cdd:PRK10419   4 LNVSGLSHHYAHGGLSgkhqhqtvlNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQ 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  93 -----RDIGLVFQSY--ALFPNMTVAGNIAFSLavRGISRRDAKERVEWAIELVRLNGL--EH--RKPSQLSGGQQQRVA 161
Cdd:PRK10419  84 rkafrRDIQMVFQDSisAVNPRKTVREIIREPL--RHLLSLDKAERLARASEMLRAVDLddSVldKRPPQLSGGQLQRVC 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 162 IARALVFGPKLLLLDEPLAALDRKLREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGEL-- 239
Cdd:PRK10419 162 LARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDKlt 241


                 ....*..
gi 914601027 240 YRQPANR 246
Cdd:PRK10419 242 FSSPAGR 248
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
 19-252 1.36e-36

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 133.11  E-value: 1.36e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  19 RPAIEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQ-----PTGGRIVIGSRDVTHVPPAQ- 92
Cdd:PRK14247   1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIEl 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  93 -RDIGLVFQSYALFPNMTVAGNIAFSLAVRGI--SRRDAKERVEWAIELVRL-NGLEHR---KPSQLSGGQQQRVAIARA 165
Cdd:PRK14247  81 rRRVQMVFQIPNPIPNLSIFENVALGLKLNRLvkSKKELQERVRWALEKAQLwDEVKDRldaPAGKLSGGQQQRLCIARA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 166 LVFGPKLLLLDEPLAALD----RKLrEEVRLELRRlqgtlGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELYR 241
Cdd:PRK14247 161 LAFQPEVLLADEPTANLDpentAKI-ESLFLELKK-----DMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFT 234

                        250
                 ....*....|....*
gi 914601027 242 QP----ANRFVAGFL 252
Cdd:PRK14247 235 NPrhelTEKYVTGRL 249
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
17-232 1.37e-36

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 132.63  E-value: 1.37e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  17 SRRPAIEVSGLSKHF--GTVCA--VSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPA- 91
Cdd:PRK11629   1 MNKILLQCDNLCKRYqeGSVQTdvLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAa 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  92 -----QRDIGLVFQSYALFPNMTVAGNIAFSLAVRGISRRDAKERvewAIELVRLNGLEHR---KPSQLSGGQQQRVAIA 163
Cdd:PRK11629  81 kaelrNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSR---ALEMLAAVGLEHRanhRPSELSGGERQRVAIA 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 914601027 164 RALVFGPKLLLLDEPLAALDRKLRE---EVRLELRRLQGTlgvTTVLVTHDQDEAMSMSdRIAVLAQGVIQQ 232
Cdd:PRK11629 158 RALVNNPRLVLADEPTGNLDARNADsifQLLGELNRLQGT---AFLVVTHDLQLAKRMS-RQLEMRDGRLTA 225
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
 20-239 2.00e-36

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: 132.52  E-value: 2.00e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  20 PAIEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPT-GGRIVI-----GSRDVTHVppaQR 93
Cdd:COG1119    2 PLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTyGNDVRLfgerrGGEDVWEL---RK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  94 DIGLVfqSYAL---FPNMTVAGNIAFS--LAVRGISRR---DAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARA 165
Cdd:COG1119   79 RIGLV--SPALqlrFPRDETVLDVVLSgfFDSIGLYREptdEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARA 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 914601027 166 LVFGPKLLLLDEPLAALDRKLREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGEL 239
Cdd:COG1119  157 LVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEV 230
cbiO PRK13643
energy-coupling factor transporter ATPase;
36-242 3.33e-36

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 133.32  E-value: 3.33e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  36 AVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVT------HVPPAQRDIGLVFQsyalFPNM- 108
Cdd:PRK13643  21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSstskqkEIKPVRKKVGVVFQ----FPESq 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 109 ----TVAGNIAFSLAVRGISRRDAKERVEWAIELVRLNG-LEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAALD 183
Cdd:PRK13643  97 lfeeTVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADeFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLD 176

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 914601027 184 RKLREEVRLELRRLQGTlGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELYRQ 242
Cdd:PRK13643 177 PKARIEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQE 234
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
 22-215 3.66e-36

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 131.44  E-value: 3.66e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  22 IEVSGLSKHFG----TVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQR---- 93
Cdd:PRK10584   7 VEVHHLKKSVGqgehELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARaklr 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  94 --DIGLVFQSYALFPNMTVAGNIAFSLAVRGISRRDAKERvewAIELVRLNGLEHR---KPSQLSGGQQQRVAIARALVF 168
Cdd:PRK10584  87 akHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNG---AKALLEQLGLGKRldhLPAQLSGGEQQRVALARAFNG 163

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 914601027 169 GPKLLLLDEPLAALDRKLREEVRLELRRLQGTLGVTTVLVTHDQDEA 215
Cdd:PRK10584 164 RPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLA 210
cbiO PRK13649
energy-coupling factor transporter ATPase;
36-242 6.74e-36

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 132.18  E-value: 6.74e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  36 AVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTH------VPPAQRDIGLVFQsyalFPNM- 108
Cdd:PRK13649  22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITStsknkdIKQIRKKVGLVFQ----FPESq 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 109 ----TVAGNIAFSLAVRGISRRDAKERVEWAIELVRLN-GLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAALD 183
Cdd:PRK13649  98 lfeeTVLKDVAFGPQNFGVSQEEAEALAREKLALVGISeSLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 914601027 184 RKLREEVRLELRRLQgTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELYRQ 242
Cdd:PRK13649 178 PKGRKELMTLFKKLH-QSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
36-228 1.47e-35

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 129.61  E-value: 1.47e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  36 AVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVT-----HVPPAQRDIGLVFQSYALFPNMTV 110
Cdd:PRK10908  17 ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITrlknrEVPFLRRQIGMIFQDHHLLMDRTV 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 111 AGNIAFSLAVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAALDRKLREEV 190
Cdd:PRK10908  97 YDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGI 176

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 914601027 191 rLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQG 228
Cdd:PRK10908 177 -LRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDG 213
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
 19-228 1.92e-35

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: 127.93  E-value: 1.92e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  19 RPAIEVSGLSKHFgtvcAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQR-DIGL 97
Cdd:cd03215    2 EPVLEVRGLSVKG----AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAiRAGI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  98 VF-----QSYALFPNMTVAGNIAFslavrgisrrdakervewaielvrlnglehrkPSQLSGGQQQRVAIARALVFGPKL 172
Cdd:cd03215   78 AYvpedrKREGLVLDLSVAENIAL--------------------------------SSLLSGGNQQKVVLARWLARDPRV 125

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 914601027 173 LLLDEPLAALDRKLREEVRLELRRLQGTlGVTTVLVTHDQDEAMSMSDRIAVLAQG 228
Cdd:cd03215  126 LILDEPTRGVDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEG 180
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
 39-230 2.03e-35

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: 128.53  E-value: 2.03e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  39 DVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVtHVPPAQRDIGLVFQS--YALFPNmTVAGNIAF 116
Cdd:cd03226   18 DLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI-KAKERRKSIGYVMQDvdYQLFTD-SVREELLL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 117 SLavRGISrrDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAALDRKLREEVRLELRR 196
Cdd:cd03226   96 GL--KELD--AGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRE 171

                        170       180       190
                 ....*....|....*....|....*....|....
gi 914601027 197 LQGTlGVTTVLVTHDQDEAMSMSDRIAVLAQGVI 230
Cdd:cd03226  172 LAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAI 204
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
 36-240 2.46e-35

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 130.26  E-value: 2.46e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  36 AVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIV-----IGSRDVTHVppaQRDIGLVFQS-YALFPNMT 109
Cdd:PRK13648  24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFynnqaITDDNFEKL---RKHIGIVFQNpDNQFVGSI 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 110 VAGNIAFSLAVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAALDRKLREE 189
Cdd:PRK13648 101 VKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQN 180

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 914601027 190 VRLELRRLQGTLGVTTVLVTHDQDEAMSmSDRIAVLAQGVIQQLGSPGELY 240
Cdd:PRK13648 181 LLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIF 230
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
22-228 3.94e-35

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 129.75  E-value: 3.94e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  22 IEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLI---QPTGGRIVIGSRDVTHVPPAQRDI--- 95
Cdd:PRK09984   5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVQREGRLARDIrks 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  96 ----GLVFQSYALFPNMTVAGNIA---------FSLAVRGISRRDaKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAI 162
Cdd:PRK09984  85 rantGYIFQQFNLVNRLSVLENVLigalgstpfWRTCFSWFTREQ-KQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAI 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 914601027 163 ARALVFGPKLLLLDEPLAALDRKLREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQG 228
Cdd:PRK09984 164 ARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQG 229
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
 20-228 7.36e-35

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: 127.94  E-value: 7.36e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  20 PAIEVSGLSKHF------GTVC-AVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSR----DVTHV 88
Cdd:COG4778    3 TLLEVENLSKTFtlhlqgGKRLpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAQA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  89 PPAQ------RDIGLVFQSYALFPNMTVAGNIAFSLAVRGISRRDAKERV-EWaieLVRLN---GLEHRKPSQLSGGQQQ 158
Cdd:COG4778   83 SPREilalrrRTIGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARArEL---LARLNlpeRLWDLPPATFSGGEQQ 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 159 RVAIARALVFGPKLLLLDEPLAALDRKLREEVRLELRRLQGTlGVTTVLVTHDQDEAMSMSDRIAVLAQG 228
Cdd:COG4778  160 RVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRVVDVTPF 228
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
22-252 7.66e-35

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 129.11  E-value: 7.66e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  22 IEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDV-----THVPPAQRDIG 96
Cdd:PRK11831   8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamsrSRLYTVRKRMS 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  97 LVFQSYALFPNMTVAGNIAFSLavRGISRRDA---KERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLL 173
Cdd:PRK11831  88 MLFQSGALFTDMNVFDNVAYPL--REHTQLPApllHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLI 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 174 LLDEPLAALDR-------KLREEvrlelrrLQGTLGVTTVLVTHDQDEAMSMSDRIAVLA-QGVIQQlGSPGELYRQPAN 245
Cdd:PRK11831 166 MFDEPFVGQDPitmgvlvKLISE-------LNSALGVTCVVVSHDVPEVLSIADHAYIVAdKKIVAH-GSAQALQANPDP 237


                 ....*..
gi 914601027 246 RfVAGFL 252
Cdd:PRK11831 238 R-VRQFL 243
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
 36-230 7.84e-35

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: 127.71  E-value: 7.84e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  36 AVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPA--QRDIGLVFQSYALFpNMTVAGN 113
Cdd:cd03245   19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPAdlRRNIGYVPQDVTLF-YGTLRDN 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 114 IAFslavrgiSRRDAK-ERVEWAIELVRLNGLEHRKP-----------SQLSGGQQQRVAIARALVFGPKLLLLDEPLAA 181
Cdd:cd03245   98 ITL-------GAPLADdERILRAAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVALARALLNDPPILLLDEPTSA 170

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 914601027 182 LDRKLREEVRLELRRLQGtlGVTTVLVTHDQdEAMSMSDRIAVLAQGVI 230
Cdd:cd03245  171 MDMNSEERLKERLRQLLG--DKTLIIITHRP-SLLDLVDRIIVMDSGRI 216
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
31-225 1.34e-34

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 126.19  E-value: 1.34e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  31 FGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGsrdvthvppAQRDIGLVFQSYAL---FPn 107
Cdd:NF040873   2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRA---------GGARVAYVPQRSEVpdsLP- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 108 MTVAGNIAFSL-AVRGISRR---DAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAALD 183
Cdd:NF040873  72 LTVRDLVAMGRwARRGLWRRltrDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 914601027 184 RKLREEVRLELRRLQGTlGVTTVLVTHDQDEAMSmSDRIAVL 225
Cdd:NF040873 152 AESRERIIALLAEEHAR-GATVVVVTHDLELVRR-ADPCVLL 191
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
 39-242 1.56e-34

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: 127.27  E-value: 1.56e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  39 DVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQ--RDIGLVFQSYALFpNMTVAGNIAF 116
Cdd:cd03249   21 GLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWlrSQIGLVSQEPVLF-DGTIAENIRY 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 117 SlavrgisRRDAK-ERVEWAIELVRL--------NGLEHR---KPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAALDR 184
Cdd:cd03249  100 G-------KPDATdEEVEEAAKKANIhdfimslpDGYDTLvgeRGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDA 172

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 914601027 185 KLREEVRLELRRLqgTLGVTTVLVTHdQDEAMSMSDRIAVLAQGVIQQLGSPGELYRQ 242
Cdd:cd03249  173 ESEKLVQEALDRA--MKGRTTIVIAH-RLSTIRNADLIAVLQNGQVVEQGTHDELMAQ 227
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
22-264 1.77e-34

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 134.47  E-value: 1.77e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  22 IEVSGLSKHF----GTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQ----- 92
Cdd:PRK10535   5 LELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADAlaqlr 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  93 -RDIGLVFQSYALFPNMTVAGNIAFSLAVRGISRrdaKERVEWAIELVRLNGLEHR---KPSQLSGGQQQRVAIARALVF 168
Cdd:PRK10535  85 rEHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLER---KQRLLRAQELLQRLGLEDRveyQPSQLSGGQQQRVSIARALMN 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 169 GPKLLLLDEPLAALDRKLREEVRLELRRLQGTlGVTTVLVTHDQDEAmSMSDRIAVLAQGVIqqLGSPGELYRQPANRFV 248
Cdd:PRK10535 162 GGQVILADEPTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHDPQVA-AQAERVIEIRDGEI--VRNPPAQEKVNVAGGT 237

                        250
                 ....*....|....*.
gi 914601027 249 AGFLGAANLFHGIIAR 264
Cdd:PRK10535 238 EPVVNTASGWRQFVSG 253
cbiO PRK13646
energy-coupling factor transporter ATPase;
36-242 2.51e-34

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 127.97  E-value: 2.51e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  36 AVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTH------VPPAQRDIGLVFQ--SYALFPN 107
Cdd:PRK13646  22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHktkdkyIRPVRKRIGMVFQfpESQLFED 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 108 mTVAGNIAFSLAVRGISRRDAKERvewAIELVRLNGLEH----RKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAALD 183
Cdd:PRK13646 102 -TVEREIIFGPKNFKMNLDEVKNY---AHRLLMDLGFSRdvmsQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLD 177

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 914601027 184 RKLREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELYRQ 242
Cdd:PRK13646 178 PQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKD 236
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
 22-231 4.65e-34

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: 125.91  E-value: 4.65e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  22 IEVSGLSKHFGT---------------------VCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVI 80
Cdd:cd03267    1 IEVSNLSKSYRVyskepgligslkslfkrkyreVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  81 GSRdvthVPPAQRD-----IGLVF-QSYALFPNMTVAGNIAFSLAVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSG 154
Cdd:cd03267   81 AGL----VPWKRRKkflrrIGVVFgQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSL 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 914601027 155 GQQQRVAIARALVFGPKLLLLDEPLAALDRKLREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQ 231
Cdd:cd03267  157 GQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
 32-243 6.02e-34

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 126.73  E-value: 6.02e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  32 GTVcAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTH----VPPAQRDIGLVFQSY--ALF 105
Cdd:PRK13639  14 GTE-ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYdkksLLEVRKTVGIVFQNPddQLF 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 106 PNmTVAGNIAFSLAVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAALDRK 185
Cdd:PRK13639  93 AP-TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPM 171

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 914601027 186 LREEVRLELRRLQGTlGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELYRQP 243
Cdd:PRK13639 172 GASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDI 228
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 21-280 7.75e-34

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


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 127.51  E-value: 7.75e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  21 AIEVSGLSKHF-------G--------------TVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIV 79
Cdd:COG4586    1 IIEVENLSKTYrvyekepGlkgalkglfrreyrEVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  80 IGSrdvtHVPPAQR-----DIGLVF-QSYALFPNMTVAGNiaFSL--AVRGISRRDAKERVEWAIELVRLNGLEHRKPSQ 151
Cdd:COG4586   81 VLG----YVPFKRRkefarRIGVVFgQRSQLWWDLPAIDS--FRLlkAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQ 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 152 LSGGQQQRVAIARALVFGPKLLLLDEPLAALDRKLREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQ 231
Cdd:COG4586  155 LSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRII 234

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 914601027 232 QLGSPGELYRQ-PANRFV----AGFLGAANLFHG--IIAREGNGAVLALDGGTRLP 280
Cdd:COG4586  235 YDGSLEELKERfGPYKTIvlelAEPVPPLELPRGgeVIEREGNRVRLEVDPRESLA 290
type_I_sec_LssB TIGR03375
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ...
 36-237 8.88e-34

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: 132.30  E-value: 8.88e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   36 AVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPA--QRDIGLVFQSYALFpNMTVAGN 113
Cdd:TIGR03375 480 ALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPAdlRRNIGYVPQDPRLF-YGTLRDN 558

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  114 IAfsLAVRGISRRDAKERVEWA--IELVRL--NGLEHR---KPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAALDRkl 186
Cdd:TIGR03375 559 IA--LGAPYADDEEILRAAELAgvTEFVRRhpDGLDMQigeRGRSLSGGQRQAVALARALLRDPPILLLDEPTSAMDN-- 634

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 914601027  187 REEVRLeLRRLQGTL-GVTTVLVTHDQdEAMSMSDRIAVLAQG----------VIQQLGSPG 237
Cdd:TIGR03375 635 RSEERF-KDRLKRWLaGKTLVLVTHRT-SLLDLVDRIIVMDNGrivadgpkdqVLEALRKGR 694
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
 16-242 1.20e-33

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 125.42  E-value: 1.20e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  16 VSRRPAIEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSR-----DVTHVPP 90
Cdd:PRK11701   1 MMDQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLYALSE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  91 AQR------DIGLVFQSYA--LFPNMTVAGNIAFSLAVRGIS-----RRDAK---ERVEwaIELVRLNGLehrkPSQLSG 154
Cdd:PRK11701  81 AERrrllrtEWGFVHQHPRdgLRMQVSAGGNIGERLMAVGARhygdiRATAGdwlERVE--IDAARIDDL----PTTFSG 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 155 GQQQRVAIARALVFGPKLLLLDEPLAALDRKLREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQG-VIQQ- 232
Cdd:PRK11701 155 GMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGrVVESg 234

                        250
                 ....*....|....*
gi 914601027 233 -----LGSPGELYRQ 242
Cdd:PRK11701 235 ltdqvLDDPQHPYTQ 249
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
4-239 1.29e-33

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 127.64  E-value: 1.29e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   4 HQLTSERDTLAPVSRRP-AIEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRI-VIG 81
Cdd:PRK13536  23 HQGISEAKASIPGSMSTvAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKItVLG 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  82 SRDVTHVPPAQRDIGLVFQSYALFPNMTVAGNIAFSLAVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVA 161
Cdd:PRK13536 103 VPVPARARLARARIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLT 182

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 914601027 162 IARALVFGPKLLLLDEPLAALDRKLREEVRLELRRLQgTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGEL 239
Cdd:PRK13536 183 LARALINDPQLLILDEPTTGLDPHARHLIWERLRSLL-ARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHAL 259
cbiO PRK13642
energy-coupling factor transporter ATPase;
34-240 1.54e-33

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 125.98  E-value: 1.54e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  34 VCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVT--HVPPAQRDIGLVFQSY-ALFPNMTV 110
Cdd:PRK13642  20 VNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTaeNVWNLRRKIGMVFQNPdNQFVGATV 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 111 AGNIAFSLAVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAALDRKLREEV 190
Cdd:PRK13642 100 EDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEI 179

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 914601027 191 RLELRRLQGTLGVTTVLVTHDQDEAMSmSDRIAVLAQGVIQQLGSPGELY 240
Cdd:PRK13642 180 MRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
 37-230 2.15e-33

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: 122.32  E-value: 2.15e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  37 VSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQ--RDIGLVFQSYALFPNmTVAGNI 114
Cdd:cd03246   18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNElgDHVGYLPQDDELFSG-SIAENI 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 115 afslavrgisrrdakervewaielvrlnglehrkpsqLSGGQQQRVAIARALVFGPKLLLLDEPLAALDRKLREEVRLEL 194
Cdd:cd03246   97 -------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAI 139

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 914601027 195 RRLQGTlGVTTVLVTHdQDEAMSMSDRIAVLAQGVI 230
Cdd:cd03246  140 AALKAA-GATRIVIAH-RPETLASADRILVLEDGRV 173
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
 22-234 2.79e-33

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: 123.41  E-value: 2.79e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  22 IEVSGLSKHF----------------------GTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIV 79
Cdd:cd03220    1 IELENVSKSYptykggssslkklgilgrkgevGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  80 IGSRDVTHVppaqrDIGLVFQsyalfPNMTVAGNIAFSLAVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQR 159
Cdd:cd03220   81 VRGRVSSLL-----GLGGGFN-----PELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKAR 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 914601027 160 VAIARALVFGPKLLLLDEPLAALDRKLREEVrleLRRLQGTL--GVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLG 234
Cdd:cd03220  151 LAFAIATALEPDILLIDEVLAVGDAAFQEKC---QRRLRELLkqGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
 20-242 3.03e-33

