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Conserved domains on  [gi|2753759418|ref|WP_353887721|]
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ABC transporter ATP-binding protein [uncultured Fructobacillus sp.]

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 ...
 4-346 3.04e-177

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


:

Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 496.93  E-value: 3.04e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   4 KMPILEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEKRRVNT 83
Cdd:COG3842     2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  84 VFQNYSLFPNMNVFDNVAFGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDE 163
Cdd:COG3842    82 VFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 164 PLSALDYKLRKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDEPINHFVADFIGETNI 243
Cdd:COG3842   162 PLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGEANL 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 244 VPGIM--KYDYLVHFVGKDFE-NVDAGMRPNERVEVVLRPEDLDLTDPAN-GKLVVTIQDQLFRGDYYEITAVDDDMNTW 319
Cdd:COG3842   242 LPGTVlgDEGGGVRTGGRTLEvPADAGLAAGGPVTVAIRPEDIRLSPEGPeNGLPGTVEDVVFLGSHVRYRVRLGDGQEL 321

                         330       340       350
                  ....*....|....*....|....*....|.
gi 2753759418 320 QVQATNPA----TVGARVGLTFDPEDIHIMR 346
Cdd:COG3842   322 VVRVPNRAalplEPGDRVGLSWDPEDVVVLP 352
 
Name Accession Description Interval E-value
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
 4-346 3.04e-177

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 496.93  E-value: 3.04e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   4 KMPILEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEKRRVNT 83
Cdd:COG3842     2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  84 VFQNYSLFPNMNVFDNVAFGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDE 163
Cdd:COG3842    82 VFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 164 PLSALDYKLRKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDEPINHFVADFIGETNI 243
Cdd:COG3842   162 PLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGEANL 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 244 VPGIM--KYDYLVHFVGKDFE-NVDAGMRPNERVEVVLRPEDLDLTDPAN-GKLVVTIQDQLFRGDYYEITAVDDDMNTW 319
Cdd:COG3842   242 LPGTVlgDEGGGVRTGGRTLEvPADAGLAAGGPVTVAIRPEDIRLSPEGPeNGLPGTVEDVVFLGSHVRYRVRLGDGQEL 321

                         330       340       350
                  ....*....|....*....|....*....|.
gi 2753759418 320 QVQATNPA----TVGARVGLTFDPEDIHIMR 346
Cdd:COG3842   322 VVRVPNRAalplEPGDRVGLSWDPEDVVVLP 352
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
1-283 2.87e-139

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 401.25  E-value: 2.87e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   1 MVEKMPILEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEKRR 80
Cdd:PRK09452    8 PSSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRH 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  81 VNTVFQNYSLFPNMNVFDNVAFGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLL 160
Cdd:PRK09452   88 VNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLL 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 161 LDEPLSALDYKLRKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDEPINHFVADFIGE 240
Cdd:PRK09452  168 LDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIGE 247

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 2753759418 241 TNIVPGIMK-----YDYLVHFVGKDFEN-VDAGMRPNERVEVVLRPEDL 283
Cdd:PRK09452  248 INIFDATVIerldeQRVRANVEGRECNIyVNFAVEPGQKLHVLLRPEDL 296
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
 8-239 7.38e-135

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: 384.67  E-value: 7.38e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   8 LEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEKRRVNTVFQN 87
Cdd:cd03300     1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  88 YSLFPNMNVFDNVAFGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDEPLSA 167
Cdd:cd03300    81 YALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2753759418 168 LDYKLRKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDEPINHFVADFIG 239
Cdd:cd03300   161 LDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
PhnT2 TIGR03265
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ...
 5-335 1.63e-110

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: 327.38  E-value: 1.63e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   5 MPILEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEKRRVNTV 84
Cdd:TIGR03265   2 SPYLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYGIV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  85 FQNYSLFPNMNVFDNVAFGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDEP 164
Cdd:TIGR03265  82 FQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 165 LSALDYKLRKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDEPINHFVADFIGETNIV 244
Cdd:TIGR03265 162 LSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVGEVNWL 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 245 PGIMKYDYLVHFVGKDFENVDAGMRPNERVEVVLRPED--LDLTDPANGKLVVTIQDQLFRGDYYEITAVDDDMNTWQVQ 322
Cdd:TIGR03265 242 PGTRGGGSRARVGGLTLACAPGLAQPGASVRLAVRPEDirVSPAGNAANLLLARVEDMEFLGAFYRLRLRLEGLPGQALV 321

                         330
                  ....*....|...
gi 2753759418 323 ATNPATVGARVGL 335
Cdd:TIGR03265 322 ADVSASEVERLGI 334
tungstate_WtpC NF040840
tungstate ABC transporter ATP-binding protein WtpC;
23-286 1.08e-87

tungstate ABC transporter ATP-binding protein WtpC;


Pssm-ID: 468779 [Multi-domain]  Cd Length: 347  Bit Score: 268.87  E-value: 1.08e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  23 LKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEKRRVNTVFQNYSLFPNMNVFDNVAF 102
Cdd:NF040840   16 LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIAYVYQNYMLFPHKTVFENIAF 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 103 GPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDEPLSALDYKLRKELQQELRN 182
Cdd:NF040840   96 GLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALDVQTRDELIREMKR 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 183 IQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDEPINHFVADFIGETNIVPGIMKYDYLVHFVGKDFE 262
Cdd:NF040840  176 WHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVGFENIIEGVAEKGGEGTILDTGNI 255

                         250       260
                  ....*....|....*....|....
gi 2753759418 263 NVDAGMRPNERVEVVLRPEDLDLT 286
Cdd:NF040840  256 KIELPEEKKGKVRIGIRPEDITIS 279
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 23-166 1.28e-47

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: 158.97  E-value: 1.28e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  23 LKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVIN--DVPAEKRRVNTVFQNYSLFPNMNVFDNV 100
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTddERKSLRKEIGYVFQDPQLFPRLTVRENL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 101 AFGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREI----SELSGGQQQRVAIARALANDPEVLLLDEPLS 166
Cdd:pfam00005  81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVgerpGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
ABC_ATP_DarD NF038007
darobactin export ABC transporter ATP-binding protein;
20-214 9.79e-41

darobactin export ABC transporter ATP-binding protein;