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: 129.54  E-value: 3.03e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   20 PAIEVSGLSKHF-----GTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGR--IVIGSR--DVTHVPP 90
Cdd:TIGR03269 278 PIIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnVRVGDEwvDMTKPGP 357

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   91 -----AQRDIGLVFQSYALFPNMTVAGNIAFSLavrGISRRDAKERVEwAIELVRLNGLEHRK--------PSQLSGGQQ 157
Cdd:TIGR03269 358 dgrgrAKRYIGILHQEYDLYPHRTVLDNLTEAI---GLELPDELARMK-AVITLKMVGFDEEKaeeildkyPDELSEGER 433

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  158 QRVAIARALVFGPKLLLLDEPLAALDRKLREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPG 237
Cdd:TIGR03269 434 HRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPE 513


                  ....*
gi 914601027  238 ELYRQ 242
Cdd:TIGR03269 514 EIVEE 518
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
 21-236 3.19e-33

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 124.85  E-value: 3.19e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  21 AIEVSGLSKHF--GTVcAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVThvPPAQRDI--- 95
Cdd:PRK13647   4 IIEVEDLHFRYkdGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVN--AENEKWVrsk 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  96 -GLVFQSY--ALFpNMTVAGNIAFSLAVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKL 172
Cdd:PRK13647  81 vGLVFQDPddQVF-SSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDV 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 914601027 173 LLLDEPLAALDRKLREEVRLELRRLQGTlGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSP 236
Cdd:PRK13647 160 IVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDK 222
cbiO PRK13640
energy-coupling factor transporter ATPase;
36-243 3.45e-33

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 124.91  E-value: 3.45e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  36 AVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQP---TGGRIVIGSRDVTH--VPPAQRDIGLVFQSY-ALFPNMT 109
Cdd:PRK13640  22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAktVWDIREKVGIVFQNPdNQFVGAT 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 110 VAGNIAFSLAVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAALDRKLREE 189
Cdd:PRK13640 102 VGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQ 181

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 914601027 190 VRLELRRLQGTLGVTTVLVTHDQDEAmSMSDRIAVLAQGVIQQLGSPGELYRQP 243
Cdd:PRK13640 182 ILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKV 234
cbiO PRK13645
energy-coupling factor transporter ATPase;
36-240 8.15e-33

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 124.35  E-value: 8.15e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  36 AVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGS-------RDVTHVPPAQRDIGLVFQ--SYALFP 106
Cdd:PRK13645  26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipanlKKIKEVKRLRKEIGLVFQfpEYQLFQ 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 107 NmTVAGNIAFSLAVRGISRRDAKERVEWAIELVRL-NGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAALDRK 185
Cdd:PRK13645 106 E-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPK 184

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 914601027 186 LREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELY 240
Cdd:PRK13645 185 GEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIF 239
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
 1-230 9.19e-33

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 128.22  E-value: 9.19e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   1 MISHQLTSERDTLAPVSRRPAIEVSGLS-KHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIV 79
Cdd:COG3845  237 MVGREVLLRVEKAPAEPGEVVLEVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIR 316

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  80 IGSRDVTHVPPAQ-RDIGLVF-----QSYALFPNMTVAGNIAFSLAVR-GISRR---DAKERVEWAIEL-----VRLNGL 144
Cdd:COG3845  317 LDGEDITGLSPRErRRLGVAYipedrLGRGLVPDMSVAENLILGRYRRpPFSRGgflDRKAIRAFAEELieefdVRTPGP 396

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 145 EHRkPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAALDRKLREEVR---LELRRlqgtLGVTTVLVTHDQDEAMSMSDR 221
Cdd:COG3845  397 DTP-ARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHqrlLELRD----AGAAVLLISEDLDEILALSDR 471


                 ....*....
gi 914601027 222 IAVLAQGVI 230
Cdd:COG3845  472 IAVMYEGRI 480
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
 37-252 1.22e-32

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 122.85  E-value: 1.22e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  37 VSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQ------PTGGRIVIGSRDVTHVPPAQ--RDIGLVFQSYALFPNM 108
Cdd:PRK14246  26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIKlrKEVGMVFQQPNPFPHL 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 109 TVAGNIAFSLAVRGIS-RRDAKERVEWAIELVRLNGLEHRK----PSQLSGGQQQRVAIARALVFGPKLLLLDEPLAALD 183
Cdd:PRK14246 106 SIYDNIAYPLKSHGIKeKREIKKIVEECLRKVGLWKEVYDRlnspASQLSGGQQQRLTIARALALKPKVLLMDEPTSMID 185

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 914601027 184 RKLREEVRLELRRLQGTlgVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELYRQPANRFVAGFL 252
Cdd:PRK14246 186 IVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYV 252
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
 18-228 1.62e-32

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 121.74  E-value: 1.62e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  18 RRPAIEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQ--RDI 95
Cdd:PRK10247   4 NSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIyrQQV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  96 GLVFQSYALFPNmTVAGNIAFSLAVRGisrrDAKERVEWAIELVRLNGLEH--RKP-SQLSGGQQQRVAIARALVFGPKL 172
Cdd:PRK10247  84 SYCAQTPTLFGD-TVYDNLIFPWQIRN----QQPDPAIFLDDLERFALPDTilTKNiAELSGGEKQRISLIRNLQFMPKV 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 914601027 173 LLLDEPLAALDRKLREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQG 228
Cdd:PRK10247 159 LLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITLQPHA 214
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
 22-230 1.86e-32

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 123.66  E-value: 1.86e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  22 IEVSGLSKHFGT-----VCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRI------------------ 78
Cdd:PRK13651   3 IKVKNIVKIFNKklpteLKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekek 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  79 -----VIG---SRDVTHVPPAQRDIGLVFQ--SYALFPNmTVAGNIAFSLAVRGISRRDAKERVEWAIELVRL--NGLEh 146
Cdd:PRK13651  83 vleklVIQktrFKKIKKIKEIRRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdeSYLQ- 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 147 RKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAALDRKLREEVRLELRRLQGTlGVTTVLVTHDQDEAMSMSDRIAVLA 226
Cdd:PRK13651 161 RSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFK 239


                 ....
gi 914601027 227 QGVI 230
Cdd:PRK13651 240 DGKI 243
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
 15-287 3.89e-32

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 123.15  E-value: 3.89e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  15 PVSRrpaievsGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQ-- 92
Cdd:PRK11308  16 PVKR-------GLFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAqk 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  93 ---RDIGLVFQS-YA-LFPNMTVAGNIAFSLAVRgiSRRDAKERVEWAIELVRLNGL--EH--RKPSQLSGGQQQRVAIA 163
Cdd:PRK11308  89 llrQKIQIVFQNpYGsLNPRKKVGQILEEPLLIN--TSLSAAERREKALAMMAKVGLrpEHydRYPHMFSGGQRQRIAIA 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 164 RALVFGPKLLLLDEPLAALDRKLREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELYRQP 243
Cdd:PRK11308 167 RALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNP 246

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 914601027 244 ANRFVAGFLGAANLFHGIIAREgngavlaldggtRLPLAGDYPS 287
Cdd:PRK11308 247 RHPYTQALLSATPRLNPDDRRE------------RIKLTGELPS 278
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
1-230 4.72e-32

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 125.90  E-value: 4.72e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   1 MISHQLTSERDTLAPVSRRPAIEVSGLSKHFGtvcaVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVI 80
Cdd:COG1129  236 MVGRELEDLFPKRAAAPGEVVLEVEGLSVGGV----VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRL 311

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  81 GSRDVTHVPPAQR-DIGLVF-----QSYALFPNMTVAGNIAFS----LAVRG-ISRRDAKERVEWAIEL--VRLNGLEhR 147
Cdd:COG1129  312 DGKPVRIRSPRDAiRAGIAYvpedrKGEGLVLDLSIRENITLAsldrLSRGGlLDRRRERALAEEYIKRlrIKTPSPE-Q 390

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 148 KPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAALDRKLREEV-RLeLRRL--QgtlGVTTVLVTHDQDEAMSMSDRIAV 224
Cdd:COG1129  391 PVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIyRL-IRELaaE---GKAVIVISSELPELLGLSDRILV 466


                 ....*.
gi 914601027 225 LAQGVI 230
Cdd:COG1129  467 MREGRI 472
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
 22-243 5.66e-32

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 121.45  E-value: 5.66e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  22 IEVSGLSKHF-GTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVT--HVPPAQRDIGLV 98
Cdd:PRK13652   4 IETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITkeNIREVRKFVGLV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  99 FQSY--ALFpNMTVAGNIAFSLAVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLD 176
Cdd:PRK13652  84 FQNPddQIF-SPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLD 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 914601027 177 EPLAALDRKLREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELYRQP 243
Cdd:PRK13652 163 EPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
 36-242 5.87e-32

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: 120.41  E-value: 5.87e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  36 AVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQ--RDIGLVFQSYALFpNMTVAGN 113
Cdd:cd03251   17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASlrRQIGLVSQDVFLF-NDTVAEN 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 114 IAFslAVRGISRrdakERVEWAIELVRLNGLEHRKP-----------SQLSGGQQQRVAIARALVFGPKLLLLDEPLAAL 182
Cdd:cd03251   96 IAY--GRPGATR----EEVEEAARAANAHEFIMELPegydtvigergVKLSGGQRQRIAIARALLKDPPILILDEATSAL 169

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 183 DRKLREEVRLELRRLQGtlGVTTVLVTHDQDEAMSmSDRIAVLAQGVIQQLGSPGELYRQ 242
Cdd:cd03251  170 DTESERLVQAALERLMK--NRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEELLAQ 226
nickel_nikD TIGR02770
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ...
 36-255 1.03e-31

nickel import ATP-binding protein NikD; This family represents the NikD 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. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 131817 [Multi-domain]  Cd Length: 230  Bit Score: 119.40  E-value: 1.03e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   36 AVSDVDLTVAEGEFLSILGPSGSGKST----LLGLVAGLIQPTGGRIVIGSRDVTHVPPAQRDIGLVFQS--YALFPNMT 109
Cdd:TIGR02770   1 LVQDLNLSLKRGEVLALVGESGSGKSLtclaILGLLPPGLTQTSGEILLDGRPLLPLSIRGRHIATIMQNprTAFNPLFT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  110 VAGNIAFSLAVRGISRRDAKERVEWAIELVRLNGLE---HRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAALDRKL 186
Cdd:TIGR02770  81 MGNHAIETLRSLGKLSKQARALILEALEAVGLPDPEevlKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVN 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 914601027  187 REEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELYRQPANRFVAGFLGAA 255
Cdd:TIGR02770 161 QARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKHETTRKLLSAH 229
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
 21-242 1.15e-31

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


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 119.80  E-value: 1.15e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  21 AIEVSGLSKHF----------------------GTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRI 78
Cdd:COG1134    4 MIEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  79 VIGSRdvtHVPPAqrDIGLVFQsyalfPNMTVAGNIAFSLAVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQ 158
Cdd:COG1134   84 EVNGR---VSALL--ELGAGFH-----PELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQPVKTYSSGMRA 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 159 RVAIARALVFGPKLLLLDEPLAALDRKLREEVRLELRRLQGTlGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGE 238
Cdd:COG1134  154 RLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEE 232


                 ....*..
gi 914601027 239 ---LYRQ 242
Cdd:COG1134  233 viaAYEA 239
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
 20-239 1.33e-31

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 123.41  E-value: 1.33e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  20 PAIEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVthvppAQRDIGLVF 99
Cdd:PRK09536   2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDV-----EALSARAAS 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 100 QSYALFPNMTvagNIAFSLAVRGI------------SRRDAKER--VEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARA 165
Cdd:PRK09536  77 RRVASVPQDT---SLSFEFDVRQVvemgrtphrsrfDTWTETDRaaVERAMERTGVAQFADRPVTSLSGGERQRVLLARA 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 914601027 166 LVFGPKLLLLDEPLAALDrkLREEVR-LELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGEL 239
Cdd:PRK09536 154 LAQATPVLLLDEPTASLD--INHQVRtLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADV 226
CP_lyasePhnK TIGR02323
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ...
 20-234 3.90e-31

phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]


Pssm-ID: 188208 [Multi-domain]  Cd Length: 253  Bit Score: 118.78  E-value: 3.90e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   20 PAIEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRD-----VTHVPPAQR- 93
Cdd:TIGR02323   2 PLLQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSgaeleLYQLSEAERr 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   94 -----DIGLVFQSYALFPNMTVA--GNIA---FSLAVR--GISRRDAK---ERVEwaIELVRLNGLehrkPSQLSGGQQQ 158
Cdd:TIGR02323  82 rlmrtEWGFVHQNPRDGLRMRVSagANIGerlMAIGARhyGNIRATAQdwlEEVE--IDPTRIDDL----PRAFSGGMQQ 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 914601027  159 RVAIARALVFGPKLLLLDEPLAALDRKLREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLG 234
Cdd:TIGR02323 156 RLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESG 231
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
 37-238 4.45e-31

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: 123.70  E-value: 4.45e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  37 VSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQ--RDIGLVFQSYALFPNmTVAGNI 114
Cdd:COG4618  348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREElgRHIGYLPQDVELFDG-TIAENI 426

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 115 A-FSLAvrgisrrDAkERVEWAIELVRLNGLEHRKP-----------SQLSGGQQQRVAIARALvFG-PKLLLLDEPLAA 181
Cdd:COG4618  427 ArFGDA-------DP-EKVVAAAKLAGVHEMILRLPdgydtrigeggARLSGGQRQRIGLARAL-YGdPRLVVLDEPNSN 497

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 914601027 182 LD----RKLREEVRlELRRlqgtLGVTTVLVTHDQdEAMSMSDRIAVLAQGVIQQLGSPGE 238
Cdd:COG4618  498 LDdegeAALAAAIR-ALKA----RGATVVVITHRP-SLLAAVDKLLVLRDGRVQAFGPRDE 552
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
 20-246 7.98e-31

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 117.95  E-value: 7.98e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  20 PAIEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLV--AGLIQP---TGGRIVIGSRDV----THVPP 90
Cdd:PRK14239   4 PILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPevtITGSIVYNGHNIysprTDTVD 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  91 AQRDIGLVFQSYALFPnMTVAGNIAFSLAVRGIsrRDaKERVEWAIElVRLNGLE---------HRKPSQLSGGQQQRVA 161
Cdd:PRK14239  84 LRKEIGMVFQQPNPFP-MSIYENVVYGLRLKGI--KD-KQVLDEAVE-KSLKGASiwdevkdrlHDSALGLSGGQQQRVC 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 162 IARALVFGPKLLLLDEPLAALD----RKLrEEVRLELRRlqgtlGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPG 237
Cdd:PRK14239 159 IARVLATSPKIILLDEPTSALDpisaGKI-EETLLGLKD-----DYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTK 232


                 ....*....
gi 914601027 238 ELYRQPANR 246
Cdd:PRK14239 233 QMFMNPKHK 241
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
 39-239 1.72e-30

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: 116.56  E-value: 1.72e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  39 DVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHV--PPAQRDIGLVFQSYALFpNMTVAGNIAF 116
Cdd:cd03253   19 DVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVtlDSLRRAIGVVPQDTVLF-NDTIGYNIRY 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 117 SlavrgisRRDA-KERVEWAIELVRLNGLEHRKPSQ-----------LSGGQQQRVAIARALVFGPKLLLLDEPLAALDR 184
Cdd:cd03253   98 G-------RPDAtDEEVIEAAKAAQIHDKIMRFPDGydtivgerglkLSGGEKQRVAIARAILKNPPILLLDEATSALDT 170

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 914601027 185 KLREEVRLELRRLQGtlGVTTVLVTHDQDEAMSmSDRIAVLAQGVIQQLGSPGEL 239
Cdd:cd03253  171 HTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEEL 222
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
 36-240 2.55e-30

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 117.26  E-value: 2.55e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  36 AVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTH----VPPAQRDIGLVFQS--YALFpNMT 109
Cdd:PRK13636  21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYsrkgLMKLRESVGMVFQDpdNQLF-SAS 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 110 VAGNIAFSLAVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAALDRKLREE 189
Cdd:PRK13636 100 VYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSE 179

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 914601027 190 VRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELY 240
Cdd:PRK13636 180 IMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
19-230 3.04e-30

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


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 115.75  E-value: 3.04e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  19 RPAIEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQ---RDI 95
Cdd:PRK11614   3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKimrEAV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  96 GLVFQSYALFPNMTVAGNiafsLAVRGI--SRRDAKERVEWAIELV-RLNGLEHRKPSQLSGGQQQRVAIARALVFGPKL 172
Cdd:PRK11614  83 AIVPEGRRVFSRMTVEEN----LAMGGFfaERDQFQERIKWVYELFpRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRL 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 914601027 173 LLLDEPLAALDRKLREEVRLELRRLQGTlGVTTVLVTHDQDEAMSMSDRIAVLAQGVI 230
Cdd:PRK11614 159 LLLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHV 215
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
 39-242 3.53e-30

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: 121.47  E-value: 3.53e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  39 DVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPA--QRDIGLVFQSYALFpNMTVAGNIAF 116
Cdd:COG5265  376 GVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQAslRAAIGIVPQDTVLF-NDTIAYNIAY 454

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 117 slavrgiSRRDA-KERVEWAIELVRL--------NGLEHR------KpsqLSGGQQQRVAIARALVFGPKLLLLDEPLAA 181
Cdd:COG5265  455 -------GRPDAsEEEVEAAARAAQIhdfieslpDGYDTRvgerglK---LSGGEKQRVAIARTLLKNPPILIFDEATSA 524

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 914601027 182 LDRKLREEVRLELRRLqgTLGVTTVLVTH------DqdeamsmSDRIAVLAQGVIQQLGSPGELYRQ 242
Cdd:COG5265  525 LDSRTERAIQAALREV--ARGRTTLVIAHrlstivD-------ADEILVLEAGRIVERGTHAELLAQ 582
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
 36-242 4.27e-30

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: 115.66  E-value: 4.27e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  36 AVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPA--QRDIGLVFQSYALFpNMTVAGN 113
Cdd:cd03252   17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAwlRRQVGVVLQENVLF-NRSIRDN 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 114 IAfsLAVRGISRrdakERVEWAIELVRLNGLEHRKP-----------SQLSGGQQQRVAIARALVFGPKLLLLDEPLAAL 182
Cdd:cd03252   96 IA--LADPGMSM----ERVIEAAKLAGAHDFISELPegydtivgeqgAGLSGGQRQRIAIARALIHNPRILIFDEATSAL 169

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 183 DrklREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELYRQ 242
Cdd:cd03252  170 D---YESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAE 226
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
22-255 4.96e-30

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 116.04  E-value: 4.96e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  22 IEVSGLSKHF---------GTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQ 92
Cdd:PRK15112   5 LEVRNLSKTFryrtgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSY 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  93 RD--IGLVFQ--SYALFPNMTVAGNIAFSLavRGISRRDAKERVEWAIELVRLNGL--EHRK--PSQLSGGQQQRVAIAR 164
Cdd:PRK15112  85 RSqrIRMIFQdpSTSLNPRQRISQILDFPL--RLNTDLEPEQREKQIIETLRQVGLlpDHASyyPHMLAPGQKQRLGLAR 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 165 ALVFGPKLLLLDEPLAALDRKLREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELYRQP- 243
Cdd:PRK15112 163 ALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPl 242

                        250
                 ....*....|....*
gi 914601027 244 ---ANRFVAGFLGAA 255
Cdd:PRK15112 243 helTKRLIAGHFGEA 257
cbiO PRK13641
energy-coupling factor transporter ATPase;
39-243 6.18e-30

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 116.47  E-value: 6.18e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  39 DVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVT------HVPPAQRDIGLVFQ--SYALFPNmTV 110
Cdd:PRK13641  25 NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgnkNLKKLRKKVSLVFQfpEAQLFEN-TV 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 111 AGNIAFSLAVRGISRRDAKERvewAIELVRLNGLE----HRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAALDRKL 186
Cdd:PRK13641 104 LKDVEFGPKNFGFSEDEAKEK---ALKWLKKVGLSedliSKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEG 180

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 914601027 187 REEVrLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELYRQP 243
Cdd:PRK13641 181 RKEM-MQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
 36-239 6.30e-30

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: 114.63  E-value: 6.30e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  36 AVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQ--RDIGLVFQSYALFPNmTVAGN 113
Cdd:cd03254   18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSlrSMIGVVLQDTFLFSG-TIMEN 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 114 IAFslavrgiSRRDAK-ERVEWAIELVRL--------NGLEH---RKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAA 181
Cdd:cd03254   97 IRL-------GRPNATdEEVIEAAKEAGAhdfimklpNGYDTvlgENGGNLSQGERQLLAIARAMLRDPKILILDEATSN 169

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 914601027 182 LDRKLREEVRLELRRLQGtlGVTTVLVTHD----QDeamsmSDRIAVLAQGVIQQLGSPGEL 239
Cdd:cd03254  170 IDTETEKLIQEALEKLMK--GRTSIIIAHRlstiKN-----ADKILVLDDGKIIEEGTHDEL 224
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
20-239 8.19e-30

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 116.44  E-value: 8.19e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  20 PAIEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDV-THVPPAQRDIGLV 98
Cdd:PRK13537   6 APIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVpSRARHARQRVGVV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  99 FQSYALFPNMTVAGNIAFSLAVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEP 178
Cdd:PRK13537  86 PQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEP 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 914601027 179 LAALDRKLREEVRLELRRLQGTlGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGEL 239
Cdd:PRK13537 166 TTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHAL 225
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
 15-244 1.07e-29

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 116.49  E-value: 1.07e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  15 PVSRRPAIEVSGLSKHFGT-----VCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIG-------- 81
Cdd:PRK13631  15 PLSDDIILRVKNLYCVFDEkqeneLVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyigdkk 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  82 ----------SRDVTHVPPAQRDIGLVFQ--SYALFPNmTVAGNIAFSLAVRGISRRDAKERVEWAIELVRLNG--LEhR 147
Cdd:PRK13631  95 nnhelitnpySKKIKNFKELRRRVSMVFQfpEYQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDsyLE-R 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 148 KPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAALDRK-LREEVRLELRRLQGtlGVTTVLVTHDQDEAMSMSDRIAVLA 226
Cdd:PRK13631 173 SPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKgEHEMMQLILDAKAN--NKTVFVITHTMEHVLEVADEVIVMD 250

                        250
                 ....*....|....*...
gi 914601027 227 QGVIQQLGSPGELYRQPA 244
Cdd:PRK13631 251 KGKILKTGTPYEIFTDQH 268
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
 27-239 1.10e-29

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 114.61  E-value: 1.10e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  27 LSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVP---PAQRDIGLVFQSYA 103
Cdd:PRK10895   9 LAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlhaRARRGIGYLPQEAS 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 104 LFPNMTVAGNIAFSLAVR-GISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAAL 182
Cdd:PRK10895  89 IFRRLSVYDNLMAVLQIRdDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGV 168

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 914601027 183 DRKLREEVRLELRRLQGTlGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGEL 239
Cdd:PRK10895 169 DPISVIDIKRIIEHLRDS-GLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
 12-239 1.23e-29

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: 119.82  E-value: 1.23e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   12 TLAPVSRRPAIEVSGLSKHFG--TVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVP 89
Cdd:TIGR02203 321 TRAIERARGDVEFRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYT 400

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   90 PA--QRDIGLVFQSYALFpNMTVAGNIAFSlAVRGISRrdakERVEWAIELVRLNGLEHRKP-----------SQLSGGQ 156
Cdd:TIGR02203 401 LAslRRQVALVSQDVVLF-NDTIANNIAYG-RTEQADR----AEIERALAAAYAQDFVDKLPlgldtpigengVLLSGGQ 474

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  157 QQRVAIARALVFGPKLLLLDEPLAALDRKLREEVRLELRRLQGtlGVTTVLVTHdQDEAMSMSDRIAVLAQGVIQQLGSP 236
Cdd:TIGR02203 475 RQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAH-RLSTIEKADRIVVMDDGRIVERGTH 551


                  ...
gi 914601027  237 GEL 239
Cdd:TIGR02203 552 NEL 554
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
 22-184 1.92e-29

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 112.66  E-value: 1.92e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  22 IEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVI--GSRDVTHVPPAQRDIGlvf 99
Cdd:PRK13539   3 LEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLdgGDIDDPDVAEACHYLG--- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 100 QSYALFPNMTVAGNIAFSLAVRGISRRDAKErvewAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPL 179
Cdd:PRK13539  80 HRNAMKPALTVAENLEFWAAFLGGEELDIAA----ALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPT 155


                 ....*
gi 914601027 180 AALDR 184
Cdd:PRK13539 156 AALDA 160
cbiO PRK13644
energy-coupling factor transporter ATPase;
36-248 2.63e-29

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 114.31  E-value: 2.63e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  36 AVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIV---IGSRDVTHVPPAQRDIGLVFQS-YALFPNMTVA 111
Cdd:PRK13644  17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLvsgIDTGDFSKLQGIRKLVGIVFQNpETQFVGRTVE 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 112 GNIAFSLAVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAALDRKLREEVR 191
Cdd:PRK13644  97 EDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVL 176

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 914601027 192 LELRRLQGTlGVTTVLVTHDQDEaMSMSDRIAVLAQGVIQQLGSPGELYRQPANRFV 248
Cdd:PRK13644 177 ERIKKLHEK-GKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDVSLQTL 231
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
 20-230 3.14e-29

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 118.23  E-value: 3.14e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  20 PAIEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPA---QRDIG 96
Cdd:PRK15439  10 PLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAkahQLGIY 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  97 LVFQSYALFPNMTVAGNIAFSLAvrgiSRRDAKERVEwaiELVRLNGLE---HRKPSQLSGGQQQRVAIARALVFGPKLL 173
Cdd:PRK15439  90 LVPQEPLLFPNLSVKENILFGLP----KRQASMQKMK---QLLAALGCQldlDSSAGSLEVADRQIVEILRGLMRDSRIL 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 914601027 174 LLDEPLAALDRKLREEVRLELRRLQgTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVI 230
Cdd:PRK15439 163 ILDEPTASLTPAETERLFSRIRELL-AQGVGIVFISHKLPEIRQLADRISVMRDGTI 218
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
 20-236 5.64e-29

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: 118.96  E-value: 5.64e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027    20 PAIEVSGLSKHFGTVC--AVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDV-THVPPAQRDIG 96
Cdd:TIGR01257  927 PGVCVKNLVKIFEPSGrpAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIeTNLDAVRQSLG 1006

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027    97 LVFQSYALFPNMTVAGNIAFSLAVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLD 176
Cdd:TIGR01257 1007 MCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLD 1086

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   177 EPLAALDRKLREEVRLELRRLQGtlGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSP 236
Cdd:TIGR01257 1087 EPTSGVDPYSRRSIWDLLLKYRS--GRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
22-238 6.06e-29

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 112.80  E-value: 6.06e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  22 IEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQ--RDIGLVF 99
Cdd:PRK11231   3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQlaRRLALLP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 100 QSYALFPNMTVAGNIAF------SLAVRgISRRDaKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLL 173
Cdd:PRK11231  83 QHHLTPEGITVRELVAYgrspwlSLWGR-LSAED-NARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVV 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 914601027 174 LLDEPLAALDRKLREEVRLELRRLQgTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGE 238
Cdd:PRK11231 161 LLDEPTTYLDINHQVELMRLMRELN-TQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEE 224
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
 36-185 1.30e-28

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: 110.53  E-value: 1.30e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   36 AVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPA-QRDIGLVFQSYALFPNMTVAGNI 114
Cdd:TIGR01189  15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEpHENILYLGHLPGLKPELSALENL 94

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 914601027  115 AFSLAVRGISRRDAKErvewAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAALDRK 185
Cdd:TIGR01189  95 HFWAAIHGGAQRTIED----ALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
 8-254 1.96e-27

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 113.80  E-value: 1.96e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   8 SERDTLAPvsRRPAIEVSGLSKHFGT-----------VCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGG 76
Cdd:PRK10261 302 IEQDTVVD--GEPILQVRNLVTRFPLrsgllnrvtreVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGG 379

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  77 RIVIGSRDVTHVPPAQ-----RDIGLVFQS-YA-LFPNMTVAGNIAFSLAVRGISRRD-AKERVEWAIELVRLNGlEH-- 146
Cdd:PRK10261 380 EIIFNGQRIDTLSPGKlqalrRDIQFIFQDpYAsLDPRQTVGDSIMEPLRVHGLLPGKaAAARVAWLLERVGLLP-EHaw 458

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 147 RKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAALDRKLREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLA 226
Cdd:PRK10261 459 RYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMY 538

                        250       260
                 ....*....|....*....|....*...
gi 914601027 227 QGVIQQLGSPGELYRQPANRFVAGFLGA 254
Cdd:PRK10261 539 LGQIVEIGPRRAVFENPQHPYTRKLMAA 566
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
 22-251 2.25e-27

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: 112.97  E-value: 2.25e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   22 IEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGL--IQPTGGRIV-------------IGSRDVT 86
Cdd:TIGR03269   1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyveRPSKVGE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   87 HVPPA----------------------QRDIGLVFQ-SYALFPNMTVAGNIAFSLAVRGISrrdAKERVEWAIELVRLNG 143
Cdd:TIGR03269  81 PCPVCggtlepeevdfwnlsdklrrriRKRIAIMLQrTFALYGDDTVLDNVLEALEEIGYE---GKEAVGRAVDLIEMVQ 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  144 LEHRK---PSQLSGGQQQRVAIARALVFGPKLLLLDEPLAALDRKLREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSD 220
Cdd:TIGR03269 158 LSHRIthiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSD 237

                         250       260       270
                  ....*....|....*....|....*....|.
gi 914601027  221 RIAVLAQGVIQQLGSPGELyrqpANRFVAGF 251
Cdd:TIGR03269 238 KAIWLENGEIKEEGTPDEV----VAVFMEGV 264
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
 12-369 7.09e-27

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 109.04  E-value: 7.09e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  12 TLAPVSRRPAIEVSGLSKHFGT----VCAVSDVDLTVAEGEFLSILGPSGSGKS----TLLGLVA--GLIqptGGRIVIG 81
Cdd:PRK09473   3 PLAQQQADALLDVKDLRVTFSTpdgdVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAanGRI---GGSATFN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  82 SRDVTHVPPAQ------RDIGLVFQS--YALFPNMTVAGNIAFSLAV-RGISRRDAKERVEWAIELVRLNglEHRK---- 148
Cdd:PRK09473  80 GREILNLPEKElnklraEQISMIFQDpmTSLNPYMRVGEQLMEVLMLhKGMSKAEAFEESVRMLDAVKMP--EARKrmkm 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 149 -PSQLSGGQQQRVAIARALVFGPKLLLLDEPLAALDRKLREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQ 227
Cdd:PRK09473 158 yPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYA 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 228 GVIQQLGSPGELYRQPANRFVAGFLGAanlfhgiIARegngavLALDGGTRLPLAGDYPSLgrratmLVRPERVNLQPAt 307
Cdd:PRK09473 238 GRTMEYGNARDVFYQPSHPYSIGLLNA-------VPR------LDAEGESLLTIPGNPPNL------LRLPKGCPFQPR- 297

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 914601027 308 eapanrfcidCHVADVVYQgeivryavEAPPVGPviascqhvvprFSPGD-RACFswRPEDAW 369
Cdd:PRK09473 298 ----------CPHAMEICS--------SAPPLEE-----------FGPGRlRACF--KPVEEL 329
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
20-228 7.61e-27

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 111.41  E-value: 7.61e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  20 PAIEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPP---AQRDIG 96
Cdd:PRK09700   4 PYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHklaAQLGIG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  97 LVFQSYALFPNMTVAGNIAFS-LAVR---GISRRDAKE-RVEWAIELVRLnGLE---HRKPSQLSGGQQQRVAIARALVF 168
Cdd:PRK09700  84 IIYQELSVIDELTVLENLYIGrHLTKkvcGVNIIDWREmRVRAAMMLLRV-GLKvdlDEKVANLSISHKQMLEIAKTLML 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 169 GPKLLLLDEPLAALDRKLREEVRLELRRLQGTlGVTTVLVTHDQDEAMSMSDRIAVLAQG 228
Cdd:PRK09700 163 DAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDG 221
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
 37-234 3.26e-26

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: 104.66  E-value: 3.26e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  37 VSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQP---TGGRIVIGSRDVThvpPA--QRDIGLVFQSYALFPNMTVA 111
Cdd:cd03234   23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPRK---PDqfQKCVAYVRQDDILLPGLTVR 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 112 GNIAFSLAVRGISRRDAKER-VEWAIELVRLNGLE---HRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAALDRKLR 187
Cdd:cd03234  100 ETLTYTAILRLPRKSSDAIRkKRVEDVLLRDLALTrigGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTA 179

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 914601027 188 EEVRLELRRLqgTLGVTTVLVTHDQ--DEAMSMSDRIAVLAQGVIQQLG 234
Cdd:cd03234  180 LNLVSTLSQL--ARRNRIVILTIHQprSDLFRLFDRILLLSSGEIVYSG 226
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
 16-211 4.02e-26

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: 109.37  E-value: 4.02e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   16 VSRRPAIEVSGLSKHF-GTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQ-- 92
Cdd:TIGR02868 329 GLGKPTLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEvr 408

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   93 RDIGLVFQSYALFpNMTVAGNIAfslavrgISRRDA-KERVEWAIELVRLNGLEHRKP-----------SQLSGGQQQRV 160
Cdd:TIGR02868 409 RRVSVCAQDAHLF-DTTVRENLR-------LARPDAtDEELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRL 480

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 914601027  161 AIARALVFGPKLLLLDEPLAALDRKLREEVRLELrrLQGTLGVTTVLVTHD 211
Cdd:TIGR02868 481 ALARALLADAPILLLDEPTEHLDAETADELLEDL--LAALSGRTVVLITHH 529
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
 22-254 4.46e-26

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 106.75  E-value: 4.46e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  22 IEVSGLSKHFGTVC----AVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTG----GRIVIGSRDVTHVPPAQR 93
Cdd:PRK11022   4 LNVDKLSVHFGDESapfrAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGrvmaEKLEFNGQDLQRISEKER 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  94 ------DIGLVFQS--YALFPNMTVAGNIAFSLAV-RGISRRDAKERvewAIELVRLNGL---EHR---KPSQLSGGQQQ 158
Cdd:PRK11022  84 rnlvgaEVAMIFQDpmTSLNPCYTVGFQIMEAIKVhQGGNKKTRRQR---AIDLLNQVGIpdpASRldvYPHQLSGGMSQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 159 RVAIARALVFGPKLLLLDEPLAALDRKLREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGE 238
Cdd:PRK11022 161 RVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHD 240

                        250
                 ....*....|....*.
gi 914601027 239 LYRQPANRFVAGFLGA 254
Cdd:PRK11022 241 IFRAPRHPYTQALLRA 256
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
 38-228 4.98e-26

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: 103.32  E-value: 4.98e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  38 SDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRdvthvppaqrdIGLVFQSyALFPNMTVAGNIAFS 117
Cdd:cd03250   22 KDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS-----------IAYVSQE-PWIQNGTIRENILFG 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 118 lavrgiSRRDaKERVEWAIE---LVR-LNGLEHR-------KPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAALD--- 183
Cdd:cd03250   90 ------KPFD-EERYEKVIKacaLEPdLEILPDGdlteigeKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDahv 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 914601027 184 -RKLREEVrlelrrLQGTL--GVTTVLVTHdQDEAMSMSDRIAVLAQG 228
Cdd:cd03250  163 gRHIFENC------ILGLLlnNKTRILVTH-QLQLLPHADQIVVLDNG 203
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
 36-247 2.06e-25

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 107.48  E-value: 2.06e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  36 AVSDVDLTVAEGEFLSILGPSGSGKST----LLGLVAgliqpTGGRIVIGSRDVTHVP-----PAQRDIGLVFQ--SYAL 104
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLHNLNrrqllPVRHRIQVVFQdpNSSL 375

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 105 FPNMTVAGNIAFSLAV--RGISRRDAKERVEWAIELVRLN-GLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAA 181
Cdd:PRK15134 376 NPRLNVLQIIEEGLRVhqPTLSAAQREQQVIAVMEEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSS 455

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 914601027 182 LDRKLREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELYRQPANRF 247
Cdd:PRK15134 456 LDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEY 521
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
 22-223 2.42e-25

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 103.32  E-value: 2.42e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  22 IEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLL---GLVAGLIQP--TGGRIVIGSRDV--THVPPAQ-- 92
Cdd:PRK14243  11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILrcfNRLNDLIPGfrVEGKVTFHGKNLyaPDVDPVEvr 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  93 RDIGLVFQSYALFPNmTVAGNIAFSLAVRGIsRRDAKERVEWAI----------ELVRLNGLehrkpsQLSGGQQQRVAI 162
Cdd:PRK14243  91 RRIGMVFQKPNPFPK-SIYDNIAYGARINGY-KGDMDELVERSLrqaalwdevkDKLKQSGL------SLSGGQQQRLCI 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 914601027 163 ARALVFGPKLLLLDEPLAALD--RKLR-EEVRLELRRlqgtlGVTTVLVTHDQDEAMSMSDRIA 223
Cdd:PRK14243 163 ARAIAVQPEVILMDEPCSALDpiSTLRiEELMHELKE-----QYTIIIVTHNMQQAARVSDMTA 221
type_I_sec_PrtD TIGR01842
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ...
 37-234 2.61e-25

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: 107.05  E-value: 2.61e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   37 VSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQ--RDIGLVFQSYALFPNmTVAGNI 114
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETfgKHIGYLPQDVELFPG-TVAENI 412

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  115 AfslavrgisRRDAKERVEWAIELVRLNG---LEHRKP-----------SQLSGGQQQRVAIARALVFGPKLLLLDEPLA 180
Cdd:TIGR01842 413 A---------RFGENADPEKIIEAAKLAGvheLILRLPdgydtvigpggATLSGGQRQRIALARALYGDPKLVVLDEPNS 483

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 914601027  181 ALDRKLREEVRLELRRLQGTlGVTTVLVTHdQDEAMSMSDRIAVLAQGVIQQLG 234
Cdd:TIGR01842 484 NLDEEGEQALANAIKALKAR-GITVVVITH-RPSLLGCVDKILVLQDGRIARFG 535
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
52-240 3.42e-25

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 103.16  E-value: 3.42e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  52 ILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTH----VPPAQRDIGLVFQSyalfPNMTV-----AGNIAFSLAVRG 122
Cdd:PRK13638  32 LVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYskrgLLALRQQVATVFQD----PEQQIfytdiDSDIAFSLRNLG 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 123 ISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAALDRKLREEVRLELRRLQGTlG 202
Cdd:PRK13638 108 VPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQ-G 186

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 914601027 203 VTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELY 240
Cdd:PRK13638 187 NHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
 24-231 5.60e-25

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 105.92  E-value: 5.60e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  24 VSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIgSRDVThvppaqrdIGLVFQSYA 103
Cdd:COG0488    1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI-PKGLR--------IGYLPQEPP 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 104 LFPNMTVAGNIAFSLA-VRGISRR-------------------DAKERVE----WAIElVR----LNGLE------HRKP 149
Cdd:COG0488   72 LDDDLTVLDTVLDGDAeLRALEAEleeleaklaepdedlerlaELQEEFEalggWEAE-ARaeeiLSGLGfpeedlDRPV 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 150 SQLSGGQQQRVAIARALVFGPKLLLLDEPLAALDrklREEVR-LE--LRRLQGTLgvttVLVTHDQ---DEamsMSDRIA 223
Cdd:COG0488  151 SELSGGWRRRVALARALLSEPDLLLLDEPTNHLD---LESIEwLEefLKNYPGTV----LVVSHDRyflDR---VATRIL 220


                 ....*...
gi 914601027 224 VLAQGVIQ 231
Cdd:COG0488  221 ELDRGKLT 228
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
 38-210 6.83e-25

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: 100.26  E-value: 6.83e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  38 SDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPA-QRDIGLVFQSYALFPNMTVAGNIAF 116
Cdd:cd03231   17 SGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSiARGLLYLGHAPGIKTTLSVLENLRF 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 117 slavrgISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAALDR----KLREEVRL 192
Cdd:cd03231   97 ------WHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKagvaRFAEAMAG 170

                        170
                 ....*....|....*...
gi 914601027 193 ELRRlqgtlGVTTVLVTH 210
Cdd:cd03231  171 HCAR-----GGMVVLTTH 183
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
 37-228 8.17e-25

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: 99.93  E-value: 8.17e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  37 VSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTG--GRIVIGSRDVTHVPPAQRdIGLVFQSYALFPNMTVAGNI 114
Cdd:cd03213   25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGRPLDKRSFRKI-IGYVPQDDILHPTLTVRETL 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 115 AFSLAVRGISrrdakervewaielvrlnglehrkpsqlsGGQQQRVAIARALVFGPKLLLLDEPLAALDRKLREEVRLEL 194
Cdd:cd03213  104 MFAAKLRGLS-----------------------------GGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLL 154

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 914601027 195 RRLQGTlGVTTVLVTHD-QDEAMSMSDRIAVLAQG 228
Cdd:cd03213  155 RRLADT-GRTIICSIHQpSSEIFELFDKLLLLSQG 188
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
38-213 9.47e-25