Pssm-ID: 411600 [Multi-domain]  Cd Length: 218  Bit Score: 143.32  E-value: 9.79e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  20 TEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQ-VINDVPAEK---RR--VNTVFQNYSLFPN 93
Cdd:NF038007   18 TKVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKeVTNLSYSQKiilRRelIGYIFQSFNLIPH 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  94 MNVFDNVAFGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDEPLSALDYKLR 173
Cdd:NF038007   98 LSIFDNVALPLKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNPALLLADEPTGNLDSKNA 177

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2753759418 174 KELQQELRNIQKRlGITFVFVTHDQeEALAMSDWIFVMHDG 214
Cdd:NF038007  178 RAVLQQLKYINQK-GTTIIMVTHSD-EASTYGNRIINMKDG 216
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
16-203 5.70e-32

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 119.26  E-value: 5.70e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  16 SFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIffegqvindVPAEKRRVNTVFQNYSL---FP 92
Cdd:NF040873    1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV---------RRAGGARVAYVPQRSEVpdsLP 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  93 nMNVFDNVAFG--PRLKKMSEKDIQDK--VKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDEPLSAL 168
Cdd:NF040873   72 -LTVRDLVAMGrwARRGLWRRLTRDDRaaVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2753759418 169 DYKLRKELQQELRNIQKRlGITFVFVTHDQEEALA 203
Cdd:NF040873  151 DAESRERIIALLAEEHAR-GATVVVVTHDLELVRR 184
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
7-225 1.10e-17

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 84.79  E-value: 1.10e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   7 ILEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISG--QLQadagkiffEGQVI---NDVpAEKRRV 81
Cdd:NF033858    1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGarKIQ--------QGRVEvlgGDM-ADARHR 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  82 NTVFQ-----------NysLFPNMNVFDNVAFGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIAR 150
Cdd:NF033858   72 RAVCPriaympqglgkN--LYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCC 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2753759418 151 ALANDPEVLLLDEPLSALDYKLRK---ELQQELRniQKRLGITFVFVTHDQEEAlAMSDWIFVMHDGLIQQNGTPEDI 225
Cdd:NF033858  150 ALIHDPDLLILDEPTTGVDPLSRRqfwELIDRIR--AERPGMSVLVATAYMEEA-ERFDWLVAMDAGRVLATGTPAEL 224
GguA NF040905
sugar ABC transporter ATP-binding protein;
7-214 2.42e-14

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 74.06  E-value: 2.42e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   7 ILEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQAD--AGKIFFEGQV-----INDvpAEKR 79
Cdd:NF040905    1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGsyEGEILFDGEVcrfkdIRD--SEAL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  80 RVNTVFQNYSLFPNMNVFDNVAFG-PRLKK--MSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDP 156
Cdd:NF040905   79 GIVIIHQELALIPYLSIAENIFLGnERAKRgvIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDV 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2753759418 157 EVLLLDEPLSALD-------YKLRKELQQElrniqkrlGITFVFVTHDQEEALAMSDWIFVMHDG 214
Cdd:NF040905  159 KLLILDEPTAALNeedsaalLDLLLELKAQ--------GITSIIISHKLNEIRRVADSITVLRDG 215
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
39-225 1.42e-13

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 72.46  E-value: 1.42e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  39 LGPSGSGKSTILKLISGQLQADAGKIFFEGQVI--NDVpAEKRRVNTVFQNYSLFPNMNVFDNVAFGPRLKKMSEKDIQD 116
Cdd:NF033858  298 LGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVdaGDI-ATRRRVGYMSQAFSLYGELTVRQNLELHARLFHLPAAEIAA 376

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 117 KVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDEPLSALDYKLRKELQQELRNIQKRLGITfVFV-T 195
Cdd:NF033858  377 RVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELSREDGVT-IFIsT 455

                         170       180       190
                  ....*....|....*....|....*....|
gi 2753759418 196 HDQEEAlAMSDWIFVMHDGLIQQNGTPEDI 225
Cdd:NF033858  456 HFMNEA-ERCDRISLMHAGRVLASDTPAAL 484
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 32-204 5.09e-13

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: 66.24  E-value: 5.09e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   32 SGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFegqvindvpaekrrVNTvfqnyslfpnmnvfdnvafgprlkkmse 111
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY--------------IDG---------------------------- 38

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  112 kdiqDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDEPLSALDYKLRKELQQELR-----NIQKR 186
Cdd:smart00382  39 ----EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrlllLLKSE 114

                          170
                   ....*....|....*...
gi 2753759418  187 LGITFVFVTHDQEEALAM 204
Cdd:smart00382 115 KNLTVILTTNDEKDLGPA 132
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
98-225 3.55e-10

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 60.90  E-value: 3.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  98 DNVAFGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDEPLSALDYKLRKELQ 177
Cdd:NF000106  105 ENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVW 184

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2753759418 178 QELRNIQkRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDI 225
Cdd:NF000106  185 DEVRSMV-RDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
GguA NF040905
sugar ABC transporter ATP-binding protein;
104-216 1.82e-06

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 49.79  E-value: 1.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 104 PRLKKMSEKDIQDKVKEMlglVKLSGFERR----------EISELSGGQQQRVAIARALANDPEVLLLDEPLSALD---- 169
Cdd:NF040905  364 ANLGKVSRRGVIDENEEI---KVAEEYRKKmniktpsvfqKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDvgak 440

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2753759418 170 ---YKLRKELQQElrniqkrlGITFVFVTHDQEEALAMSDWIFVMHDGLI 216
Cdd:NF040905  441 yeiYTIINELAAE--------GKGVIVISSELPELLGMCDRIYVMNEGRI 482
 
Name Accession Description Interval E-value
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
 4-346 3.04e-177

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 496.93  E-value: 3.04e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   4 KMPILEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEKRRVNT 83
Cdd:COG3842     2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  84 VFQNYSLFPNMNVFDNVAFGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDE 163
Cdd:COG3842    82 VFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 164 PLSALDYKLRKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDEPINHFVADFIGETNI 243
Cdd:COG3842   162 PLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGEANL 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 244 VPGIM--KYDYLVHFVGKDFE-NVDAGMRPNERVEVVLRPEDLDLTDPAN-GKLVVTIQDQLFRGDYYEITAVDDDMNTW 319
Cdd:COG3842   242 LPGTVlgDEGGGVRTGGRTLEvPADAGLAAGGPVTVAIRPEDIRLSPEGPeNGLPGTVEDVVFLGSHVRYRVRLGDGQEL 321

                         330       340       350
                  ....*....|....*....|....*....|.
gi 2753759418 320 QVQATNPA----TVGARVGLTFDPEDIHIMR 346
Cdd:COG3842   322 VVRVPNRAalplEPGDRVGLSWDPEDVVVLP 352
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
1-283 2.87e-139

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 401.25  E-value: 2.87e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   1 MVEKMPILEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEKRR 80
Cdd:PRK09452    8 PSSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRH 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  81 VNTVFQNYSLFPNMNVFDNVAFGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLL 160
Cdd:PRK09452   88 VNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLL 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 161 LDEPLSALDYKLRKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDEPINHFVADFIGE 240
Cdd:PRK09452  168 LDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIGE 247

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 2753759418 241 TNIVPGIMK-----YDYLVHFVGKDFEN-VDAGMRPNERVEVVLRPEDL 283
Cdd:PRK09452  248 INIFDATVIerldeQRVRANVEGRECNIyVNFAVEPGQKLHVLLRPEDL 296
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
 5-344 1.48e-137

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


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 395.98  E-value: 1.48e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   5 MPILEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEKRRVNTV 84
Cdd:COG3839     1 MASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIAMV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  85 FQNYSLFPNMNVFDNVAFGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDEP 164
Cdd:COG3839    81 FQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 165 LSALDYKLRKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDEPINHFVADFIGE--TN 242
Cdd:COG3839   161 LSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGFIGSppMN 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 243 IVPGIMKyDYLVHFVGKDFE-NVDAGMRPNERVEVVLRPEDLDLTDPANGKLVVTIQDQLFRGDYYEITA-VDDDMNTWQ 320
Cdd:COG3839   241 LLPGTVE-GGGVRLGGVRLPlPAALAAAAGGEVTLGIRPEHLRLADEGDGGLEATVEVVEPLGSETLVHVrLGGQELVAR 319

                         330       340
                  ....*....|....*....|....
gi 2753759418 321 VQATNPATVGARVGLTFDPEDIHI 344
Cdd:COG3839   320 VPGDTRLRPGDTVRLAFDPERLHL 343
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
 8-239 7.38e-135

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: 384.67  E-value: 7.38e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   8 LEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEKRRVNTVFQN 87
Cdd:cd03300     1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  88 YSLFPNMNVFDNVAFGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDEPLSA 167
Cdd:cd03300    81 YALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2753759418 168 LDYKLRKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDEPINHFVADFIG 239
Cdd:cd03300   161 LDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
 8-344 7.61e-126

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


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 366.01  E-value: 7.61e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   8 LEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVIN-DVPAEKRRVNTVFQ 86
Cdd:COG1118     3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFtNLPPRERRVGFVFQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  87 NYSLFPNMNVFDNVAFGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDEPLS 166
Cdd:COG1118    83 HYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFG 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 167 ALDYKLRKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDEPINHFVADFIGETNIVPG 246
Cdd:COG1118   163 ALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLGCVNVLRG 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 247 IMKyDYLVHFVGKDFENVDAGmrPNERVEVVLRPEDLDLTDPANGK--LVVTIQDQLFRGDYYEITAVDDDMNTWQVQA- 323
Cdd:COG1118   243 RVI-GGQLEADGLTLPVAEPL--PDGPAVAGVRPHDIEVSREPEGEntFPATVARVSELGPEVRVELKLEDGEGQPLEAe 319

                         330       340
                  ....*....|....*....|....*...
gi 2753759418 324 -------TNPATVGARVGLTFDPEDIHI 344
Cdd:COG1118   320 vtkeawaELGLAPGDPVYLRPRPARVFL 347
PhnT2 TIGR03265
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ...
 5-335 1.63e-110

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: 327.38  E-value: 1.63e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   5 MPILEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEKRRVNTV 84
Cdd:TIGR03265   2 SPYLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYGIV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  85 FQNYSLFPNMNVFDNVAFGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDEP 164
Cdd:TIGR03265  82 FQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 165 LSALDYKLRKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDEPINHFVADFIGETNIV 244
Cdd:TIGR03265 162 LSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVGEVNWL 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 245 PGIMKYDYLVHFVGKDFENVDAGMRPNERVEVVLRPED--LDLTDPANGKLVVTIQDQLFRGDYYEITAVDDDMNTWQVQ 322
Cdd:TIGR03265 242 PGTRGGGSRARVGGLTLACAPGLAQPGASVRLAVRPEDirVSPAGNAANLLLARVEDMEFLGAFYRLRLRLEGLPGQALV 321

                         330
                  ....*....|...
gi 2753759418 323 ATNPATVGARVGL 335
Cdd:TIGR03265 322 ADVSASEVERLGI 334
potA TIGR01187
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ...
 38-339 1.49e-109

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: 324.06  E-value: 1.49e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  38 LLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEKRRVNTVFQNYSLFPNMNVFDNVAFGPRLKKMSEKDIQDK 117
Cdd:TIGR01187   1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 118 VKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDEPLSALDYKLRKELQQELRNIQKRLGITFVFVTHD 197
Cdd:TIGR01187  81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 198 QEEALAMSDWIFVMHDGLIQQNGTPEDIYDEPINHFVADFIGETNIVPGIMKY---DYLV-HFVGKDFENVDAGM--RPN 271
Cdd:TIGR01187 161 QEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVFEATVIErksEQVVlAGVEGRRCDIYTDVpvEKD 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2753759418 272 ERVEVVLRPEDLDL--TDPANG--KLVVTIQDQLFRGD----YYEITAVDDDMNTWQVQATNPA---TVGARVGLTFDP 339
Cdd:TIGR01187 241 QPLHVVLRPEKIVIeeEDEANSsnAIIGHVIDITYLGMtlevHVRLETGQKVLVSEFFNEDDPHmspSIGDRVGLTWHP 319
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
 8-220 3.70e-108