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 99.88  E-value: 9.47e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  38 SDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVThvppAQRDiglVFQSYALF--------PNMT 109
Cdd:PRK13538  18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIR----RQRD---EYHQDLLYlghqpgikTELT 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 110 VAGNIAFSLAVRGISRRDAkerVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAALDRKLREE 189
Cdd:PRK13538  91 ALENLRFYQRLHGPGDDEA---LWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVAR 167

                        170       180
                 ....*....|....*....|....*
gi 914601027 190 V-RLELRRLQGtlGVTTVLVTHdQD 213
Cdd:PRK13538 168 LeALLAQHAEQ--GGMVILTTH-QD 189
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
 20-228 1.99e-24

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 104.24  E-value: 1.99e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  20 PAIEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGlIQPTG---GRIVIGSRDVT--HVPPAQRD 94
Cdd:PRK13549   4 YLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPHGtyeGEIIFEGEELQasNIRDTERA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  95 -IGLVFQSYALFPNMTVAGNIaF---SLAVRGISRRDA-KERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFG 169
Cdd:PRK13549  83 gIAIIHQELALVKELSVLENI-FlgnEITPGGIMDYDAmYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQ 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 914601027 170 PKLLLLDEPLAALDRKlREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQG 228
Cdd:PRK13549 162 ARLLILDEPTASLTES-ETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDG 219
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
 39-243 2.67e-24

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 104.42  E-value: 2.67e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   39 DVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVT---HVPpAQRDIGLVFQSYALFpNMTVAGNIA 115
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVqydHHY-LHRQVALVGQEPVLF-SGSVRENIA 576

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  116 FSLavrgisRRDAKERVEWAIELVR----LNGLEH-------RKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAALDR 184
Cdd:TIGR00958 577 YGL------TDTPDEEIMAAAKAANahdfIMEFPNgydtevgEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDA 650

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 914601027  185 KLrEEVRLELRRLQGTlgvTTVLVTHdQDEAMSMSDRIAVLAQGVIQQLGSPGELYRQP 243
Cdd:TIGR00958 651 EC-EQLLQESRSRASR---TVLLIAH-RLSTVERADQILVLKKGSVVEMGTHKQLMEDQ 704
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
 24-254 2.68e-24

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 104.55  E-value: 2.68e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  24 VSGLSKHF----GTVCAVSDVDLTVAEGEFLSILGPSGSGKS-TLLGLVAgLIQPTGG-------------RIVIGSRDV 85
Cdd:PRK10261  15 VENLNIAFmqeqQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMR-LLEQAGGlvqcdkmllrrrsRQVIELSEQ 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  86 T-----HVPPAqrDIGLVFQS--YALFPNMTVAGNIAFSLAV-RGISRRDAKERVEWAIELVRL---NGLEHRKPSQLSG 154
Cdd:PRK10261  94 SaaqmrHVRGA--DMAMIFQEpmTSLNPVFTVGEQIAESIRLhQGASREEAMVEAKRMLDQVRIpeaQTILSRYPHQLSG 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 155 GQQQRVAIARALVFGPKLLLLDEPLAALDRKLREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLG 234
Cdd:PRK10261 172 GMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETG 251

                        250       260
                 ....*....|....*....|
gi 914601027 235 SPGELYRQPANRFVAGFLGA 254
Cdd:PRK10261 252 SVEQIFHAPQHPYTRALLAA 271
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
 20-253 3.12e-24

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 100.56  E-value: 3.12e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  20 PAIEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPT-----------GGRIVIGSRDVTHV 88
Cdd:PRK14271  20 PAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVsgyrysgdvllGGRSIFNYRDVLEF 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  89 ppaQRDIGLVFQSYALFP----NMTVAGNIAFSLA----VRGISRRDAKERVEWAIELVRLNGlehrKPSQLSGGQQQRV 160
Cdd:PRK14271 100 ---RRRVGMLFQRPNPFPmsimDNVLAGVRAHKLVprkeFRGVAQARLTEVGLWDAVKDRLSD----SPFRLSGGQQQLL 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 161 AIARALVFGPKLLLLDEPLAALDRKLREEVRLELRRLQGTLgvTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELY 240
Cdd:PRK14271 173 CLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLF 250

                        250
                 ....*....|....*..
gi 914601027 241 RQPAN----RFVAGFLG 253
Cdd:PRK14271 251 SSPKHaetaRYVAGLSG 267
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
11-239 1.21e-23

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 102.35  E-value: 1.21e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  11 DTLAPVSRRP-AIEVSGLS----------KHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIV 79
Cdd:PRK13657 314 DAVPDVRDPPgAIDLGRVKgavefddvsfSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRIL 393

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  80 IGSRDVTHVPPA--QRDIGLVFQSYALFpNMTVAGNIAfslavrgISRRDA-KERVEWAIELVRLNGLEHRKP------- 149
Cdd:PRK13657 394 IDGTDIRTVTRAslRRNIAVVFQDAGLF-NRSIEDNIR-------VGRPDAtDEEMRAAAERAQAHDFIERKPdgydtvv 465

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 150 ----SQLSGGQQQRVAIARALVFGPKLLLLDEPLAALDRKLREEVRLELRRLqgTLGVTTVLVTHdQDEAMSMSDRIAVL 225
Cdd:PRK13657 466 gergRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDEL--MKGRTTFIIAH-RLSTVRNADRILVF 542

                        250
                 ....*....|....
gi 914601027 226 AQGVIQQLGSPGEL 239
Cdd:PRK13657 543 DNGRVVESGSFDEL 556
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
 22-228 2.21e-23

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: 101.05  E-value: 2.21e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   22 IEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGlIQPTG---GRIVIGSRDV--THVPPAQRD-I 95
Cdd:TIGR02633   2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPHGtwdGEIYWSGSPLkaSNIRDTERAgI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   96 GLVFQSYALFPNMTVAGNIAF--SLAVRGISRRDAK--ERVEWAIELVRLNGLEHRKP-SQLSGGQQQRVAIARALVFGP 170
Cdd:TIGR02633  81 VIIHQELTLVPELSVAENIFLgnEITLPGGRMAYNAmyLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQA 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 914601027  171 KLLLLDEPLAALDRKlREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQG 228
Cdd:TIGR02633 161 RLLILDEPSSSLTEK-ETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDG 217
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
 20-223 2.48e-23

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 97.80  E-value: 2.48e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  20 PAIEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTG-----GRIVIGSRDV----THVPP 90
Cdd:PRK14258   6 PAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIyerrVNLNR 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  91 AQRDIGLVFQSYALFPnMTVAGNIAFSLAVRGISRR-DAKERVEWAIELVRL-----NGLeHRKPSQLSGGQQQRVAIAR 164
Cdd:PRK14258  86 LRRQVSMVHPKPNLFP-MSVYDNVAYGVKIVGWRPKlEIDDIVESALKDADLwdeikHKI-HKSALDLSGGQQQRLCIAR 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 914601027 165 ALVFGPKLLLLDEPLAALD--RKLREEVRLELRRLQGTLgvTTVLVTHDQDEAMSMSDRIA 223
Cdd:PRK14258 164 ALAVKPKVLLMDEPCFGLDpiASMKVESLIQSLRLRSEL--TMVIVSHNLHQVSRLSDFTA 222
SapD COG4170
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
32-243 3.05e-23

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


Pssm-ID: 443330 [Multi-domain]  Cd Length: 331  Bit Score: 98.82  E-value: 3.05e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  32 GTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQP----TGGRIVIGSRDVTHVPPAQR------DIGLVFQ- 100
Cdd:COG4170   18 GRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLLKLSPRERrkiigrEIAMIFQe 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 101 -SYALFPNMTVAGNIAFSL---AVRGISRRDAKERVEWAIELVRLNGL-EHRK-----PSQLSGGQQQRVAIARALVFGP 170
Cdd:COG4170   98 pSSCLDPSAKIGDQLIEAIpswTFKGKWWQRFKWRKKRAIELLHRVGIkDHKDimnsyPHELTEGECQKVMIAMAIANQP 177

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 914601027 171 KLLLLDEPLAALDRKLREEV-RLeLRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELYRQP 243
Cdd:COG4170  178 RLLIADEPTNAMESTTQAQIfRL-LARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSP 250
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
 14-231 4.83e-23

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 100.14  E-value: 4.83e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  14 APVSRRPAIEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGsrdvTHVppaqr 93
Cdd:COG0488  308 PERLGKKVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLG----ETV----- 378

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  94 DIGLVFQSYALF-PNMTVAGNIafslavrgisRRDAKERVEWAIE--LVRLN--GLEHRKP-SQLSGGQQQRVAIARALV 167
Cdd:COG0488  379 KIGYFDQHQEELdPDKTVLDEL----------RDGAPGGTEQEVRgyLGRFLfsGDDAFKPvGVLSGGEKARLALAKLLL 448

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 914601027 168 FGPKLLLLDEPLAALDRKLREEvrLE--LRRLQGTLgvttVLVTHDQDEAMSMSDRIAVLAQGVIQ 231
Cdd:COG0488  449 SPPNVLLLDEPTNHLDIETLEA--LEeaLDDFPGTV----LLVSHDRYFLDRVATRILEFEDGGVR 508
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
 39-230 5.20e-23

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: 96.00  E-value: 5.20e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  39 DVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPA--QRDIGLVFQSYALFPNmTVAGNIAF 116
Cdd:cd03248   32 DVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKylHSKVSLVGQEPVLFAR-SLQDNIAY 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 117 SLAvrGISRRDAKERVEWAIELVRLNGLEH-------RKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAALDRKLREE 189
Cdd:cd03248  111 GLQ--SCSFECVKEAAQKAHAHSFISELASgydtevgEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQ 188

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 914601027 190 VRlelRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVI 230
Cdd:cd03248  189 VQ---QALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
 36-236 6.77e-23

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: 95.25  E-value: 6.77e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  36 AVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQ--RDIGLVFQSYALFpnmtvAGN 113
Cdd:cd03244   19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDlrSRISIIPQDPVLF-----SGT 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 114 IAFSLAVRGISrrdAKERVEWAIELVRL--------NGLEHR---KPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAAL 182
Cdd:cd03244   94 IRSNLDPFGEY---SDEELWQALERVGLkefveslpGGLDTVveeGGENLSVGQRQLLCLARALLRKSKILVLDEATASV 170

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 914601027 183 D----RKLREEVRLELRrlqgtlGVTTVLVTHDQDEAMSmSDRIAVLAQGVIQQLGSP 236
Cdd:cd03244  171 DpetdALIQKTIREAFK------DCTVLTIAHRLDTIID-SDRILVLDKGRVVEFDSP 221
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
 22-213 1.06e-22

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: 92.51  E-value: 1.06e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  22 IEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDvthvppaqrDIGLVfqs 101
Cdd:cd03221    1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV---------KIGYF--- 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 102 yalfpnmtvagniafslavrgisrrdakervewaielvrlnglehrkpSQLSGGQQQRVAIARALVFGPKLLLLDEPLAA 181
Cdd:cd03221   69 ------------------------------------------------EQLSGGEKMRLALAKLLLENPNLLLLDEPTNH 100

                        170       180       190
                 ....*....|....*....|....*....|..
gi 914601027 182 LDRKLREEVRLELRRLQGTLgvttVLVTHDQD 213
Cdd:cd03221  101 LDLESIEALEEALKEYPGTV----ILVSHDRY 128
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
 40-243 1.49e-22

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 99.15  E-value: 1.49e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  40 VDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIqPTGGRIVIGSRDVTHVPPAQ--RDIGLVFQSYALFPNmTVAGNIAfs 117
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESwrKHLSWVGQNPQLPHG-TLRDNVL-- 444

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 118 LAVRGISRRDAKERVE--WAIELVRL--NGLEHRKPSQ---LSGGQQQRVAIARALVFGPKLLLLDEPLAALDRKLREEV 190
Cdd:PRK11174 445 LGNPDASDEQLQQALEnaWVSEFLPLlpQGLDTPIGDQaagLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLV 524

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 914601027 191 RLELRrlQGTLGVTTVLVTHDQDEAMSMsDRIAVLAQGVIQQLGSPGELYRQP 243
Cdd:PRK11174 525 MQALN--AASRRQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAELSQAG 574
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
 37-210 2.44e-22

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 98.34  E-value: 2.44e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  37 VSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIvigsrdvtHVPPAQRdigLVF---QSYalFPNMTVAGN 113
Cdd:COG4178  379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRI--------ARPAGAR---VLFlpqRPY--LPLGTLREA 445

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 114 IAFSLAVRGISRRDAKErvewAIELVRLNGL------EHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAALDRKLR 187
Cdd:COG4178  446 LLYPATAEAFSDAELRE----ALEAVGLGHLaerldeEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENE 521

                        170       180
                 ....*....|....*....|....
gi 914601027 188 EEVrleLRRLQGTL-GVTTVLVTH 210
Cdd:COG4178  522 AAL---YQLLREELpGTTVISVGH 542
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
 36-234 3.06e-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: 92.38  E-value: 3.06e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  36 AVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQRD-IGLVFQSYALFpNMTVAGNI 114
Cdd:cd03247   17 VLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSlISVLNQRPYLF-DTTLRNNL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 115 AfslavrgisrrdakervewaielvrlnglehrkpSQLSGGQQQRVAIARALVFGPKLLLLDEPLAALDRKLREEVrLEL 194
Cdd:cd03247   96 G----------------------------------RRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQL-LSL 140

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 914601027 195 rRLQGTLGVTTVLVTHdQDEAMSMSDRIAVLAQGVIQQLG 234
Cdd:cd03247  141 -IFEVLKDKTLIWITH-HLTGIEHMDKILFLENGKIIMQG 178
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
 22-239 4.65e-22

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: 97.89  E-value: 4.65e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   22 IEVSGLSKHFG-TVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGsrdvtHVPPAQRDIGLVFQ 100
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLN-----GFSLKDIDRHTLRQ 548

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  101 SYALFPNMTV--AGNIAFSL---AVRGISRRDAKERVEWA-----IELVRLnGLEHR---KPSQLSGGQQQRVAIARALV 167
Cdd:TIGR01193 549 FINYLPQEPYifSGSILENLllgAKENVSQDEIWAACEIAeikddIENMPL-GYQTElseEGSSISGGQKQRIALARALL 627

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 914601027  168 FGPKLLLLDEPLAALDRKLREEVRLELRRLQGTlgvTTVLVTHDQDEAmSMSDRIAVLAQGVIQQLGSPGEL 239
Cdd:TIGR01193 628 TDSKVLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVA-KQSDKIIVLDHGKIIEQGSHDEL 695
BtuD COG4138
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ...
 37-238 1.11e-21

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


Pssm-ID: 443313 [Multi-domain]  Cd Length: 248  Bit Score: 92.60  E-value: 1.11e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  37 VSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIqPTGGRIVIGSRDVTHVPP---AQRDIGLVFQSYALFpNMTVAGN 113
Cdd:COG4138   12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAaelARHRAYLSQQQSPPF-AMPVFQY 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 114 IAFSLAvRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALV-------FGPKLLLLDEPL------- 179
Cdd:COG4138   90 LALHQP-AGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLqvwptinPEGQLLLLDEPMnsldvaq 168

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 180 -AALDRKLREEVRlelrrlqgtLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGE 238
Cdd:COG4138  169 qAALDRLLRELCQ---------QGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAE 219
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
 15-239 3.57e-21

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 94.89  E-value: 3.57e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  15 PVSRRPAIEVSGLSKHF--GTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQ 92
Cdd:PRK11160 332 AAADQVSLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAA 411

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  93 -RD-IGLVFQSYALFpNMTVAGNIAfsLAVRGISrrdaKERVEWAIELVRLNGL-EHRKP---------SQLSGGQQQRV 160
Cdd:PRK11160 412 lRQaISVVSQRVHLF-SATLRDNLL--LAAPNAS----DEALIEVLQQVGLEKLlEDDKGlnawlgeggRQLSGGEQRRL 484

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 914601027 161 AIARALVFGPKLLLLDEPLAALDRKLREEVrLELRRlQGTLGVTTVLVTHdQDEAMSMSDRIAVLAQGVIQQLGSPGEL 239
Cdd:PRK11160 485 GIARALLHDAPLLLLDEPTEGLDAETERQI-LELLA-EHAQNKTVLMITH-RLTGLEQFDRICVMDNGQIIEQGTHQEL 560
SufC COG0396
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ...
 39-239 3.85e-21

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


Pssm-ID: 440165 [Multi-domain]  Cd Length: 245  Bit Score: 91.28  E-value: 3.85e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  39 DVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLI--QPTGGRIVIGSRDVTHVPP---AQRDIGLVFQSYALFPNMTVAG- 112
Cdd:COG0396   18 GVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDILELSPderARAGIFLAFQYPVEIPGVSVSNf 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 113 -NIAFSlAVRG--ISRRDAKERVEWAIELVRLNglehrkPSQL--------SGGQQQRVAIARALVFGPKLLLLDEPLAA 181
Cdd:COG0396   98 lRTALN-ARRGeeLSAREFLKLLKEKMKELGLD------EDFLdryvnegfSGGEKKRNEILQMLLLEPKLAILDETDSG 170

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 914601027 182 LD----RKLREEVRlELRrlqgTLGVTTVLVTH-----DQDEAmsmsDRIAVLAQGVIQQLGSPgEL 239
Cdd:COG0396  171 LDidalRIVAEGVN-KLR----SPDRGILIITHyqrilDYIKP----DFVHVLVDGRIVKSGGK-EL 227
GguA NF040905
sugar ABC transporter ATP-binding protein;
23-228 5.57e-21

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 94.09  E-value: 5.57e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  23 EVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGlIQPTG---GRIVI--------GSRDVTHvppa 91
Cdd:NF040905   3 EMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG-VYPHGsyeGEILFdgevcrfkDIRDSEA---- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  92 qRDIGLVFQSYALFPNMTVAGNIaF---SLAVRG-ISRRDAKERvewAIELVRLNGLE---HRKPSQLSGGQQQRVAIAR 164
Cdd:NF040905  78 -LGIVIIHQELALIPYLSIAENI-FlgnERAKRGvIDWNETNRR---ARELLAKVGLDespDTLVTDIGVGKQQLVEIAK 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 914601027 165 ALVFGPKLLLLDEPLAALD----RKLREEVrLELRRlQgtlGVTTVLVTHDQDEAMSMSDRIAVLAQG 228
Cdd:NF040905 153 ALSKDVKLLILDEPTAALNeedsAALLDLL-LELKA-Q---GITSIIISHKLNEIRRVADSITVLRDG 215
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
20-228 9.60e-21

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 93.44  E-value: 9.60e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  20 PAIEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRdvTHVPPAQRD----- 94
Cdd:PRK11288   3 PYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQ--EMRFASTTAalaag 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  95 IGLVFQSYALFPNMTVAGNIAF-SLAVRG--ISRRDAKERVewAIELVRLnGLE---HRKPSQLSGGQQQRVAIARALVF 168
Cdd:PRK11288  81 VAIIYQELHLVPEMTVAENLYLgQLPHKGgiVNRRLLNYEA--REQLEHL-GVDidpDTPLKYLSIGQRQMVEIAKALAR 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 914601027 169 GPKLLLLDEPLAALDRklREEVRL-----ELRRlQGTLgvtTVLVTHDQDEAMSMSDRIAVLAQG 228
Cdd:PRK11288 158 NARVIAFDEPTSSLSA--REIEQLfrvirELRA-EGRV---ILYVSHRMEEIFALCDAITVFKDG 216
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
19-246 1.49e-20

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 91.72  E-value: 1.49e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  19 RPAIEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLlGLVAGLIQPTGGR-------IVIGSRDVTHVPPA 91
Cdd:NF000106  11 RNAVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RG-ALPAHV*GPDAGRrpwrf*tWCANRRALRRTIG* 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  92 QRDIGL-VFQSYALFPNMTVAGNIAfslavrGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGP 170
Cdd:NF000106  90 HRPVR*gRRESFSGRENLYMIGR*L------DLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRP 163

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 914601027 171 KLLLLDEPLAALDRKLREEVRLELRRLQGTlGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELYRQPANR 246
Cdd:NF000106 164 AVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVGGR 238
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
 39-242 1.62e-20

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: 88.35  E-value: 1.62e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  39 DVDLTVAEGEFLSILGPSGSGKSTLLGLVAGL--IQPTGGRIVIGSRDVTHVPP---AQRDIGLVFQSYALFPNMTVAgn 113
Cdd:cd03217   18 GVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPeerARLGIFLAFQYPPEIPGVKNA-- 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 114 iafslavrgisrrdakervewaiELVR-LN-GlehrkpsqLSGGQQQRVAIARALVFGPKLLLLDEPLAALD---RKLRE 188
Cdd:cd03217   96 -----------------------DFLRyVNeG--------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDidaLRLVA 144

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 914601027 189 EVRLELRRlqgtLGVTTVLVTHDQDEAMSM-SDRIAVLAQGVIQQLGSPgELYRQ 242
Cdd:cd03217  145 EVINKLRE----EGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDK-ELALE 194
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
 35-254 3.28e-20