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: 316.00  E-value: 3.70e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   8 LEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEKRRVNTVFQN 87
Cdd:cd03259     1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVFQD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  88 YSLFPNMNVFDNVAFGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDEPLSA 167
Cdd:cd03259    81 YALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2753759418 168 LDYKLRKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNG 220
Cdd:cd03259   161 LDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
 5-240 5.39e-98

ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213263 [Multi-domain]  Cd Length: 239  Bit Score: 291.17  E-value: 5.39e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   5 MPIlEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEKRRVNTV 84
Cdd:cd03296     1 MSI-EVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  85 FQNYSLFPNMNVFDNVAFGPRLKKMSEK----DIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLL 160
Cdd:cd03296    80 FQHYALFRHMTVFDNVAFGLRVKPRSERppeaEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 161 LDEPLSALDYKLRKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDEPINHFVADFIGE 240
Cdd:cd03296   160 LDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFLGE 239
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
5-310 3.47e-94

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 285.82  E-value: 3.47e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   5 MPIlEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEKRRVNTV 84
Cdd:PRK10851    1 MSI-EIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  85 FQNYSLFPNMNVFDNVAFG----PRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLL 160
Cdd:PRK10851   80 FQHYALFRHMTVFDNIAFGltvlPRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 161 LDEPLSALDYKLRKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDEPINHFVADFIGE 240
Cdd:PRK10851  160 LDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMGE 239

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2753759418 241 TNIVPGIMKYDYLvhFVGKDFENVDAGMRPNERVEVVLRPEDLDLTDPAN--GKLVVTIQDQLFRGDYYEIT 310
Cdd:PRK10851  240 VNRLQGTIRGGQF--HVGAHRWPLGYTPAYQGPVDLFLRPWEVDISRRTSldSPLPVQVLEVSPKGHYWQLV 309
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
 1-211 6.86e-94

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


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 281.59  E-value: 6.86e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   1 MVEKMPILEFSKVALSF----GDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDvPA 76
Cdd:COG1116     1 MSAAAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG-PG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  77 EKRRVntVFQNYSLFPNMNVFDNVAFGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDP 156
Cdd:COG1116    80 PDRGV--VFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDP 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2753759418 157 EVLLLDEPLSALDYKLRKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVM 211
Cdd:COG1116   158 EVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVL 212
3a0106s01 TIGR00968
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
 8-244 2.62e-93

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


Pssm-ID: 130041 [Multi-domain]  Cd Length: 237  Bit Score: 279.38  E-value: 2.62e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   8 LEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEKRRVNTVFQN 87
Cdd:TIGR00968   1 IEIANISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARDRKIGFVFQH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  88 YSLFPNMNVFDNVAFGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDEPLSA 167
Cdd:TIGR00968  81 YALFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGA 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2753759418 168 LDYKLRKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDEPINHFVADFIGETNIV 244
Cdd:TIGR00968 161 LDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLGEVNVL 237
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
8-322 9.34e-93

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 281.99  E-value: 9.34e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   8 LEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEKRRVNTVFQN 87
Cdd:PRK11432    7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMVFQS 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  88 YSLFPNMNVFDNVAFGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDEPLSA 167
Cdd:PRK11432   87 YALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSN 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 168 LDYKLRKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDEPINHFVADFIGETNIVPGI 247
Cdd:PRK11432  167 LDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMGDANIFPAT 246

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2753759418 248 MKYDYlVHFVGKDF--ENVDAGMRPNERVEVVLRPEDLDLTDPANGKLVVTIQDQLFRGDYYEITAvdddmnTWQVQ 322
Cdd:PRK11432  247 LSGDY-VDIYGYRLprPAAFAFNLPDGECTVGVRPEAITLSEQGEESQRCTIKHVAYMGPQYEVTV------DWHGQ 316
OpuBA COG1125
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ...
 9-240 3.62e-91

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


Pssm-ID: 440742 [Multi-domain]  Cd Length: 306  Bit Score: 276.20  E-value: 3.62e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   9 EFSKVALSFGD-TEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEK--RRVNTVF 85
Cdd:COG1125     3 EFENVTKRYPDgTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVElrRRIGYVI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  86 QNYSLFPNMNVFDNVAFGPRLKKMSEKDIQDKVKEMLGLVKL--SGFERREISELSGGQQQRVAIARALANDPEVLLLDE 163
Cdd:COG1125    83 QQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAADPPILLMDE 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2753759418 164 PLSALDYKLRKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDEPINHFVADFIGE 240
Cdd:COG1125   163 PFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADFVGA 239
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
 8-220 3.11e-88

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: 265.27  E-value: 3.11e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   8 LEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEKRRVNTVFQN 87
Cdd:cd03301     1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVFQN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  88 YSLFPNMNVFDNVAFGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDEPLSA 167
Cdd:cd03301    81 YALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2753759418 168 LDYKLRKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNG 220
Cdd:cd03301   161 LDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
tungstate_WtpC NF040840
tungstate ABC transporter ATP-binding protein WtpC;
23-286 1.08e-87

tungstate ABC transporter ATP-binding protein WtpC;


Pssm-ID: 468779 [Multi-domain]  Cd Length: 347  Bit Score: 268.87  E-value: 1.08e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  23 LKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEKRRVNTVFQNYSLFPNMNVFDNVAF 102
Cdd:NF040840   16 LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIAYVYQNYMLFPHKTVFENIAF 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 103 GPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDEPLSALDYKLRKELQQELRN 182
Cdd:NF040840   96 GLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALDVQTRDELIREMKR 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 183 IQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDEPINHFVADFIGETNIVPGIMKYDYLVHFVGKDFE 262
Cdd:NF040840  176 WHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVGFENIIEGVAEKGGEGTILDTGNI 255

                         250       260
                  ....*....|....*....|....
gi 2753759418 263 NVDAGMRPNERVEVVLRPEDLDLT 286
Cdd:NF040840  256 KIELPEEKKGKVRIGIRPEDITIS 279
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
 8-211 5.81e-85