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 92.08  E-value: 3.28e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  35 CAVSDVDLTVAEGEFLSILGPSGSGKS-TLLGLVAGLIQP----TGGRIVIGSRDVTHVPPAQ------RDIGLVFQS-- 101
Cdd:PRK15134  23 TVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQTlrgvrgNKIAMIFQEpm 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 102 YALFPNMTVAGNIAFSLAV-RGISRRDAKERVEWAIELV-------RLNGLEHrkpsQLSGGQQQRVAIARALVFGPKLL 173
Cdd:PRK15134 103 VSLNPLHTLEKQLYEVLSLhRGMRREAARGEILNCLDRVgirqaakRLTDYPH----QLSGGERQRVMIAMALLTRPELL 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 174 LLDEPLAALDRKLREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELYRQPANRFVAGFLG 253
Cdd:PRK15134 179 IADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPTHPYTQKLLN 258


                 .
gi 914601027 254 A 254
Cdd:PRK15134 259 S 259
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
 22-245 3.92e-20

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 91.60  E-value: 3.92e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  22 IEVSGLSkhfGTvcAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQ--------- 92
Cdd:PRK10762 258 LKVDNLS---GP--GVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDglangivyi 332

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  93 -----RDiGLVFqSYALFPNMTVAGNIAFSLAVRGISRRDAKERVEWAIELVRLnglehRKPSQ------LSGGQQQRVA 161
Cdd:PRK10762 333 sedrkRD-GLVL-GMSVKENMSLTALRYFSRAGGSLKHADEQQAVSDFIRLFNI-----KTPSMeqaiglLSGGNQQKVA 405

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 162 IARALVFGPKLLLLDEPLAALDRKLREEVRLELRRLQGTlGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQqlgspGELYR 241
Cdd:PRK10762 406 IARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGRIS-----GEFTR 479


                 ....
gi 914601027 242 QPAN 245
Cdd:PRK10762 480 EQAT 483
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
36-243 3.93e-20

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


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 91.70  E-value: 3.93e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  36 AVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVppaQRD-----IGLVFQSYALFPNmTV 110
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKL---QLDswrsrLAVVSQTPFLFSD-TV 405

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 111 AGNIAfslavrgISRRDA-KERVEWAIELVRLNGLEHRKPS-----------QLSGGQQQRVAIARALVFGPKLLLLDEP 178
Cdd:PRK10789 406 ANNIA-------LGRPDAtQQEIEHVARLASVHDDILRLPQgydtevgergvMLSGGQKQRISIARALLLNAEILILDDA 478

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 914601027 179 LAALDRKLREEVRLELRRL-QGtlgvTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELYRQP 243
Cdd:PRK10789 479 LSAVDGRTEHQILHNLRQWgEG----RTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQS 540
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
 46-245 7.09e-20

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


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 91.26  E-value: 7.09e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   46 EGEFLSILGPSGSGKSTLLGLVAGLIqpTGGRIVIGSRDVTHVP---PAQRDI-GLVFQSYALFPNMTVAGNIAFSLAVR 121
Cdd:TIGR00955  50 PGELLAVMGSSGAGKTTLMNALAFRS--PKGVKGSGSVLLNGMPidaKEMRAIsAYVQQDDLFIPTLTVREHLMFQAHLR 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  122 ---GISRRDAKERVEWAIELVRLN-------GLEHRKPSqLSGGQQQRVAIARALVFGPKLLLLDEPLAALDRKLREEVR 191
Cdd:TIGR00955 128 mprRVTKKEKRERVDEVLQALGLRkcantriGVPGRVKG-LSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVV 206

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 914601027  192 LELRRLqGTLGVTTVLVTHD-QDEAMSMSDRIAVLAQGVIQQLGSPGEL--------YRQPAN 245
Cdd:TIGR00955 207 QVLKGL-AQKGKTIICTIHQpSSELFELFDKIILMAEGRVAYLGSPDQAvpffsdlgHPCPEN 268
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
2-233 8.78e-20

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 90.61  E-value: 8.78e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   2 ISHQLTSERDTLAPVSRRPAIEVSGL-SKHFGTVcavSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVI 80
Cdd:PRK09700 246 LQNRFNAMKENVSNLAHETVFEVRNVtSRDRKKV---RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRL 322

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  81 GSRDVTHVPP---AQRDIGLVFQSY---ALFPNMTVAGNIAFSLAVRG---------ISRRDAKERVEWAIELVRLNGLE 145
Cdd:PRK09700 323 NGKDISPRSPldaVKKGMAYITESRrdnGFFPNFSIAQNMAISRSLKDggykgamglFHEVDEQRTAENQRELLALKCHS 402

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 146 -HRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAALDRKLREEVRLELRRLQGTlGVTTVLVTHDQDEAMSMSDRIAV 224
Cdd:PRK09700 403 vNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAV 481


                 ....*....
gi 914601027 225 LAQGVIQQL 233
Cdd:PRK09700 482 FCEGRLTQI 490
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
 38-245 9.53e-20

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 90.50  E-value: 9.53e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  38 SDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQR-DIGLVF-----QSYALFPNMTVA 111
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRlARGLVYlpedrQSSGLYLDAPLA 359

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 112 GNIAfSLAV--RGISRRDAK-----ERVEWAIElVRLNGLEhRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAALDR 184
Cdd:PRK15439 360 WNVC-ALTHnrRGFWIKPARenavlERYRRALN-IKFNHAE-QAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDV 436

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 914601027 185 KLREEVRLELRRLQGTlGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQqlgspGELYRQPAN 245
Cdd:PRK15439 437 SARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEIS-----GALTGAAIN 491
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
 37-257 1.06e-19

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 87.45  E-value: 1.06e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  37 VSDVDLTVAEGEFLSILGPSGSGKS----TLLGLVAGLIQPTGGRIVIgsrDVTHVPPAQ---RDIGLVFQS--YALFPN 107
Cdd:PRK10418  19 VHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLL---DGKPVAPCAlrgRKIATIMQNprSAFNPL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 108 MTVAGNIAFSLAVRGISRRDAkeRVEWAIELVrlnGLEHRK------PSQLSGGQQQRVAIARALVFGPKLLLLDEPLAA 181
Cdd:PRK10418  96 HTMHTHARETCLALGKPADDA--TLTAALEAV---GLENAArvlklyPFEMSGGMLQRMMIALALLCEAPFIIADEPTTD 170

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 914601027 182 LDRKLREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELYRQPANRfVAGFLGAANL 257
Cdd:PRK10418 171 LDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHA-VTRSLVSAHL 245
PLN03211 PLN03211
ABC transporter G-25; Provisional
 47-228 1.71e-19

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 89.94  E-value: 1.71e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  47 GEFLSILGPSGSGKSTLLGLVAGLIQPTG--GRIVIGSRDVTHvpPAQRDIGLVFQSYALFPNMTVAGNIAFSLAVR--- 121
Cdd:PLN03211  94 GEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTK--QILKRTGFVTQDDILYPHLTVRETLVFCSLLRlpk 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 122 GISRRDAKERVEWAIELVRLNGLEHRKPSQ-----LSGGQQQRVAIARALVFGPKLLLLDEPLAALDRKLREEVRLELRR 196
Cdd:PLN03211 172 SLTKQEKILVAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGS 251

                        170       180       190
                 ....*....|....*....|....*....|...
gi 914601027 197 LQGTlGVTTVLVTHD-QDEAMSMSDRIAVLAQG 228
Cdd:PLN03211 252 LAQK-GKTIVTSMHQpSSRVYQMFDSVLVLSEG 283
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
27-239 1.81e-19

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 86.96  E-value: 1.81e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  27 LSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQ--RDIGLVFQsyal 104
Cdd:PRK10253  13 LTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvaRRIGLLAQ---- 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 105 fpNMTVAGNIAFS-LAVRGIS---------RRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLL 174
Cdd:PRK10253  89 --NATTPGDITVQeLVARGRYphqplftrwRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIML 166

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 914601027 175 LDEPLAALDRKLREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGEL 239
Cdd:PRK10253 167 LDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
 22-227 2.20e-19

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 86.32  E-value: 2.20e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  22 IEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIvigsrdvthVPPAQRDIGLVFQS 101
Cdd:PRK09544   5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI---------KRNGKLRIGYVPQK 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 102 YALFPNM--TVAGNIAFSLAVRGISRRDAKERVEwAIELvrlngleHRKPSQ-LSGGQQQRVAIARALVFGPKLLLLDEP 178
Cdd:PRK09544  76 LYLDTTLplTVNRFLRLRPGTKKEDILPALKRVQ-AGHL-------IDAPMQkLSGGETQRVLLARALLNRPQLLVLDEP 147

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 914601027 179 LAALDRKLREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQ 227
Cdd:PRK09544 148 TQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH 196
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
36-242 2.29e-19

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 89.69  E-value: 2.29e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  36 AVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTH--VPPAQRDIGLVFQSYALFpNMTVAGN 113
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDytLASLRNQVALVSQNVHLF-NDTIANN 436

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 114 IAFSlAVRGISRRDAKERVEWAIELVRLNGLEH-------RKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAALDRKL 186
Cdd:PRK11176 437 IAYA-RTEQYSREQIEEAARMAYAMDFINKMDNgldtvigENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTES 515

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 914601027 187 REEVRLELRRLQGTlgvTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELYRQ 242
Cdd:PRK11176 516 ERAIQAALDELQKN---RTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQ 568
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
42-243 3.08e-19

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 86.38  E-value: 3.08e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  42 LTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVT--HVPPAQRDIGLVFQSYALFPNMTVAGNIAF--- 116
Cdd:PRK10575  32 LTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLEswSSKAFARKVAYLPQQLPAAEGMTVRELVAIgry 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 117 ----SLAVRGISRRdakERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAALDRKLREEVRL 192
Cdd:PRK10575 112 pwhgALGRFGAADR---EKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLA 188

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 914601027 193 ELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELYRQP 243
Cdd:PRK10575 189 LVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGE 239
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
 43-243 6.15e-19

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 84.98  E-value: 6.15e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  43 TVAEGEFLSILGPSGSGKSTLLGLVAGLIqPTGGRIVIGSRDVTHVPP---AQRDIGLVFQSYALFpNMTVAGNIAFSLA 119
Cdd:PRK03695  18 EVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAaelARHRAYLSQQQTPPF-AMPVFQYLTLHQP 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 120 VrGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARAL-----VFGP--KLLLLDEPLAALDrkLREEVRL 192
Cdd:PRK03695  96 D-KTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqvwpDINPagQLLLLDEPMNSLD--VAQQAAL 172

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 914601027 193 E--LRRLQGtLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELYRQP 243
Cdd:PRK03695 173 DrlLSELCQ-QGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPE 224
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
 20-228 3.65e-18

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 85.83  E-value: 3.65e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  20 PAIEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQRD---IG 96
Cdd:PRK10762   3 ALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQeagIG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  97 LVFQSYALFPNMTVAGNIAFSLA-VRGISRRDAKERVEWAIELV-RLNgLEH---RKPSQLSGGQQQRVAIARALVFGPK 171
Cdd:PRK10762  83 IIHQELNLIPQLTIAENIFLGREfVNRFGRIDWKKMYAEADKLLaRLN-LRFssdKLVGELSIGEQQMVEIAKVLSFESK 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 914601027 172 LLLLDEPLAALD-----------RKLREEvrlelrrlqgtlGVTTVLVTHDQDEAMSMSDRIAVLAQG 228
Cdd:PRK10762 162 VIIMDEPTDALTdteteslfrviRELKSQ------------GRGIVYISHRLKEIFEICDDVTVFRDG 217
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
 43-249 7.19e-18

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: 82.07  E-value: 7.19e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  43 TVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPpaqrdiglvfQSYALFPNMTVAgniAFslaVRG 122
Cdd:cd03237   21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKP----------QYIKADYEGTVR---DL---LSS 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 123 ISRrDAKERVEWAIELVR---LNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAALDRKLREEVRLELRRLQG 199
Cdd:cd03237   85 ITK-DFYTHPYFKTEIAKplqIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAE 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 914601027 200 TLGVTTVLVTHDQDEAMSMSDRIAVL-AQGVIQQLGSPGELYRQPANRFVA 249
Cdd:cd03237  164 NNEKTAFVVEHDIIMIDYLADRLIVFeGEPSVNGVANPPQSLRSGMNRFLK 214
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
20-242 1.05e-17

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 84.79  E-value: 1.05e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  20 PAIEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRI-----VIGSRDVThvppAQRD 94
Cdd:NF033858 265 PAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAwlfgqPVDAGDIA----TRRR 340

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  95 IGLVFQSYALFPNMTVAGNIAfsLAVR--GISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKL 172
Cdd:NF033858 341 VGYMSQAFSLYGELTVRQNLE--LHARlfHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPEL 418

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 914601027 173 LLLDEPLAALDRKLRE---EVRLELRRLQgtlGVTTVLVTHDQDEAMSmSDRIA------VLAQgviqqlGSPGELYRQ 242
Cdd:NF033858 419 LILDEPTSGVDPVARDmfwRLLIELSRED---GVTIFISTHFMNEAER-CDRISlmhagrVLAS------DTPAALVAA 487
PTZ00243 PTZ00243
ABC transporter; Provisional
 39-243 1.54e-17

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 84.45  E-value: 1.54e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   39 DVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVigsrdvthvppAQRDIGLVFQSyALFPNMTVAGNIAFSL 118
Cdd:PTZ00243  678 DVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW-----------AERSIAYVPQQ-AWIMNATVRGNILFFD 745

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  119 AVRGISRRDAKERVEWAIELVRLN-GLEHR---KPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAALDRKLREEVRLEL 194
Cdd:PTZ00243  746 EEDAARLADAVRVSQLEADLAQLGgGLETEigeKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEEC 825

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 914601027  195 rrLQGTL-GVTTVLVTHdQDEAMSMSDRIAVLAQGVIQQLGSPGELYRQP 243
Cdd:PTZ00243  826 --FLGALaGKTRVLATH-QVHVVPRADYVVALGDGRVEFSGSSADFMRTS 872
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
 37-210 1.65e-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: 79.12  E-value: 1.65e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  37 VSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVI-GSRDVTHVPpaQRdiglvfqSYalFPNMTVAGNIA 115
Cdd:cd03223   17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMpEGEDLLFLP--QR-------PY--LPLGTLREQLI 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 116 FSlavrgisrrdakerveWAIELvrlnglehrkpsqlSGGQQQRVAIARALVFGPKLLLLDEPLAALDrklrEEVRLELR 195
Cdd:cd03223   86 YP----------------WDDVL--------------SGGEQQRLAFARLLLHKPKFVFLDEATSALD----EESEDRLY 131

                        170
                 ....*....|....*
gi 914601027 196 RLQGTLGVTTVLVTH 210
Cdd:cd03223  132 QLLKELGITVISVGH 146
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
 37-220 2.09e-17

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127 [Multi-domain]  Cd Length: 200  Bit Score: 79.61  E-value: 2.09e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  37 VSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPA-QRDIGLVFQSYALFPNMTVAGN-- 113
Cdd:PRK13540  17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTyQKQLCFVGHRSGINPYLTLRENcl 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 114 --IAFSLAVRGISrrdakervewaiELVRLNGLEHR---KPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAALDRKLRE 188
Cdd:PRK13540  97 ydIHFSPGAVGIT------------ELCRLFSLEHLidyPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLL 164

                        170       180       190
                 ....*....|....*....|....*....|....
gi 914601027 189 EV--RLELRRLQGtlgvTTVLVTHDQDEAMSMSD 220
Cdd:PRK13540 165 TIitKIQEHRAKG----GAVLLTSHQDLPLNKAD 194
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
 39-213 3.70e-17

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


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 79.62  E-value: 3.70e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  39 DVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLI--QPTGGRIVIGSRDVThvppaqrdiglvfqsyalfPNMTVAGNIAf 116
Cdd:COG2401   48 DLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQFG-------------------REASLIDAIG- 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 117 slavrgiSRRDAKERVEwAIELVRLNG--LEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAALDRKLREEVRLEL 194
Cdd:COG2401  108 -------RKGDFKDAVE-LLNAVGLSDavLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNL 179

                        170
                 ....*....|....*....
gi 914601027 195 RRLQGTLGVTTVLVTHDQD 213
Cdd:COG2401  180 QKLARRAGITLVVATHHYD 198
PRK15093 PRK15093
peptide ABC transporter ATP-binding protein SapD;
20-243 5.45e-17

peptide ABC transporter ATP-binding protein SapD;


Pssm-ID: 185049 [Multi-domain]  Cd Length: 330  Bit Score: 81.00  E-value: 5.45e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  20 PAIEVSGLSKHF----GTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGL----IQPTGGRIVIGSRDVTHVPPA 91
Cdd:PRK15093   2 PLLDIRNLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVtkdnWRVTADRMRFDDIDLLRLSPR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  92 QR------DIGLVFQ--SYALFPNMTVAGNIafslaVRGISRRDAK----ERVEW----AIELVRLNGLEHRK------P 149
Cdd:PRK15093  82 ERrklvghNVSMIFQepQSCLDPSERVGRQL-----MQNIPGWTYKgrwwQRFGWrkrrAIELLHRVGIKDHKdamrsfP 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 150 SQLSGGQQQRVAIARALVFGPKLLLLDEPLAALDRKLREEVRLELRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGV 229
Cdd:PRK15093 157 YELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQ 236

                        250
                 ....*....|....
gi 914601027 230 IQQLGSPGELYRQP 243
Cdd:PRK15093 237 TVETAPSKELVTTP 250
hmuV PRK13547
heme ABC transporter ATP-binding protein;
39-241 5.49e-17

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 80.26  E-value: 5.49e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  39 DVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLI---QPTGGRIVIGSRDVTHVPPAQRDIGLVFQSYALFPNmtvAGNIA 115
Cdd:PRK13547  19 DLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtggGAPRGARVTGDVTLNGEPLAAIDAPRLARLRAVLPQ---AAQPA 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 116 FSLAVRGI---------------SRRDaKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARAL---------VFGPK 171
Cdd:PRK13547  96 FAFSAREIvllgrypharragalTHRD-GEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQPPR 174

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 914601027 172 LLLLDEPLAALD----RKLREEVRLELRRLQgtLGVTTVLvtHDQDEAMSMSDRIAVLAQGVIQQLGSPGELYR 241
Cdd:PRK13547 175 YLLLDEPTAALDlahqHRLLDTVRRLARDWN--LGVLAIV--HDPNLAARHADRIAMLADGAIVAHGAPADVLT 244
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
 22-183 1.43e-16

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: 81.13  E-value: 1.43e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   22 IEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSrdvthvppaQRDIGLVFQS 101
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGE---------TVKLAYVDQS 393

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  102 Y-ALFPNMTVAGNIAFSLAVRGISRRDAKERVewaiELVRLN---GLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDE 177
Cdd:TIGR03719 394 RdALDPNKTVWEEISGGLDIIKLGKREIPSRA----YVGRFNfkgSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDE 469


                  ....*.
gi 914601027  178 PLAALD 183
Cdd:TIGR03719 470 PTNDLD 475
PRK10522 PRK10522
multidrug transporter membrane component/ATP-binding component; Provisional
 36-233 1.63e-16

multidrug transporter membrane component/ATP-binding component; Provisional


Pssm-ID: 236707 [Multi-domain]  Cd Length: 547  Bit Score: 80.79  E-value: 1.63e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  36 AVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPA--QRDIGLVFQSYALFPN-MTVAG 112
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEdyRKLFSAVFTDFHLFDQlLGPEG 417

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 113 NIAFSLAVRG-ISRRDAKERVEwaIELVRLNGLehrkpsQLSGGQQQRVAIARALVFGPKLLLLDEPLAALDRKLREEVR 191
Cdd:PRK10522 418 KPANPALVEKwLERLKMAHKLE--LEDGRISNL------KLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFY 489

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 914601027 192 LELRRLQGTLGVTTVLVTHDqDEAMSMSDRIAVLAQGVIQQL 233
Cdd:PRK10522 490 QVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQLSEL 530
PLN03130 PLN03130
ABC transporter C family member; Provisional
 38-239 2.41e-16

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 80.94  E-value: 2.41e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   38 SDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPpaqrDIGLVFqsyalfpNMTVAGNIAFS 117
Cdd:PLN03130  634 SNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVVIRGTVAYVP----QVSWIF-------NATVRDNILFG 702

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  118 lavrgiSRRDAkERVEWAIelvRLNGLEH--------------RKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAALD 183
Cdd:PLN03130  703 ------SPFDP-ERYERAI---DVTALQHdldllpggdlteigERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 914601027  184 RKLREEV-----RLELRrlqgtlGVTTVLVThDQDEAMSMSDRIAVLAQGVIQQLGSPGEL 239
Cdd:PLN03130  773 AHVGRQVfdkciKDELR------GKTRVLVT-NQLHFLSQVDRIILVHEGMIKEEGTYEEL 826
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
 36-235 1.63e-15