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: 257.40  E-value: 5.81e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   8 LEFSKVALSFGD----TEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDvPAEKRRVnt 83
Cdd:cd03293     1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG-PGPDRGY-- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  84 VFQNYSLFPNMNVFDNVAFGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDE 163
Cdd:cd03293    78 VFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDE 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2753759418 164 PLSALDYKLRKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVM 211
Cdd:cd03293   158 PFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
5-291 1.10e-82

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 257.07  E-value: 1.10e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   5 MPILEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEKRRVNTV 84
Cdd:PRK11607   17 TPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMM 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  85 FQNYSLFPNMNVFDNVAFGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDEP 164
Cdd:PRK11607   97 FQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEP 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 165 LSALDYKLRKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDEPINHFVADFIGETNIV 244
Cdd:PRK11607  177 MGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNVF 256

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2753759418 245 PGIMKYDY----------LVHFVGKDfenVDAGMRPNERVEVVLRPEDLDLTD--PANG 291
Cdd:PRK11607  257 EGVLKERQedglvidspgLVHPLKVD---ADASVVDNVPVHVALRPEKIMLCEepPADG 312
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
 8-240 5.32e-82

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: 250.68  E-value: 5.32e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   8 LEFSKVALSFGDTE-VLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEK--RRVNTV 84
Cdd:cd03295     1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElrRKIGYV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  85 FQNYSLFPNMNVFDNVAFGPRLKKMSEKDIQDKVKEMLGLVKL--SGFERREISELSGGQQQRVAIARALANDPEVLLLD 162
Cdd:cd03295    81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2753759418 163 EPLSALDYKLRKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDEPINHFVADFIGE 240
Cdd:cd03295   161 EPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVGA 238
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
 22-243 7.41e-82

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: 249.95  E-value: 7.41e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  22 VLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEKRRVNTVFQNYSLFPNMNVFDNVA 101
Cdd:cd03299    14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVPQNYALFPHMTVYKNIA 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 102 FGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDEPLSALDYKLRKELQQELR 181
Cdd:cd03299    94 YGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELK 173

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2753759418 182 NIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDEPINHFVADFIGETNI 243
Cdd:cd03299   174 KIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLGFNNI 235
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
5-344 1.07e-80

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


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 251.30  E-value: 1.07e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   5 MPILEFSKVALSF-GDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDV-PAEkRRVN 82
Cdd:PRK11650    1 MAGLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELePAD-RDIA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  83 TVFQNYSLFPNMNVFDNVAFGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLD 162
Cdd:PRK11650   80 MVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFD 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 163 EPLSALDYKLRKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDEPINHFVADFIGE-- 240
Cdd:PRK11650  160 EPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASFIGSpa 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 241 TNIVPGIMKYDYLVHFVGKDFE---NVDAGMRPNERVEVVLRPEDLDLTDPAnGKLVVTIQ-------DQLFRGDyyeit 310
Cdd:PRK11650  240 MNLLDGRVSADGAAFELAGGIAlplGGGYRQYAGRKLTLGIRPEHIALSSAE-GGVPLTVDtvellgaDNLAHGR----- 313

                         330       340       350
                  ....*....|....*....|....*....|....
gi 2753759418 311 aVDDDMNTWQVQATNPATVGARVGLTFDPEDIHI 344
Cdd:PRK11650  314 -WGGQPLVVRLPHQERPAAGSTLWLHLPANQLHL 346
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
 6-238 1.94e-80

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: 246.43  E-value: 1.94e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   6 PILEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEK-----RR 80
Cdd:COG1127     4 PMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKElyelrRR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  81 VNTVFQNYSLFPNMNVFDNVAFGPR-LKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVL 159
Cdd:COG1127    84 IGMLFQGGALFDSLTVFENVAFPLReHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEIL 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2753759418 160 LLDEPLSALDYKLRKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDEPiNHFVADFI 238
Cdd:COG1127   164 LYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASD-DPWVRQFL 241
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
13-346 4.95e-76

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 239.55  E-value: 4.95e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  13 VALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEKRRVNTVFQNYSLFP 92
Cdd:PRK11000    9 VTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGMVFQSYALYP 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  93 NMNVFDNVAFGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDEPLSALDYKL 172
Cdd:PRK11000   89 HLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAAL 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 173 RKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDEPINHFVADFIG--ETNIVPgimky 250
Cdd:PRK11000  169 RVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGspKMNFLP----- 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 251 dylVHFVGKDFENVD---------------AGMRPNERVEVVLRPEDLDLTDPANGKLVVTIQ--DQLfrGD----YYEI 309
Cdd:PRK11000  244 ---VKVTATAIEQVQvelpnrqqvwlpvegRGVQVGANMSLGIRPEHLLPSDIADVTLEGEVQvvEQL--GNetqiHIQI 318

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 2753759418 310 TAVDDDMnTWQVQATNPATVGARVGLTFDPEDIHIMR 346
Cdd:PRK11000  319 PAIRQNL-VYRQNDVVLVEEGATFAIGLPPERCHLFR 354
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
 4-238 6.63e-74

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: 230.99  E-value: 6.63e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   4 KMPILEfskvalSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAE------ 77
Cdd:cd03294    27 KEEILK------KTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKelrelr 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  78 KRRVNTVFQNYSLFPNMNVFDNVAFGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPE 157
Cdd:cd03294   101 RKKISMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPD 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 158 VLLLDEPLSALDYKLRKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDEPINHFVADF 237
Cdd:cd03294   181 ILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREF 260


                  .
gi 2753759418 238 I 238
Cdd:cd03294   261 F 261
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
6-216 6.39e-73

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 226.85  E-value: 6.39e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   6 PILEFSKVALSFGD----TEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEKR-- 79
Cdd:COG1136     3 PLLELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELar 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  80 -RVNT---VFQNYSLFPNMNVFDNVAFGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALAND 155
Cdd:COG1136    83 lRRRHigfVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNR 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2753759418 156 PEVLLLDEPLSALDYKLRKELQQELRNIQKRLGITFVFVTHDqEEALAMSDWIFVMHDGLI 216
Cdd:COG1136   163 PKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHD-PELAARADRVIRLRDGRI 222
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
 8-226 2.61e-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: 225.29  E-value: 2.61e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   8 LEFSKVALSF-GDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEK--RRVNTV 84
Cdd:COG1122     1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElrRKVGLV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  85 FQN--YSLFpNMNVFDNVAFGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLD 162
Cdd:COG1122    81 FQNpdDQLF-APTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLD 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2753759418 163 EPLSALDYKLRKELQQELRNIQKRlGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIY 226
Cdd:COG1122   160 EPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVF 222
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
 25-220 3.20e-72

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: 224.48  E-value: 3.20e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  25 EIDLVLeSGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVIND------VPAEKRRVNTVFQNYSLFPNMNVFD 98
Cdd:cd03297    16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDsrkkinLPPQQRKIGLVFQQYALFPHLNVRE 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  99 NVAFGprLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDEPLSALDYKLRKELQQ 178
Cdd:cd03297    95 NLAFG--LKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLP 172

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2753759418 179 ELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNG 220
Cdd:cd03297   173 ELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
 7-229 3.52e-71

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


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 222.56  E-value: 3.52e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   7 ILEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAE----KRRVN 82
Cdd:COG1126     1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDinklRRKVG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  83 TVFQNYSLFPNMNVFDNVAFGPR-LKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLL 161
Cdd:COG1126    81 MVFQQFNLFPHLTVLENVTLAPIkVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLF 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2753759418 162 DEPLSALDyklrKELQQELRNIQKRL---GITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDEP 229
Cdd:COG1126   161 DEPTSALD----PELVGEVLDVMRDLakeGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENP 227
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
 8-237 3.89e-71

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: 222.38  E-value: 3.89e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   8 LEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDV-PAEK----RRVN 82
Cdd:cd03261     1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLsEAELyrlrRRMG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  83 TVFQNYSLFPNMNVFDNVAFGPRLK-KMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLL 161
Cdd:cd03261    81 MLFQSGALFDSLTVFENVAFPLREHtRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2753759418 162 DEPLSALDYKLRKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDEPiNHFVADF 237
Cdd:cd03261   161 DEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASD-DPLVRQF 235
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
 8-216 2.17e-70

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: 220.05  E-value: 2.17e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   8 LEFSKVALSFGD----TEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEKR---- 79
Cdd:cd03255     1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  80 --RVNTVFQNYSLFPNMNVFDNVAFGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPE 157
Cdd:cd03255    81 rrHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2753759418 158 VLLLDEPLSALDYKLRKELQQELRNIQKRLGITFVFVTHDQEEAlAMSDWIFVMHDGLI 216
Cdd:cd03255   161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
 8-214 3.69e-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: 217.83  E-value: 3.69e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   8 LEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVIND----VPAEKRRVNT 83
Cdd:cd03229     1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDledeLPPLRRRIGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  84 VFQNYSLFPNMNVFDNVAFGprlkkmsekdiqdkvkemlglvklsgferreiseLSGGQQQRVAIARALANDPEVLLLDE 163
Cdd:cd03229    81 VFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVLLLDE 126

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2753759418 164 PLSALDYKLRKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDG 214
Cdd:cd03229   127 PTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
 6-229 3.95e-70

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: 228.63  E-value: 3.95e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   6 PILEFSKVALSF-----GDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEK-- 78
Cdd:COG1123   259 PLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlr 338

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  79 ---RRVNTVFQN--YSLFPNMNVFDNVAFGPRL-KKMSEKDIQDKVKEMLGLVKLS-GFERREISELSGGQQQRVAIARA 151
Cdd:COG1123   339 elrRRVQMVFQDpySSLNPRMTVGDIIAEPLRLhGLLSRAERRERVAELLERVGLPpDLADRYPHELSGGQRQRVAIARA 418

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2753759418 152 LANDPEVLLLDEPLSALDYKLRKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDEP 229
Cdd:COG1123   419 LALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANP 496
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
 9-214 3.29e-68

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: 214.25  E-value: 3.29e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   9 EFSKVALSFGDTE--VLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEK--RRVNTV 84
Cdd:cd03225     1 ELKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKElrRKVGLV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  85 FQN--YSLFpNMNVFDNVAFGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLD 162
Cdd:cd03225    81 FQNpdDQFF-GPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLD 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2753759418 163 EPLSALDYKLRKELQQELRNIQKRlGITFVFVTHDQEEALAMSDWIFVMHDG 214
Cdd:cd03225   160 EPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDG 210
TauB COG4525
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
5-211 1.24e-67

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


Pssm-ID: 443596 [Multi-domain]  Cd Length: 262  Bit Score: 214.34  E-value: 1.24e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   5 MPILEFSKVALSFG----DTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDvPAEKRR 80
Cdd:COG4525     1 MSMLTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG-PGADRG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  81 VntVFQNYSLFPNMNVFDNVAFGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLL 160
Cdd:COG4525    80 V--VFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLL 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2753759418 161 LDEPLSALDYKLRKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVM 211
Cdd:COG4525   158 MDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVM 208
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
 7-225 1.64e-67

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: 213.75  E-value: 1.64e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   7 ILEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEK--RRVNTV 84
Cdd:COG1120     1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRElaRRIAYV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  85 FQNYSLFPNMNVFDNVAFG-----PRLKKMSEKDIQdKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVL 159
Cdd:COG1120    81 PQEPPAPFGLTVRELVALGryphlGLFGRPSAEDRE-AVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLL 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2753759418 160 LLDEPLSALDYKLRKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDI 225
Cdd:COG1120   160 LLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
proV TIGR01186
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ...
 18-244 8.00e-67

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: 215.87  E-value: 8.00e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  18 GDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDV-PAE-----KRRVNTVFQNYSLF 91
Cdd:TIGR01186   4 GGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQsPVElrevrRKKIGMVFQQFALF 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  92 PNMNVFDNVAFGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDEPLSALDYK 171
Cdd:TIGR01186  84 PHMTILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDPL 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2753759418 172 LRKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDEPINHFVADFIGETNIV 244
Cdd:TIGR01186 164 IRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGKVDLS 236
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
8-240 1.46e-66