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: 78.52  E-value: 1.63e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027    36 AVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDV-THVPPAQRDIGLVFQSYALFPNMTVAGNI 114
Cdd:TIGR01257 1954 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTNISDVHQNMGYCPQFDAIDDLLTGREHL 2033

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   115 AFSLAVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAALDRKLReevRLEL 194
Cdd:TIGR01257 2034 YLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQAR---RMLW 2110

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 914601027   195 RRLQGTL--GVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGS 235
Cdd:TIGR01257 2111 NTIVSIIreGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGT 2153
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
21-178 1.73e-15

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 78.24  E-value: 1.73e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  21 AIEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGL--IQpTGGRIVIGS--RDVTHVPPAQRDI- 95
Cdd:NF033858   1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGArkIQ-QGRVEVLGGdmADARHRRAVCPRIa 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  96 ----GLvfqSYALFPNMTVAGNIAFSLAVRGISRRDAKERVEwaiELVRLNGLE---HRKPSQLSGGQQQRVAIARALVF 168
Cdd:NF033858  80 ympqGL---GKNLYPTLSVFENLDFFGRLFGQDAAERRRRID---ELLRATGLApfaDRPAGKLSGGMKQKLGLCCALIH 153

                        170
                 ....*....|
gi 914601027 169 GPKLLLLDEP 178
Cdd:NF033858 154 DPDLLILDEP 163
PRK13543 PRK13543
heme ABC exporter ATP-binding protein CcmA;
11-183 2.36e-15

heme ABC exporter ATP-binding protein CcmA;


Pssm-ID: 184129 [Multi-domain]  Cd Length: 214  Bit Score: 74.11  E-value: 2.36e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  11 DTLAPVSRRPAIEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIgsrDVTHVPP 90
Cdd:PRK13543   1 MIEPLHTAPPLLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQI---DGKTATR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  91 AQRDIGLVFQSY--ALFPNMTVAGNIAFSLAVRGisrRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVF 168
Cdd:PRK13543  78 GDRSRFMAYLGHlpGLKADLSTLENLHFLCGLHG---RRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLS 154

                        170
                 ....*....|....*
gi 914601027 169 GPKLLLLDEPLAALD 183
Cdd:PRK13543 155 PAPLWLLDEPYANLD 169
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
16-224 3.27e-15

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 76.77  E-value: 3.27e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  16 VSRRPAIEVSGLSKHFGtvcavsDVDLTV-----AEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIvigSRDVT---- 86
Cdd:PRK13409 335 SERETLVEYPDLTKKLG------DFSLEVeggeiYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV---DPELKisyk 405

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  87 --HVPPAQrdiglvfqsyalfpNMTVAGNIafslavrgisrRDAKERVE---WAIELVRLNGLEH---RKPSQLSGGQQQ 158
Cdd:PRK13409 406 pqYIKPDY--------------DGTVEDLL-----------RSITDDLGssyYKSEIIKPLQLERlldKNVKDLSGGELQ 460

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 914601027 159 RVAIARALVFGPKLLLLDEPLAALDRKLREEVRLELRRLQGTLGVTTVLVTHD---QDeamSMSDRIAV 224
Cdd:PRK13409 461 RVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDiymID---YISDRLMV 526
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
 22-210 4.01e-15

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 77.38  E-value: 4.01e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   22 IEVSGLSKHFGT---VCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGS----RDVtHVPPAQRD 94
Cdd:PTZ00265  383 IQFKNVRFHYDTrkdVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlKDI-NLKWWRSK 461

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   95 IGLVFQSYALFPNmTVAGNIAFSL------------------------AVRGISRRDAKERVEWAIELVRLNGLEHRK-- 148
Cdd:PTZ00265  462 IGVVSQDPLLFSN-SIKNNIKYSLyslkdlealsnyynedgndsqenkNKRNSCRAKCAGDLNDMSNTTDSNELIEMRkn 540

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  149 ------------------------------------PSQLSGGQQQRVAIARALVFGPKLLLLDEPLAALDRKLREEVRL 192
Cdd:PTZ00265  541 yqtikdsevvdvskkvlihdfvsalpdkyetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQK 620

                         250
                  ....*....|....*...
gi 914601027  193 ELRRLQGTLGVTTVLVTH 210
Cdd:PTZ00265  621 TINNLKGNENRITIIIAH 638
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
 40-239 1.32e-14

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: 75.75  E-value: 1.32e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027    40 VDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVI-GSrdVTHVPpaqrdiglvfqSYALFPNMTVAGNIAFSL 118
Cdd:TIGR00957  657 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMkGS--VAYVP-----------QQAWIQNDSLRENILFGK 723

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   119 AVRGISRRDAKERVEWAIELVRLNGLEH----RKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAALDRKLREEVRLEL 194
Cdd:TIGR00957  724 ALNEKYYQQVLEACALLPDLEILPSGDRteigEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHV 803

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 914601027   195 RRLQGTL-GVTTVLVTHDQdEAMSMSDRIAVLAQGVIQQLGSPGEL 239
Cdd:TIGR00957  804 IGPEGVLkNKTRILVTHGI-SYLPQVDVIIVMSGGKISEMGSYQEL 848
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
 39-242 2.41e-14

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: 74.98  E-value: 2.41e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027    39 DVDLTVAEGEFLSILGPSGSGKSTL-LGLVAgLIQPTGGRIVIGSRDVThvppaqrDIGL---------VFQSYALFpnm 108
Cdd:TIGR00957 1304 HINVTIHGGEKVGIVGRTGAGKSSLtLGLFR-INESAEGEIIIDGLNIA-------KIGLhdlrfkitiIPQDPVLF--- 1372

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   109 tvAGNIAFSLAVRGisrRDAKERVEWAIELVRLNGLEHRKPSQL-----------SGGQQQRVAIARALVFGPKLLLLDE 177
Cdd:TIGR00957 1373 --SGSLRMNLDPFS---QYSDEEVWWALELAHLKTFVSALPDKLdhecaeggenlSVGQRQLVCLARALLRKTKILVLDE 1447

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 914601027   178 PLAALDRKLREEVRLELRRLQGTLGVTTvlVTHDQDEAMSMSdRIAVLAQGVIQQLGSPGELYRQ 242
Cdd:TIGR00957 1448 ATAAVDLETDNLIQSTIRTQFEDCTVLT--IAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLLQQ 1509
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
38-233 2.81e-14

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


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 73.98  E-value: 2.81e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  38 SDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVT---------HVPPAQRDIglVFQSYALFPNM 108
Cdd:PRK10790 358 QNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSslshsvlrqGVAMVQQDP--VVLADTFLANV 435

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 109 TVAgniafslavRGISrrdaKERVEWAIELVRLNGLEHRKP-----------SQLSGGQQQRVAIARALVFGPKLLLLDE 177
Cdd:PRK10790 436 TLG---------RDIS----EEQVWQALETVQLAELARSLPdglytplgeqgNNLSVGQKQLLALARVLVQTPQILILDE 502

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 914601027 178 PLAALDRKLREEVRLELR--RLQGTLGVT-----------TVLVTHdqdeamsmsdRIAVLAQGVIQQL 233
Cdd:PRK10790 503 ATANIDSGTEQAIQQALAavREHTTLVVIahrlstiveadTILVLH----------RGQAVEQGTHQQL 561
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
38-245 3.11e-14

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 73.79  E-value: 3.11e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  38 SDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVI-GSRDVTHVPPAQRDIGLVF-----QSYALFPNMTVA 111
Cdd:PRK11288 270 EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLdGKPIDIRSPRDAIRAGIMLcpedrKAEGIIPVHSVA 349

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 112 GNIAFSlAVRGISR-----RDAKERvEWAIELVRLNGLEHRKPSQ----LSGGQQQRVAIARALVFGPKLLLLDEPLAAL 182
Cdd:PRK11288 350 DNINIS-ARRHHLRagcliNNRWEA-ENADRFIRSLNIKTPSREQlimnLSGGNQQKAILGRWLSEDMKVILLDEPTRGI 427

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 914601027 183 DRKLREEVRLELRRLQGTlGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQqlgspGELYRQPAN 245
Cdd:PRK11288 428 DVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRIA-----GELAREQAT 484
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
 43-257 3.35e-14

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: 71.63  E-value: 3.35e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  43 TVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIvigsrdvtHVPPAQRDI-----GLVFQSY--------------- 102
Cdd:cd03236   22 VPREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKF--------DDPPDWDEIldefrGSELQNYftkllegdvkvivkp 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 103 ---ALFPNmTVAGNIAFSLavrgiSRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPL 179
Cdd:cd03236   94 qyvDLIPK-AVKGKVGELL-----KKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPS 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 180 AALDRKLREEVRLELRRLqGTLGVTTVLVTHDQDEAMSMSDRIAVL-----AQGVIQQLGSpgelYRQPANRFVAGFLGA 254
Cdd:cd03236  168 SYLDIKQRLNAARLIREL-AEDDNYVLVVEHDLAVLDYLSDYIHCLygepgAYGVVTLPKS----VREGINEFLDGYLPT 242


                 ...
gi 914601027 255 ANL 257
Cdd:cd03236  243 ENM 245
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
 22-230 4.68e-14

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 73.45  E-value: 4.68e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  22 IEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIgSRDVThVPPAQRDiglvfqs 101
Cdd:PRK11147   4 ISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIY-EQDLI-VARLQQD------- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 102 yalfPNMTVAGN----IAFSLAVRG--------ISRRDAKERVEWAI-ELVRLNG-LEHR-------------------- 147
Cdd:PRK11147  75 ----PPRNVEGTvydfVAEGIEEQAeylkryhdISHLVETDPSEKNLnELAKLQEqLDHHnlwqlenrinevlaqlgldp 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 148 --KPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAALDRKLREEVRLELRRLQGTLgvttVLVTHDQDEAMSMSDRIAVL 225
Cdd:PRK11147 151 daALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSI----IFISHDRSFIRNMATRIVDL 226


                 ....*
gi 914601027 226 AQGVI 230
Cdd:PRK11147 227 DRGKL 231
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
 37-228 7.49e-14

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


Pssm-ID: 213200 [Multi-domain]  Cd Length: 202  Bit Score: 69.60  E-value: 7.49e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  37 VSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTG---GRIVIGSRDVTH-VPPAQRDIGLVFQSYALFPNMTVAG 112
Cdd:cd03233   23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNGIPYKEfAEKYPGEIIYVSEEDVHFPTLTVRE 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 113 NIAFSLAVRGIsrrdakervewaiELVRlnglehrkpsQLSGGQQQRVAIARALVFGPKLLLLDEPLAALDRKLREEVRL 192
Cdd:cd03233  103 TLDFALRCKGN-------------EFVR----------GISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILK 159

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 914601027 193 ELRRLQGTLGVTTVlVTHDQ--DEAMSMSDRIAVLAQG 228
Cdd:cd03233  160 CIRTMADVLKTTTF-VSLYQasDEIYDLFDKVLVLYEG 196
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 16-224 7.67e-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: 72.89  E-value: 7.67e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  16 VSRRPAIEVSGLSKHFGtvcavsDVDLTVA-----EGEFLSILGPSGSGKSTLLGLVAGLIQPTGGrIVIGSRDVTHVPp 90
Cdd:COG1245  336 KEEETLVEYPDLTKSYG------GFSLEVEggeirEGEVLGIVGPNGIGKTTFAKILAGVLKPDEG-EVDEDLKISYKP- 407

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  91 aQRdiglVFQSYalfpNMTVAGNIafslavrgisRRDAKERVE---WAIELVRLNGLEH---RKPSQLSGGQQQRVAIAR 164
Cdd:COG1245  408 -QY----ISPDY----DGTVEEFL----------RSANTDDFGssyYKTEIIKPLGLEKlldKNVKDLSGGELQRVAIAA 468

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 914601027 165 ALVFGPKLLLLDEPLAALDRKLREEVRLELRRLQGTLGVTTVLVTHD---QDeamSMSDRIAV 224
Cdd:COG1245  469 CLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDiylID---YISDRLMV 528
PLN03232 PLN03232
ABC transporter C family member; Provisional
 37-241 1.96e-13

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 71.93  E-value: 1.96e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   37 VSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPpaqrDIGLVFqsyalfpNMTVAGNIAF 116
Cdd:PLN03232  633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVVIRGSVAYVP----QVSWIF-------NATVRENILF 701

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  117 SlavrgisRRDAKERVEWAIELvrlNGLEH--------------RKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAAL 182
Cdd:PLN03232  702 G-------SDFESERYWRAIDV---TALQHdldllpgrdlteigERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSAL 771

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 914601027  183 DRKLREEV-----RLELRrlqgtlGVTTVLVThDQDEAMSMSDRIAVLAQGVIQQLGSPGELYR 241
Cdd:PLN03232  772 DAHVAHQVfdscmKDELK------GKTRVLVT-NQLHFLPLMDRIILVSEGMIKEEGTFAELSK 828
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
 22-236 2.32e-13

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: 68.21  E-value: 2.32e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  22 IEVSGLSKHFGTVC--AVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVP--PAQRDIGL 97
Cdd:cd03369    7 IEVENLSVRYAPDLppVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPleDLRSSLTI 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  98 VFQSYALFpnmtvAGNIAFSLAVRGisrRDAKERVEWAIElVRLNGLehrkpsQLSGGQQQRVAIARALVFGPKLLLLDE 177
Cdd:cd03369   87 IPQDPTLF-----SGTIRSNLDPFD---EYSDEEIYGALR-VSEGGL------NLSQGQRQLLCLARALLKRPRVLVLDE 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 914601027 178 PLAAL----DRKLREEVRLELRRlqgtlgvTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSP 236
Cdd:cd03369  152 ATASIdyatDALIQKTIREEFTN-------STILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
36-211 3.30e-13

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 69.14  E-value: 3.30e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  36 AVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPpAQRDIGLVFQSYAL---FP----NM 108
Cdd:PRK15056  22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQAL-QKNLVAYVPQSEEVdwsFPvlveDV 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 109 TVAGNIAFSLAVRGISRRDaKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAALDRKLRE 188
Cdd:PRK15056 101 VMMGRYGHMGWLRRAKKRD-RQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEA 179

                        170       180
                 ....*....|....*....|...
gi 914601027 189 EVRLELRRLQGTlGVTTVLVTHD 211
Cdd:PRK15056 180 RIISLLRELRDE-GKTMLVSTHN 201
ABCG_PDR_domain2 cd03232
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...
 47-228 4.09e-13

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: 67.27  E-value: 4.09e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  47 GEFLSILGPSGSGKSTLLGLVA-----GLIqptGGRIVIGSRDVThvPPAQRDIGLVFQSYALFPNMTVAGNIAFSLAVR 121
Cdd:cd03232   33 GTLTALMGESGAGKTTLLDVLAgrktaGVI---TGEILINGRPLD--KNFQRSTGYVEQQDVHSPNLTVREALRFSALLR 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 122 GISrrdakervewaielvrlngLEHRKpsqlsggqqqRVAIARALVFGPKLLLLDEPLAALDRKLREEVRLELRRL--QG 199
Cdd:cd03232  108 GLS-------------------VEQRK----------RLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLadSG 158

                        170       180       190
                 ....*....|....*....|....*....|.
gi 914601027 200 tlgvTTVLVTHDQDEA--MSMSDRIAVLAQG 228
Cdd:cd03232  159 ----QAILCTIHQPSAsiFEKFDRLLLLKRG 185
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
 39-211 5.16e-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: 69.96  E-value: 5.16e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   39 DVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVigsrdvthvPPAQRDIGLVFQSYALFPNMTVAGNIAFSL 118
Cdd:TIGR03719  23 DISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEAR---------PQPGIKVGYLPQEPQLDPTKTVRENVEEGV 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  119 A--VRGISRRDA------------------KERVEWAIELVRLNGLEHR---------------KPSQLSGGQQQRVAIA 163
Cdd:TIGR03719  94 AeiKDALDRFNEisakyaepdadfdklaaeQAELQEIIDAADAWDLDSQleiamdalrcppwdaDVTKLSGGERRRVALC 173

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 914601027  164 RALVFGPKLLLLDEPLAALDrklREEVR-LE--LRRLQGTLgvttVLVTHD 211
Cdd:TIGR03719 174 RLLLSKPDMLLLDEPTNHLD---AESVAwLErhLQEYPGTV----VAVTHD 217
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
 19-235 5.39e-13

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 69.92  E-value: 5.39e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  19 RPAIEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSrdvthvppaQRDIGLV 98
Cdd:PRK15064 317 RNALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSE---------NANIGYY 387

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  99 FQ-SYALFPN-MTVAGNIAF-------SLAVRGIsrrdakervewaieLVRL--NGLEHRKPSQ-LSGGQQQRvaiaraL 166
Cdd:PRK15064 388 AQdHAYDFENdLTLFDWMSQwrqegddEQAVRGT--------------LGRLlfSQDDIKKSVKvLSGGEKGR------M 447

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 914601027 167 VFG------PKLLLLDEPLAALDRKLREEVRLELRRLQGTLgvttVLVTHDQDEAMSMSDRI-AVLAQGVIQQLGS 235
Cdd:PRK15064 448 LFGklmmqkPNVLVMDEPTNHMDMESIESLNMALEKYEGTL----IFVSHDREFVSSLATRIiEITPDGVVDFSGT 519
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
 37-231 1.09e-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: 69.08  E-value: 1.09e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   37 VSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPT-GGRIVIGSRDVTHVPPAQ---RDIGLVFQS---YALFPNMT 109
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNPAQairAGIAMVPEDrkrHGIVPILG 355

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  110 VAGNIAFSLAVR--GISRRDAKERVEWAIELVRLNGLEHRKP----SQLSGGQQQRVAIARALVFGPKLLLLDEPLAALD 183
Cdd:TIGR02633 356 VGKNITLSVLKSfcFKMRIDAAAELQIIGSAIQRLKVKTASPflpiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVD 435

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 914601027  184 RKlreeVRLELRRLQGTL---GVTTVLVTHDQDEAMSMSDRIAVLAQGVIQ 231
Cdd:TIGR02633 436 VG----AKYEIYKLINQLaqeGVAIIVVSSELAEVLGLSDRVLVIGEGKLK 482
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 47-224 1.11e-12

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: 65.09  E-value: 1.11e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027    47 GEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIgsrdvthvppaqrdiglvfqsyalfpnmtVAGniafslavrgisrr 126
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIY-----------------------------IDG-------------- 38

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   127 dakERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAALDRKLREEVRLELRRLQGTL----- 201
Cdd:smart00382  39 ---EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLlksek 115

                          170       180
                   ....*....|....*....|...
gi 914601027   202 GVTTVLVTHDQDEAMSMSDRIAV 224
Cdd:smart00382 116 NLTVILTTNDEKDLGPALLRRRF 138
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
 22-183 1.33e-12

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 68.99  E-value: 1.33e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  22 IEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSrDVthvppaqrDIGLVFQS 101
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGE-TV--------KLAYVDQS 395

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 102 Y-ALFPNMTVAGNIAFSLAVRGISRRDAKERVEWAielvRLN--GLEHRKP-SQLSGGQQQRVAIARALVFGPKLLLLDE 177
Cdd:PRK11819 396 RdALDPNKTVWEEISGGLDIIKVGNREIPSRAYVG----RFNfkGGDQQKKvGVLSGGERNRLHLAKTLKQGGNVLLLDE 471


                 ....*.
gi 914601027 178 PLAALD 183
Cdd:PRK11819 472 PTNDLD 477
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
 37-231 2.48e-12

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 68.03  E-value: 2.48e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  37 VSDVDLTVAEGEFLSILGPSGSGK----STLLGLVAGLIQptgGRIVIGSRDVTHVPPAQ---RDIGLVFQS---YALFP 106
Cdd:PRK13549 278 VDDVSFSLRRGEILGIAGLVGAGRtelvQCLFGAYPGRWE---GEIFIDGKPVKIRNPQQaiaQGIAMVPEDrkrDGIVP 354

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 107 NMTVAGNIAFSlAVRGISRR----DAKERVEWAIELVRLnglEHRKPS------QLSGGQQQRVAIARALVFGPKLLLLD 176
Cdd:PRK13549 355 VMGVGKNITLA-ALDRFTGGsridDAAELKTILESIQRL---KVKTASpelaiaRLSGGNQQKAVLAKCLLLNPKILILD 430

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 177 EPLAALDrklreeV--RLELRRLQGTL---GVTTVLVTHDQDEAMSMSDRIAVLAQGVIQ 231
Cdd:PRK13549 431 EPTRGID------VgaKYEIYKLINQLvqqGVAIIVISSELPEVLGLSDRVLVMHEGKLK 484
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
 37-210 8.21e-12

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: 64.27  E-value: 8.21e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  37 VSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPAQRDIGLVFQ-SYA----LFPNMTVA 111
Cdd:cd03290   17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSvAYAaqkpWLLNATVE 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 112 GNIAFSLAVRgisrrdaKERVEWAIELVRLNG----LEHRKPSQ-------LSGGQQQRVAIARALVFGPKLLLLDEPLA 180
Cdd:cd03290   97 ENITFGSPFN-------KQRYKAVTDACSLQPdidlLPFGDQTEigerginLSGGQRQRICVARALYQNTNIVFLDDPFS 169

                        170       180       190
                 ....*....|....*....|....*....|..
gi 914601027 181 ALDRKLREEVRLE--LRRLQGTlGVTTVLVTH 210
Cdd:cd03290  170 ALDIHLSDHLMQEgiLKFLQDD-KRTLVLVTH 200
PRK13546 PRK13546
teichoic acids export ABC transporter ATP-binding subunit TagH;
33-234 9.30e-12

teichoic acids export ABC transporter ATP-binding subunit TagH;


Pssm-ID: 184131 [Multi-domain]  Cd Length: 264  Bit Score: 64.84  E-value: 9.30e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  33 TVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIvigSRDvthvppaqRDIGLVFQSYALFPNMTVAG 112
Cdd:PRK13546  36 TFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV---DRN--------GEVSVIAISAGLSGQLTGIE 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 113 NIAFSLAVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAALDRKLREEVRL 192
Cdd:PRK13546 105 NIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLD 184

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 914601027 193 ELRRLQGTlGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLG 234
Cdd:PRK13546 185 KIYEFKEQ-NKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYG 225
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
 38-228 1.23e-11

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 65.81  E-value: 1.23e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  38 SDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGlIQPTGGrivigSRDVT----------HVPPAQRDIGLVFQSYAL--- 104
Cdd:PRK10938 277 HNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DHPQGY-----SNDLTlfgrrrgsgeTIWDIKKHIGYVSSSLHLdyr 350

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 105 ----FPNMTVAG---NIAFSLAVrgiSRRDAKERVEWaIELVRLNGLEHRKPSQ-LSGGQQQRVAIARALVFGPKLLLLD 176
Cdd:PRK10938 351 vstsVRNVILSGffdSIGIYQAV---SDRQQKLAQQW-LDILGIDKRTADAPFHsLSWGQQRLALIVRALVKHPTLLILD 426

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 914601027 177 EPLAALDRKLREEVRLELRRLQGTlGVTTVLVT--HDQDEAMSMSDRIAVLAQG 228
Cdd:PRK10938 427 EPLQGLDPLNRQLVRRFVDVLISE-GETQLLFVshHAEDAPACITHRLEFVPDG 479
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
 44-252 1.52e-11

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: 62.59  E-value: 1.52e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  44 VAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIvigsrdvthvppaqrdiglvfqsyalfpnmtvagniafslavrgi 123
Cdd:cd03222   22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDND--------------------------------------------- 56

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 124 srrdakervEWaiELVRLNglehRKPS--QLSGGQQQRVAIARALVFGPKLLLLDEPLAALDRKLREEVRLELRRLQGTL 201
Cdd:cd03222   57 ---------EW--DGITPV----YKPQyiDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEG 121

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 914601027 202 GVTTVLVTHDQDEAMSMSDRIAVL-AQGVIQQLGSPGELYRQPANRFVAGFL 252
Cdd:cd03222  122 KKTALVVEHDLAVLDYLSDRIHVFeGEPGVYGIASQPKGTREGINRFLRGYL 173
PRK13541 PRK13541
cytochrome c biogenesis protein CcmA; Provisional
 39-188 2.03e-11

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184128 [Multi-domain]  Cd Length: 195  Bit Score: 62.58  E-value: 2.03e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  39 DVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVP-PAQRDIGlvfQSYALFPNMTVAGNIAFS 117
Cdd:PRK13541  18 DLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAkPYCTYIG---HNLGLKLEMTVFENLKFW 94

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 914601027 118 LAVRgisrrDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAALDRKLRE 188
Cdd:PRK13541  95 SEIY-----NSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRD 160
PLN03232 PLN03232
ABC transporter C family member; Provisional
 44-268 2.15e-11

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 65.77  E-value: 2.15e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   44 VAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTH--VPPAQRDIGLVFQSYALFPNmTVAGNI-AFS--- 117
Cdd:PLN03232 1259 VSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKfgLTDLRRVLSIIPQSPVLFSG-TVRFNIdPFSehn 1337

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  118 -----LAVRGISRRDAKERVEWAIELVRLNGLEHrkpsqLSGGQQQRVAIARALVFGPKLLLLDEPLAALD--------R 184
Cdd:PLN03232 1338 dadlwEALERAHIKDVIDRNPFGLDAEVSEGGEN-----FSVGQRQLLSLARALLRRSKILVLDEATASVDvrtdsliqR 1412

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  185 KLREEVRlelrrlqgtlGVTTVLVTHDQDEAMSmSDRIAVLAQGVIQQLGSPGELYRQPANRF--VAGFLGAAN---LFH 259
Cdd:PLN03232 1413 TIREEFK----------SCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRDTSAFfrMVHSTGPANaqyLSN 1481


                  ....*....
gi 914601027  260 GIIAREGNG 268
Cdd:PLN03232 1482 LVFERRENG 1490
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
 37-211 2.20e-11

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 65.36  E-value: 2.20e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  37 VSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSR-DVTHvppaqrdiglvFQSY--ALFPNMTVAGN 113
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKlEVAY-----------FDQHraELDPEKTVMDN 403

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 114 IAfslavrgisrrDAKERVEwaielvrLNG------------LEHRKPSQ-----LSGGQQQRVAIARALVFGPKLLLLD 176
Cdd:PRK11147 404 LA-----------EGKQEVM-------VNGrprhvlgylqdfLFHPKRAMtpvkaLSGGERNRLLLARLFLKPSNLLILD 465

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 914601027 177 EPLAALD---RKLREEVrleLRRLQGTLgvttVLVTHD 211
Cdd:PRK11147 466 EPTNDLDvetLELLEEL---LDSYQGTV----LLVSHD 496
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
 52-211 3.78e-11

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 64.37  E-value: 3.78e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  52 ILGPSGSGKSTLLGLVAGLIQPTGGrivigsrDVTHVPPAQrdIGLVFQSYALFPNMTVAGNIAfsLAVRGIsrRDAKER 131
Cdd:PRK11819  38 VLGLNGAGKSTLLRIMAGVDKEFEG-------EARPAPGIK--VGYLPQEPQLDPEKTVRENVE--EGVAEV--KAALDR 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 132 VEW---------------AIELVRL-------NG--LEHR---------------KPSQLSGGQQQRVAIARALVFGPKL 172
Cdd:PRK11819 105 FNEiyaayaepdadfdalAAEQGELqeiidaaDAwdLDSQleiamdalrcppwdaKVTKLSGGERRRVALCRLLLEKPDM 184

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 914601027 173 LLLDEPLAALDrklREEVR-LE--LRRLQGTLgvttVLVTHD 211
Cdd:PRK11819 185 LLLDEPTNHLD---AESVAwLEqfLHDYPGTV----VAVTHD 219
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
 40-228 6.42e-11

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


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 63.97  E-value: 6.42e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027    40 VDLTVAEGEFLSILGPSGSGKSTLLGLVAGliQPTGGRIVIGSRDVTHVP---PAQRDIGLVFQSYALFPNMTVAGNIAF 116
Cdd:TIGR00956  782 VDGWVKPGTLTALMGASGAGKTTLLNVLAE--RVTTGVITGGDRLVNGRPldsSFQRSIGYVQQQDLHLPTSTVRESLRF 859

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   117 SLAVRGISRRDAKERVEWAIELVRLNGLEHRKP-------SQLSGGQQQRVAIARALVFGPKLLL-LDEPLAALDRKLRE 188
Cdd:TIGR00956  860 SAYLRQPKSVSKSEKMEYVEEVIKLLEMESYADavvgvpgEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAW 939

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 914601027   189 EVRLELRRLQGTlGvTTVLVTHDQDEAMSMS--DRIAVLAQG 228
Cdd:TIGR00956  940 SICKLMRKLADH-G-QAILCTIHQPSAILFEefDRLLLLQKG 979
ycf16 CHL00131
sulfate ABC transporter protein; Validated
 20-212 9.47e-11

sulfate ABC transporter protein; Validated


Pssm-ID: 214372 [Multi-domain]  Cd Length: 252  Bit Score: 61.58  E-value: 9.47e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  20 PAIEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGliQP----TGGRIVIGSRDVTHVPP---AQ 92
Cdd:CHL00131   6 PILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPaykiLEGDILFKGESILDLEPeerAH 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  93 RDIGLVFQsyalFPnMTVAG--NIAFSLAV-------RGISRRDAKERVEWAIELVRLNGLE----HRKPSQ-LSGGQQQ 158
Cdd:CHL00131  84 LGIFLAFQ----YP-IEIPGvsNADFLRLAynskrkfQGLPELDPLEFLEIINEKLKLVGMDpsflSRNVNEgFSGGEKK 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 914601027 159 RVAIARALVFGPKLLLLDEPLAALDRKLREEVRLELRRLQgTLGVTTVLVTHDQ 212
Cdd:CHL00131 159 RNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLM-TSENSIILITHYQ 211
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
 20-242 1.25e-10

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: 61.41  E-value: 1.25e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  20 PAIEVSGLSKHFGTVcaVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRdvthvppaqrdIGLVF 99
Cdd:cd03291   38 NNLFFSNLCLVGAPV--LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-----------ISFSS 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 100 QSYALFPNmTVAGNIAFSLAVRGISRRDAKERVEWAIELVRL----NGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLL 175
Cdd:cd03291  105 QFSWIMPG-TIKENIIFGVSYDEYRYKSVVKACQLEEDITKFpekdNTVLGEGGITLSGGQRARISLARAVYKDADLYLL 183

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 914601027 176 DEPLAALDRKLREEVrLELRRLQGTLGVTTVLVThDQDEAMSMSDRIAVLAQGVIQQLGSPGELYRQ 242
Cdd:cd03291  184 DSPFGYLDVFTEKEI-FESCVCKLMANKTRILVT-SKMEHLKKADKILILHEGSSYFYGTFSELQSL 248
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
 37-228 1.44e-10

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


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 63.20  E-value: 1.44e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027    37 VSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGliQPTGGRIVIGSRdVTHVPPAQRDI-----GLVFQSYAL---FPNM 108
Cdd:TIGR00956   77 LKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAS--NTDGFHIGVEGV-ITYDGITPEEIkkhyrGDVVYNAETdvhFPHL 153

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   109 TVAGNIAFSLAVRGISRR----DAKERVEWAIELV-RLNGLEHRKPSQ--------LSGGQQQRVAIARALVFGPKLLLL 175
Cdd:TIGR00956  154 TVGETLDFAARCKTPQNRpdgvSREEYAKHIADVYmATYGLSHTRNTKvgndfvrgVSGGERKRVSIAEASLGGAKIQCW 233

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 914601027   176 DEPLAALD--------RKLREEVRLElrrlqgtlgVTTVLVTHDQ--DEAMSMSDRIAVLAQG 228
Cdd:TIGR00956  234 DNATRGLDsatalefiRALKTSANIL---------DTTPLVAIYQcsQDAYELFDKVIVLYEG 287
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 43-256 1.45e-10

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


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 62.49  E-value: 1.45e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  43 TVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIvigsrdvtHVPPAQRDI-----GLVFQSYalFpNMTVAGNI--- 114
Cdd:COG1245   95 VPKKGKVTGILGPNGIGKSTALKILSGELKPNLGDY--------DEEPSWDEVlkrfrGTELQDY--F-KKLANGEIkva 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 115 -----------AFSLAVRGI-SRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAAL 182
Cdd:COG1245  164 hkpqyvdlipkVFKGTVRELlEKVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYL 243

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 183 DRKLREEVRLELRRLQGTlGVTTVLVTHDQdeAM--SMSDRIAVL-----AQGVIQQLGSPgelyRQPANRFVAGFLGAA 255
Cdd:COG1245  244 DIYQRLNVARLIRELAEE-GKYVLVVEHDL--AIldYLADYVHILygepgVYGVVSKPKSV----RVGINQYLDGYLPEE 316


                 .
gi 914601027 256 N 256
Cdd:COG1245  317 N 317
tagH PRK13545
teichoic acids export protein ATP-binding subunit; Provisional
 36-184 3.08e-10

teichoic acids export protein ATP-binding subunit; Provisional


Pssm-ID: 184130 [Multi-domain]  Cd Length: 549  Bit Score: 61.44  E-value: 3.08e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  36 AVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVI-GSrdvthvppaqrdIGLVFQSYALFPNMTVAGNI 114
Cdd:PRK13545  39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIkGS------------AALIAISSGLNGQLTGIENI 106

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 115 AFSLAVRGISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAALDR 184
Cdd:PRK13545 107 ELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQ 176
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
 25-228 3.24e-10

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 61.28  E-value: 3.24e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  25 SGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDV---THVPPAQRDIGLVFQS 101
Cdd:PRK10982   2 SNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfkSSKEALENGISMVHQE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 102 YALFPNMTVAGNIAFS-LAVRGI------SRRDAKervewAI--EL-VRLNGLEhrKPSQLSGGQQQRVAIARALVFGPK 171
Cdd:PRK10982  82 LNLVLQRSVMDNMWLGrYPTKGMfvdqdkMYRDTK-----AIfdELdIDIDPRA--KVATLSVSQMQMIEIAKAFSYNAK 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 914601027 172 LLLLDEPLAALDRKLREEVRLELRRLQGTlGVTTVLVTHDQDEAMSMSDRIAVLAQG 228
Cdd:PRK10982 155 IVIMDEPTSSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDG 210
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
 25-239 3.41e-10

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: 61.85  E-value: 3.41e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027    25 SGLSKHFGTVcaVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRdvthvppaqrdIGLVFQSYAL 104
Cdd:TIGR01271  432 SNFSLYVTPV--LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-----------ISFSPQTSWI 498

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   105 FPNmTVAGNIAFSLAVRGISRRDAKERVEWAIELVRL----NGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLA 180
Cdd:TIGR01271  499 MPG-TIKDNIIFGLSYDEYRYTSVIKACQLEEDIALFpekdKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFT 577

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 914601027   181 ALDRKLREEVrLELRRLQGTLGVTTVLVThDQDEAMSMSDRIAVLAQGVIQQLGSPGEL 239
Cdd:TIGR01271  578 HLDVVTEKEI-FESCLCKLMSNKTRILVT-SKLEHLKKADKILLLHEGVCYFYGTFSEL 634
PTZ00243 PTZ00243
ABC transporter; Provisional
 40-247 4.41e-10

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 61.72  E-value: 4.41e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   40 VDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTH--VPPAQRDIGLVFQSYALFpNMTVAGNI-AF 116
Cdd:PTZ00243 1329 VSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAygLRELRRQFSMIPQDPVLF-DGTVRQNVdPF 1407

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  117 SLAvrgisrrdAKERVEWAIELVrlnGLEHRKPSQLSG--------------GQQQRVAIARALV-FGPKLLLLDEPLA- 180
Cdd:PTZ00243 1408 LEA--------SSAEVWAALELV---GLRERVASESEGidsrvleggsnysvGQRQLMCMARALLkKGSGFILMDEATAn 1476

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  181 ---ALDRKLREEVRlelrrlqGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELYRQPANRF 247
Cdd:PTZ00243 1477 idpALDRQIQATVM-------SAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIF 1539
sufC PRK09580
cysteine desulfurase ATPase component; Reviewed
 40-183 1.12e-09

cysteine desulfurase ATPase component; Reviewed


Pssm-ID: 181965 [Multi-domain]  Cd Length: 248  Bit Score: 58.26  E-value: 1.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  40 VDLTVAEGEFLSILGPSGSGKSTLLGLVAGL--IQPTGGRIVIGSRDVTHVPPAQR---DIGLVFQSYALFPNMTVAGNI 114
Cdd:PRK09580  20 LNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEDRageGIFMAFQYPVEIPGVSNQFFL 99

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 914601027 115 AFSL-AVRG------ISRRDAKERVEWAIELVRL--NGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAALD 183
Cdd:PRK09580 100 QTALnAVRSyrgqepLDRFDFQDLMEEKIALLKMpeDLLTRSVNVGFSGGEKKRNDILQMAVLEPELCILDESDSGLD 177
PLN03130 PLN03130
ABC transporter C family member; Provisional
 40-239 2.08e-09

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 59.37  E-value: 2.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   40 VDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPPA--QRDIGLVFQSYALFpnmtvAGNIAFS 117
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMdlRKVLGIIPQAPVLF-----SGTVRFN 1332

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  118 LAVRGiSRRDAK--ERVEWA--IELVRLN--GLE---HRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAALD----- 183
Cdd:PLN03130 1333 LDPFN-EHNDADlwESLERAhlKDVIRRNslGLDaevSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDvrtda 1411

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 914601027  184 ---RKLREEVRlelrrlqgtlGVTTVLVTHDQDEAMSmSDRIAVLAQGVIQQLGSPGEL 239
Cdd:PLN03130 1412 liqKTIREEFK----------SCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENL 1459
PvdE COG4615
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...
 40-233 2.33e-09

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: 58.66  E-value: 2.33e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  40 VDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVThvpPAQRD-----IGLVFQSYALFPNMTvagni 114
Cdd:COG4615  351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVT---ADNREayrqlFSAVFSDFHLFDRLL----- 422

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 115 afslavrGISRRDAKERV-EWaieLVRLNgLEHrKPS---------QLSGGQQQRVAIARALVFGPKLLLLDEpLAAlD- 183
Cdd:COG4615  423 -------GLDGEADPARArEL---LERLE-LDH-KVSvedgrfsttDLSQGQRKRLALLVALLEDRPILVFDE-WAA-Dq 488

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 914601027 184 -----RKLREEVRLELRRlqgtLGVTTVLVTHDqDEAMSMSDRIAVLAQGVIQQL 233
Cdd:COG4615  489 dpefrRVFYTELLPELKA----RGKTVIAISHD-DRYFDLADRVLKMDYGKLVEL 538
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
 36-228 3.11e-09

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 58.20  E-value: 3.11e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  36 AVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVPP---AQRDIGLVFQ---SYALFPNMT 109
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNAneaINHGFALVTEerrSTGIYAYLD 342

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 110 VAGN--IA----FSLAVRGISRRDAKERVEWAIELVRLNGLEHRKP-SQLSGGQQQRVAIARALVFGPKLLLLDEPLAAL 182
Cdd:PRK10982 343 IGFNslISnirnYKNKVGLLDNSRMKSDTQWVIDSMRVKTPGHRTQiGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGI 422

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 914601027 183 DRKLREEV-RLELRRLQGTLGVttVLVTHDQDEAMSMSDRIAVLAQG 228
Cdd:PRK10982 423 DVGAKFEIyQLIAELAKKDKGI--IIISSEMPELLGITDRILVMSNG 467
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
 97-225 4.25e-09

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 58.50  E-value: 4.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   97 LVFQSYALFpNMTVAGNIAFSlavrgisRRDA-KERVEWAIELVRLNGLEHRKPSQ-----------LSGGQQQRVAIAR 164
Cdd:PTZ00265 1300 IVSQEPMLF-NMSIYENIKFG-------KEDAtREDVKRACKFAAIDEFIESLPNKydtnvgpygksLSGGQKQRIAIAR 1371

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 914601027  165 ALVFGPKLLLLDEPLAALDRKLREEVRLELRRLQGTLGVTTVLVTHdQDEAMSMSDRIAVL 225
Cdd:PTZ00265 1372 ALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH-RIASIKRSDKIVVF 1431
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
43-256 4.42e-09

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 57.90  E-value: 4.42e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  43 TVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRivigsrdvTHVPPAQRDI-----GLVFQSYalFPNMtVAGNIAFS 117
Cdd:PRK13409  95 IPKEGKVTGILGPNGIGKTTAVKILSGELIPNLGD--------YEEEPSWDEVlkrfrGTELQNY--FKKL-YNGEIKVV 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 118 L----------AVRG-----ISRRDAKERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAAL 182
Cdd:PRK13409 164 HkpqyvdlipkVFKGkvrelLKKVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYL 243

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 183 DRKLREEVRLELRRLqgTLGVTTVLVTHDQdeAM--SMSDRIAVL-----AQGVIQQLGSPgelyRQPANRFVAGFLGAA 255
Cdd:PRK13409 244 DIRQRLNVARLIREL--AEGKYVLVVEHDL--AVldYLADNVHIAygepgAYGVVSKPKGV----RVGINEYLKGYLPEE 315


                 .
gi 914601027 256 N 256
Cdd:PRK13409 316 N 316
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
 41-226 1.63e-08