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 210.77  E-value: 1.46e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   8 LEFSKVALSFGDTevLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEKRRVNTVFQN 87
Cdd:COG3840     2 LRLDDLTYRYGDF--PLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSMLFQE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  88 YSLFPNMNVFDNVAFG--PRLKkMSEKDiQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDEPL 165
Cdd:COG3840    80 NNLFPHLTVAQNIGLGlrPGLK-LTAEQ-RAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPF 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2753759418 166 SALDYKLRKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDEPINHFVADFIGE 240
Cdd:COG3840   158 SALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYLGI 232
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
8-225 1.16e-63

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 203.37  E-value: 1.16e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   8 LEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAE-KRRVNTVFQ 86
Cdd:COG1131     1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEvRRRIGYVPQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  87 NYSLFPNMNVFDNVAFGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDEPLS 166
Cdd:COG1131    81 EPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2753759418 167 ALDYKLRKELQQELRNIQKRlGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDI 225
Cdd:COG1131   161 GLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
7-199 1.26e-63

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 202.59  E-value: 1.26e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   7 ILEFSKVALSF-GDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEK-----RR 80
Cdd:COG2884     1 MIRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipylrRR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  81 VNTVFQNYSLFPNMNVFDNVAFGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLL 160
Cdd:COG2884    81 IGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLL 160

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2753759418 161 LDEPLSALDYKLRKELQQELRNIQkRLGITFVFVTHDQE 199
Cdd:COG2884   161 ADEPTGNLDPETSWEIMELLEEIN-RRGTTVLIATHDLE 198
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
 8-216 8.58e-63

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: 200.45  E-value: 8.58e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   8 LEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVIN----DVPAEKRRVNT 83
Cdd:cd03262     1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTddkkNINELRQKVGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  84 VFQNYSLFPNMNVFDNVAFGPR-LKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLD 162
Cdd:cd03262    81 VFQQFNLFPHLTVLENITLAPIkVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2753759418 163 EPLSALDYKLRKELQQELRNIQKRlGITFVFVTHDQEEALAMSDWIFVMHDGLI 216
Cdd:cd03262   161 EPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
 4-230 3.68e-61

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 197.23  E-value: 3.68e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   4 KMPILEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQvinDVPAEKRRVNT 83
Cdd:COG1121     3 MMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGK---PPRRARRRIGY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  84 VFQNYSL---FPnMNVFDNVAFG-----PRLKKMSEKDiQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALAND 155
Cdd:COG1121    80 VPQRAEVdwdFP-ITVRDVVLMGrygrrGLFRRPSRAD-REAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQD 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2753759418 156 PEVLLLDEPLSALDYKLRKELQQELRNIQKRlGITFVFVTHDQEEALAMSDWIFVMHDGLIQQnGTPEDIYDEPI 230
Cdd:COG1121   158 PDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRGLVAH-GPPEEVLTPEN 230
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
7-238 4.50e-61

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 196.85  E-value: 4.50e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   7 ILEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEKRRVN---- 82
Cdd:PRK09493    1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIRqeag 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  83 TVFQNYSLFPNMNVFDNVAFGP-RLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLL 161
Cdd:PRK09493   81 MVFQQFYLFPHLTALENVMFGPlRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLF 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2753759418 162 DEPLSALDYKLRKELQQELRNIQKRlGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDEPINHFVADFI 238
Cdd:PRK09493  161 DEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFL 236
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
 7-229 8.49e-61

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: 195.88  E-value: 8.49e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   7 ILEFSKVALSFGDT----EVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVP-----AE 77
Cdd:cd03258     1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSgkelrKA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  78 KRRVNTVFQNYSLFPNMNVFDNVAFGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPE 157
Cdd:cd03258    81 RRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2753759418 158 VLLLDEPLSALDYKLRKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDEP 229
Cdd:cd03258   161 VLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANP 232
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
 6-229 2.27e-60

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: 203.21  E-value: 2.27e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   6 PILEFSKVALSF--GDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADA---GKIFFEGQVINDVPAEKR- 79
Cdd:COG1123     3 PLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALRg 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  80 -RVNTVFQN--YSLFPnMNVFDNVAFGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDP 156
Cdd:COG1123    83 rRIGMVFQDpmTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDP 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2753759418 157 EVLLLDEPLSALDYKLRKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDEP 229
Cdd:COG1123   162 DLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAP 234
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
 12-225 1.96e-59

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: 196.48  E-value: 1.96e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  12 KVALSFGDTEVlkEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVIND------VPAEKRRVNTVF 85
Cdd:COG4148     6 DFRLRRGGFTL--DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDsargifLPPHRRRIGYVF 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  86 QNYSLFPNMNVFDNVAFGPRLKKMSEKDIQ-DKVKEMLGLVKLsgFERReISELSGGQQQRVAIARALANDPEVLLLDEP 164
Cdd:COG4148    84 QEARLFPHLSVRGNLLYGRKRAPRAERRISfDEVVELLGIGHL--LDRR-PATLSGGERQRVAIGRALLSSPRLLLMDEP 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2753759418 165 LSALDYKLRKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDI 225
Cdd:COG4148   161 LAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEV 221
ECF_ATPase_2 TIGR04521
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
 20-229 6.28e-59

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: 192.67  E-value: 6.28e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  20 TEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEK-----RRVNTVFQN--YSLFP 92
Cdd:TIGR04521  18 KKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKlkdlrKKVGLVFQFpeHQLFE 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  93 NmNVFDNVAFGPRLKKMSEKDIQDKVKEMLGLVKLSGfERREIS--ELSGGQQQRVAIARALANDPEVLLLDEPLSALDY 170
Cdd:TIGR04521  98 E-TVYKDIAFGPKNLGLSEEEAEERVKEALELVGLDE-EYLERSpfELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDP 175

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2753759418 171 KLRKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDEP 229
Cdd:TIGR04521 176 KGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDV 234
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...
 5-225 2.14e-58