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 56.18  E-value: 1.63e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  41 DLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVP--PAQRDIGLVFQSyaLFPNMTVAGNIAFSL 118
Cdd:PRK10938  23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSfeQLQKLVSDEWQR--NNTDMLSPGEDDTGR 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 119 AVRGISRRDAK--ERVEWAIELVRLNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAALDRKLREEVRLELRR 196
Cdd:PRK10938 101 TTAEIIQDEVKdpARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLAS 180

                        170       180       190
                 ....*....|....*....|....*....|
gi 914601027 197 LQGTlGVTTVLVTHDQDEAMSMSDRIAVLA 226
Cdd:PRK10938 181 LHQS-GITLVLVLNRFDEIPDFVQFAGVLA 209
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
 22-222 2.56e-08

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: 53.10  E-value: 2.56e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  22 IEVSGLSKHfgtvcAVSDVDLTVAEGEFLSILGPSGSGKSTLLglVAGLIQPTGGRIVIGsrdvthvPPAQRDIGLVFqs 101
Cdd:cd03238    1 LTVSGANVH-----NLQNLDVSIPLNVLVVVTGVSGSGKSTLV--NEGLYASGKARLISF-------LPKFSRNKLIF-- 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 102 yalfpnmtvAGNIAFSLAVrgisrrdakervewAIELVRLNglehRKPSQLSGGQQQRVAIARALVFGPK--LLLLDEPL 179
Cdd:cd03238   65 ---------IDQLQFLIDV--------------GLGYLTLG----QKLSTLSGGELQRVKLASELFSEPPgtLFILDEPS 117

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 914601027 180 AALDRKLREEVRLELRRLqGTLGVTTVLVTHDqDEAMSMSDRI 222
Cdd:cd03238  118 TGLHQQDINQLLEVIKGL-IDLGNTVILIEHN-LDVLSSADWI 158
PLN03140 PLN03140
ABC transporter G family member; Provisional
 47-210 4.26e-08

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 55.24  E-value: 4.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   47 GEFLSILGPSGSGKSTLLGLVAGliQPTGGRIViGSRDVTHVPPAQ----RDIGLVFQSYALFPNMTVAGNIAFSLAVR- 121
Cdd:PLN03140  906 GVLTALMGVSGAGKTTLMDVLAG--RKTGGYIE-GDIRISGFPKKQetfaRISGYCEQNDIHSPQVTVRESLIYSAFLRl 982

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  122 --GISRRDAKERVEWAIELVRLNGLEHR-----KPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAALDRKLREEVRLEL 194
Cdd:PLN03140  983 pkEVSKEEKMMFVDEVMELVELDNLKDAivglpGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTV 1062

                         170
                  ....*....|....*.
gi 914601027  195 RRLQGTlGVTTVLVTH 210
Cdd:PLN03140 1063 RNTVDT-GRTVVCTIH 1077
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
 22-222 8.74e-08

ATP-binding cassette domain I 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: 213237 [Multi-domain]  Cd Length: 226  Bit Score: 52.26  E-value: 8.74e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  22 IEVSGLSKHfgtvcAVSDVDLTVAEGEFLSILGPSGSGKSTLlglVAGLIQPTGGRIVIGS--------------RDVTH 87
Cdd:cd03270    1 IIVRGAREH-----NLKNVDVDIPRNKLVVITGVSGSGKSSL---AFDTIYAEGQRRYVESlsayarqflgqmdkPDVDS 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  88 V---PPAqrdIGLVFQSYALFPNMTVAgniafslAVRGI--------SRRDAKERVEWAIELvrlnGLEH----RKPSQL 152
Cdd:cd03270   73 IeglSPA---IAIDQKTTSRNPRSTVG-------TVTEIydylrllfARVGIRERLGFLVDV----GLGYltlsRSAPTL 138

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 914601027 153 SGGQQQRVAIARALvfGPKLL----LLDEPLAALDRKLREEVRLELRRLQgTLGVTTVLVTHDQDeAMSMSDRI 222
Cdd:cd03270  139 SGGEAQRIRLATQI--GSGLTgvlyVLDEPSIGLHPRDNDRLIETLKRLR-DLGNTVLVVEHDED-TIRAADHV 208
PLN03073 PLN03073
ABC transporter F family; Provisional
 50-228 1.40e-07

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 53.33  E-value: 1.40e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  50 LSILGPSGSGKSTLLGLVAGLIQPTGGrIVIGSRDVTHVPPAQRDI-GLVFQSYAL------FPNMTvAGNIAFSLAVRG 122
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISGELQPSSG-TVFRSAKVRMAVFSQHHVdGLDLSSNPLlymmrcFPGVP-EQKLRAHLGSFG 615

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 123 ISrrdakervewaielvrlNGLEHRKPSQLSGGQQQRVAIARALVFGPKLLLLDEPLAALDRKLREEVRLELRRLQGtlG 202
Cdd:PLN03073 616 VT-----------------GNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQG--G 676

                        170       180
                 ....*....|....*....|....*.
gi 914601027 203 VttVLVTHDQDEAMSMSDRIAVLAQG 228
Cdd:PLN03073 677 V--LMVSHDEHLISGSVDELWVVSEG 700
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
 29-223 1.48e-07

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


Pssm-ID: 213194 [Multi-domain]  Cd Length: 162  Bit Score: 50.44  E-value: 1.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  29 KHFGTVCAVSDVDLTvaEGEFLSILGPSGSGKSTLLglvagliqptggrivigsrdvthvppaqRDIGLVfqsyalfpnm 108
Cdd:cd03227    5 GRFPSYFVPNDVTFG--EGSLTIITGPNGSGKSTIL----------------------------DAIGLA---------- 44

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 109 tVAGNiafslAVRGISRRDAKERVEWAIELVRLNGLEHrkpsQLSGGQQQRVAIARALVFGPK----LLLLDEPLAALDr 184
Cdd:cd03227   45 -LGGA-----QSATRRRSGVKAGCIVAAVSAELIFTRL----QLSGGEKELSALALILALASLkprpLYILDEIDRGLD- 113

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 914601027 185 kLREEVRLE---LRRLQGtlGVTTVLVTHDQdEAMSMSDRIA 223
Cdd:cd03227  114 -PRDGQALAeaiLEHLVK--GAQVIVITHLP-ELAELADKLI 151
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
 22-235 2.05e-07

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: 51.78  E-value: 2.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  22 IEVSGLSKHF--GTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQpTGGRIVIGSRDVTHVPPAQ--RDIGL 97
Cdd:cd03289    3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKwrKAFGV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  98 VFQSYALFpnmtvAGNIAFSLAVRGisrRDAKERVEWAIELVRLNGLEHRKPSQ-----------LSGGQQQRVAIARAL 166
Cdd:cd03289   82 IPQKVFIF-----SGTFRKNLDPYG---KWSDEEIWKVAEEVGLKSVIEQFPGQldfvlvdggcvLSHGHKQLMCLARSV 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 914601027 167 VFGPKLLLLDEPLAALDRKLREEVRlelRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQGVIQQLGS 235
Cdd:cd03289  154 LSKAKILLLDEPSAHLDPITYQVIR---KTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDS 219
ABCC_SUR2 cd03288
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...
 40-247 2.56e-07

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: 51.45  E-value: 2.56e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  40 VDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSRDVTHVP--PAQRDIGLVFQSYALFpnmtvAGNIAFS 117
Cdd:cd03288   40 VKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPlhTLRSRLSIILQDPILF-----SGSIRFN 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 118 LAVRgisRRDAKERVEWAIELVRLNGLEHRKPSQL-----------SGGQQQRVAIARALVFGPKLLLLDEPLAALDrkL 186
Cdd:cd03288  115 LDPE---CKCTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMDEATASID--M 189

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 914601027 187 REEVRLELRRLQGTLGVTTVLVTHDQDEAMSmSDRIAVLAQGVIQQLGSPGELYRQPANRF 247
Cdd:cd03288  190 ATENILQKVVMTAFADRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQEDGVF 249
TOBE_2 pfam08402
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the ...
 294-371 3.15e-07

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: 47.23  E-value: 3.15e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 914601027  294 MLVRPERVNLqpatEAPANRFciDCHVADVVYQGEIVRYAVEAPPVGPVIASCQHV-VPRFSPGDRACFSWRPEDAWLI 371
Cdd:pfam08402   1 LAIRPEKIRL----AAAANGL--SGTVTDVEYLGDHTRYHVELAGGEELVVRVPNAhARPPAPGDRVGLGWDPEDAHVL 73
3a01203 TIGR00954
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...
 37-210 3.84e-07

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: 52.06  E-value: 3.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   37 VSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGSR-DVTHVPpaQRdiglvfqsyalfPNMTVAG--- 112
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKgKLFYVP--QR------------PYMTLGTlrd 533

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  113 NIAFSLAVRGISRRDAKERV-EWAIELVRLNGLEHRKPS---------QLSGGQQQRVAIARALVFGPKLLLLDEPLAAL 182
Cdd:TIGR00954 534 QIIYPDSSEDMKRRGLSDKDlEQILDNVQLTHILEREGGwsavqdwmdVLSGGEKQRIAMARLFYHKPQFAILDECTSAV 613

                         170       180
                  ....*....|....*....|....*...
gi 914601027  183 DrklrEEVRLELRRLQGTLGVTTVLVTH 210
Cdd:TIGR00954 614 S----VDVEGYMYRLCREFGITLFSVSH 637
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
 39-246 2.63e-06

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: 49.52  E-value: 2.63e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027    39 DVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQpTGGRIVIG--SRDVTHVPPAQRDIGLVFQSYALFPnmtvagniaf 116
Cdd:TIGR01271 1237 DLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDgvSWNSVTLQTWRKAFGVIPQKVFIFS---------- 1305

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027   117 slavrGISRRDAKERVEWA-------IELVRLNGLEHRKPSQL-----------SGGQQQRVAIARALVFGPKLLLLDEP 178
Cdd:TIGR01271 1306 -----GTFRKNLDPYEQWSdeeiwkvAEEVGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLARSILSKAKILLLDEP 1380

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 914601027   179 LAALDRKLREEVRlelRRLQGTLGVTTVLVTHDQDEAMSMSDRIAVLAQG------VIQQLGSPGELYRQ---PANR 246
Cdd:TIGR01271 1381 SAHLDPVTLQIIR---KTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSsvkqydSIQKLLNETSLFKQamsAADR 1454
PLN03073 PLN03073
ABC transporter F family; Provisional
 37-183 5.60e-06

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 48.32  E-value: 5.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  37 VSDVDLTVAEGEFLSILGPSGSGKSTLLGLVA-----GLiqPTGGRI------VIGSR----------DVTHVPPAQRDI 95
Cdd:PLN03073 193 IVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAmhaidGI--PKNCQIlhveqeVVGDDttalqcvlntDIERTQLLEEEA 270

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  96 GLVFQSYAL-FPNMTVAGNIAFSLAVRGISRRDAKERVEWAIELVR-----------LNGL------EHRKPSQLSGGQQ 157
Cdd:PLN03073 271 QLVAQQRELeFETETGKGKGANKDGVDKDAVSQRLEEIYKRLELIDaytaearaasiLAGLsftpemQVKATKTFSGGWR 350

                        170       180
                 ....*....|....*....|....*.
gi 914601027 158 QRVAIARALVFGPKLLLLDEPLAALD 183
Cdd:PLN03073 351 MRIALARALFIEPDLLLLDEPTNHLD 376
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
 52-213 7.03e-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: 46.45  E-value: 7.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  52 ILGPSGSGKSTLL-GLVAGL--IQPTGGRIVIGSRDVTHVPPAQRDIGLVFQS-----YALFPNMTVAGNIAFslaVRgi 123
Cdd:cd03240   27 IVGQNGAGKTTIIeALKYALtgELPPNSKGGAHDPKLIREGEVRAQVKLAFENangkkYTITRSLAILENVIF---CH-- 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 124 srrdaKERVEWAIelvrlngLEHRKpsQLSGGQQQ------RVAIARALVFGPKLLLLDEPLAALDRKLREEVRLELRRL 197
Cdd:cd03240  102 -----QGESNWPL-------LDMRG--RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEESLAEIIEE 167

                        170
                 ....*....|....*..
gi 914601027 198 QGTLGV-TTVLVTHDQD 213
Cdd:cd03240  168 RKSQKNfQLIVITHDEE 184
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
 22-227 1.40e-05

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 47.09  E-value: 1.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  22 IEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIgsrdvthvpPAQRDIGLVFQS 101
Cdd:PRK10636   2 IVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTF---------PGNWQLAWVNQE 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 102 YALFPNMTVAGNIAFSLAVRGISRR--DAKERVE----------------WAIE---LVRLNGLEHRKP------SQLSG 154
Cdd:PRK10636  73 TPALPQPALEYVIDGDREYRQLEAQlhDANERNDghaiatihgkldaidaWTIRsraASLLHGLGFSNEqlerpvSDFSG 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 914601027 155 GQQQRVAIARALVFGPKLLLLDEPLAALDrkLREEVRLE--LRRLQGTLgvttVLVTHDQDEAMSMSDRIAVLAQ 227
Cdd:PRK10636 153 GWRMRLNLAQALICRSDLLLLDEPTNHLD--LDAVIWLEkwLKSYQGTL----ILISHDRDFLDPIVDKIIHIEQ 221
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
 20-242 2.20e-05

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 46.32  E-value: 2.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  20 PAIEVSGLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVAGLIQPTGGRIVIGsrdvthvppaqRDIGL-V 98
Cdd:PRK10636 311 PLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLA-----------KGIKLgY 379

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  99 FQSYALfpNMTVAGNIAFSLAVRgISRRDAKERVEWAIELVRLNGLEHRKPS-QLSGGQQQRVAIARALVFGPKLLLLDE 177
Cdd:PRK10636 380 FAQHQL--EFLRADESPLQHLAR-LAPQELEQKLRDYLGGFGFQGDKVTEETrRFSGGEKARLVLALIVWQRPNLLLLDE 456

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 914601027 178 PLAALDRKLREEVRLELRRLQGTLgvttVLVTHDQDEAMSMSDRIAVLAQGVIQQLGSPGELYRQ 242
Cdd:PRK10636 457 PTNHLDLDMRQALTEALIDFEGAL----VVVSHDRHLLRSTTDDLYLVHDGKVEPFDGDLEDYQQ 517
GguA NF040905
sugar ABC transporter ATP-binding protein;
37-244 2.76e-05

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 45.94  E-value: 2.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  37 VSDVDLTVAEGEFLSILGPSGSGKSTL----LGLVAGliQPTGGRIVIGSR--DVTHVPPAQrDIGLVF-----QSYALF 105
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTELamsvFGRSYG--RNISGTVFKDGKevDVSTVSDAI-DAGLAYvtedrKGYGLN 352

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 106 PNMTVAGNIafSLA-VRGISRR---DAKERVEWAIELVRlnGLEHRKPS------QLSGGQQQRVAIARALVFGPKLLLL 175
Cdd:NF040905 353 LIDDIKRNI--TLAnLGKVSRRgviDENEEIKVAEEYRK--KMNIKTPSvfqkvgNLSGGNQQKVVLSKWLFTDPDVLIL 428

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 914601027 176 DEPLAALDRKLREEVRLELRRL--QGTlGVttVLVTHDQDEAMSMSDRIAVLAQGVIQqlgspGELYRQPA 244
Cdd:NF040905 429 DEPTRGIDVGAKYEIYTIINELaaEGK-GV--IVISSELPELLGMCDRIYVMNEGRIT-----GELPREEA 491
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
 129-222 2.52e-04

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


Pssm-ID: 273184 [Multi-domain]  Cd Length: 925  Bit Score: 43.08  E-value: 2.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  129 KERVEWAIELvrlnGLEH----RKPSQLSGGQQQRVAIARALvfGPKLL----LLDEPLAALDRKLREEVRLELRRLQgT 200
Cdd:TIGR00630 466 RERLGFLIDV----GLDYlslsRAAGTLSGGEAQRIRLATQI--GSGLTgvlyVLDEPSIGLHQRDNRRLINTLKRLR-D 538

                          90       100
                  ....*....|....*....|..
gi 914601027  201 LGVTTVLVTHDQDeAMSMSDRI 222
Cdd:TIGR00630 539 LGNTLIVVEHDED-TIRAADYV 559
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
 129-222 3.09e-04

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 42.89  E-value: 3.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  129 KERVEWAIELvrlnGLEHRKPSQ----LSGGQQQRVAIARALvfGPKLL----LLDEPLAALDRKLREEVRLELRRLQGT 200
Cdd:PRK00635  454 KSRLSILIDL----GLPYLTPERalatLSGGEQERTALAKHL--GAELIgityILDEPSIGLHPQDTHKLINVIKKLRDQ 527

                          90       100
                  ....*....|....*....|..
gi 914601027  201 lGVTTVLVTHDqDEAMSMSDRI 222
Cdd:PRK00635  528 -GNTVLLVEHD-EQMISLADRI 547
VirB4 COG3451
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and ...
 52-166 3.53e-04

Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 442674 [Multi-domain]  Cd Length: 546  Bit Score: 42.63  E-value: 3.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  52 ILGPSGSGKSTLLGLVAGLIQPTGGRIVIgsrdVthvppaqrDIGlvfQSYALFPNMtVAGN-IAFSLAVR-GI---SRR 126
Cdd:COG3451  209 ILGPSGSGKSFLLKLLLLQLLRYGARIVI----F--------DPG---GSYEILVRA-LGGTyIDLSPGSPtGLnpfDLE 272

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 914601027 127 DAKERVEWAIELVR-LNGLEHRKPSqlsggQQQRVAIARAL 166
Cdd:COG3451  273 DTEEKRDFLLELLElLLGREGEPLT-----PEERAAIDRAV 308
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
 15-64 4.63e-04

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


Pssm-ID: 273184 [Multi-domain]  Cd Length: 925  Bit Score: 42.31  E-value: 4.63e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 914601027   15 PVSRRPA----IEVSGLSKHfgtvcAVSDVDLTVAEGEFLSILGPSGSGKSTLL 64
Cdd:TIGR00630 603 PAERRPGngkfLTLKGAREN-----NLKNITVSIPLGLFTCITGVSGSGKSTLI 651
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
29-211 3.61e-03

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 440188 [Multi-domain]  Cd Length: 204  Bit Score: 38.45  E-value: 3.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  29 KHFGTVCAVSDVDLTvaEGEFLsILGPSGSGKSTLL-GLVAGLIQPTGGRIVIGSrDVTHVPPAQRDIGLVF----QSYA 103
Cdd:COG0419    8 ENFRSYRDTETIDFD--DGLNL-IVGPNGAGKSTILeAIRYALYGKARSRSKLRS-DLINVGSEEASVELEFehggKRYR 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027 104 L------FPNMTVAGNIAFSLAVR---GISR--------RDAKERVEWAI-ELVRLNGLEHR---------KPSQLSGGQ 156
Cdd:COG0419   84 IerrqgeFAEFLEAKPSERKEALKrllGLEIyeelkerlKELEEALESALeELAELQKLKQEilaqlsgldPIETLSGGE 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 914601027 157 QQRVAIARALVfgpklLLLDepLAALDRKLREEVRLELRRLQgtlgvttvLVTHD 211
Cdd:COG0419  164 RLRLALADLLS-----LILD--FGSLDEERLERLLDALEELA--------IITHV 203
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
 107-213 6.09e-03

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


Pssm-ID: 273184 [Multi-domain]  Cd Length: 925  Bit Score: 38.84  E-value: 6.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914601027  107 NMTVAGNIAFSLAVRGISRRdakervewaIELVRLNGLEHRKPSQ----LSGGQQQRVAIARAL---VFGPKLLLLDEPL 179
Cdd:TIGR00630 790 DMTVEEAYEFFEAVPSISRK---------LQTLCDVGLGYIRLGQpattLSGGEAQRIKLAKELskrSTGRTLYILDEPT 860

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 914601027  180 AAL---DRKLREEVrleLRRLQGtLGVTTVLVTHDQD 213
Cdd:TIGR00630 861 TGLhfdDIKKLLEV---LQRLVD-KGNTVVVIEHNLD 893
ATPase_flagellum-secretory_path_III cd01136
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ...
 14-68 6.80e-03

Flagellum-specific ATPase/type III secretory pathway virulence-related protein; Flagellum-specific ATPase/type III secretory pathway virulence-related protein. This group of ATPases are responsible for the export of flagellum and virulence-related proteins. The bacterial flagellar motor is similar to the F0F1-ATPase, in that they both are proton-driven rotary molecular devices. However, the main function of the bacterial flagellar motor is to rotate the flagellar filament for cell motility. Intracellular pathogens such as Salmonella and Chlamydia also have proteins which are similar to the flagellar-specific ATPase, but function in the secretion of virulence-related proteins via the type III secretory pathway.


Pssm-ID: 410880 [Multi-domain]  Cd Length: 265  Bit Score: 37.92  E-value: 6.80e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 914601027  14 APVSRRPaievsgLSKHFGTVCAVSDVDLTVAEGEFLSILGPSGSGKSTLLGLVA 68
Cdd:cd01136   40 NPLKRAP------IEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGKSTLLGMIA 88
 
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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