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: 190.25  E-value: 2.14e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   5 MPILEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEKR----- 79
Cdd:COG0411     2 DPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIarlgi 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  80 -RvnTvFQNYSLFPNMNVFDNVA---------------FGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQ 143
Cdd:COG0411    82 aR--T-FQNPRLFPELTVLENVLvaaharlgrgllaalLRLPRARREEREARERAEELLERVGLADRADEPAGNLSYGQQ 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 144 QRVAIARALANDPEVLLLDEPLSALDYKLRKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDG-LIQQnGTP 222
Cdd:COG0411   159 RRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGrVIAE-GTP 237


                  ...
gi 2753759418 223 EDI 225
Cdd:COG0411   238 AEV 240
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
7-241 3.33e-58

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 192.60  E-value: 3.33e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   7 ILEFSKVALSF----GDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVP-----AE 77
Cdd:COG1135     1 MIELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSerelrAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  78 KRRVNTVFQNYSLFPNMNVFDNVAFGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPE 157
Cdd:COG1135    81 RRKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 158 VLLLDEPLSALDYKLRKELQQELRNIQKRLGITFVFVTHDqeealaMS------DWIFVMHDGLIQQNGTPEDIYDEPIN 231
Cdd:COG1135   161 VLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHE------MDvvrricDRVAVLENGRIVEQGPVLDVFANPQS 234

                         250
                  ....*....|
gi 2753759418 232 HFVADFIGET 241
Cdd:COG1135   235 ELTRRFLPTV 244
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
 7-216 7.67e-58

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: 188.10  E-value: 7.67e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   7 ILEFSKVALSF----GDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEKRR-- 80
Cdd:cd03257     1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKir 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  81 ---VNTVFQNY--SLFPNMNVFDNVAFGPRLKKMSEKDIQDKVKEMLGLVKL---SGFERREISELSGGQQQRVAIARAL 152
Cdd:cd03257    81 rkeIQMVFQDPmsSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVglpEEVLNRYPHELSGGQRQRVAIARAL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2753759418 153 ANDPEVLLLDEPLSALDYKLRKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLI 216
Cdd:cd03257   161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
 8-225 9.24e-58

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: 188.47  E-value: 9.24e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   8 LEFSKVALSFG----DTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVP--AEKRRV 81
Cdd:COG1124     2 LEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRrkAFRRRV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  82 NTVFQNY--SLFPNMNVFDNVAfGPrLKKMSEKDIQDKVKEMLGLVKL-SGFERREISELSGGQQQRVAIARALANDPEV 158
Cdd:COG1124    82 QMVFQDPyaSLHPRHTVDRILA-EP-LRIHGLPDREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEPEL 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2753759418 159 LLLDEPLSALDYKLRKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDI 225
Cdd:COG1124   160 LLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADL 226
PhnC COG3638
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ...
 6-228 3.11e-57

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


Pssm-ID: 442855 [Multi-domain]  Cd Length: 249  Bit Score: 187.19  E-value: 3.11e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   6 PILEFSKVALSF-GDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEK-----R 79
Cdd:COG3638     1 PMLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAlrrlrR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  80 RVNTVFQNYSLFPNMNVFDNVAFGpRLKKMS----------EKDIQdKVKEMLGLVKLSGFERREISELSGGQQQRVAIA 149
Cdd:COG3638    81 RIGMIFQQFNLVPRLSVLTNVLAG-RLGRTStwrsllglfpPEDRE-RALEALERVGLADKAYQRADQLSGGQQQRVAIA 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2753759418 150 RALANDPEVLLLDEPLSALDYKLRKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDE 228
Cdd:COG3638   159 RALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAELTDA 237
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
8-214 1.27e-56

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 184.25  E-value: 1.27e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   8 LEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEK--RRVNTVF 85
Cdd:COG4619     1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwrRQVAYVP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  86 QNYSLFPNMnVFDNVAFGPRLKKmsEKDIQDKVKEMLGLVKLS-GFERREISELSGGQQQRVAIARALANDPEVLLLDEP 164
Cdd:COG4619    81 QEPALWGGT-VRDNLPFPFQLRE--RKFDRERALELLERLGLPpDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEP 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2753759418 165 LSALDYKLRKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDG 214
Cdd:COG4619   158 TSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAG 207
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
 8-225 7.59e-56

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: 182.77  E-value: 7.59e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   8 LEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQA-----DAGKIFFEGQVIN----DVPAEK 78
Cdd:cd03260     1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYdldvDVLELR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  79 RRVNTVFQNYSLFPnMNVFDNVAFGPRLKKMSEKDIQDK-VKEMLGLVKLSGFE--RREISELSGGQQQRVAIARALAND 155
Cdd:cd03260    81 RRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELDErVEEALRKAALWDEVkdRLHALGLSGGQQQRLCLARALANE 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 156 PEVLLLDEPLSALDYKLRKELQQELRNIQKRlgITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDI 225
Cdd:cd03260   160 PEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
 8-205 1.57e-55

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


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 181.53  E-value: 1.57e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   8 LEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADA---GKIFFEGQVINDVPAEKRRVNTV 84
Cdd:COG4136     2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFsasGEVLLNGRRLTALPAEQRRIGIL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  85 FQNYSLFPNMNVFDNVAFG--PRLKKmSEKdiQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLD 162
Cdd:COG4136    82 FQDDLLFPHLSVGENLAFAlpPTIGR-AQR--RARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLD 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2753759418 163 EPLSALDYKLRKELQQELRNIQKRLGITFVFVTHDQEEALAMS 205
Cdd:COG4136   159 EPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAPAAG 201
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
 8-225 3.94e-55

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: 181.10  E-value: 3.94e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   8 LEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEKR------RV 81
Cdd:cd03219     1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIarlgigRT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  82 ntvFQNYSLFPNMNVFDNVAFGPRLKK----------MSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARA 151
Cdd:cd03219    81 ---FQIPRLFPELTVLENVMVAAQARTgsglllararREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARA 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2753759418 152 LANDPEVLLLDEPLSALDYKLRKELQQELRNIqKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDI 225
Cdd:cd03219   158 LATDPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEV 230
FtsE TIGR02673
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ...
 7-214 7.25e-55

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: 179.75  E-value: 7.25e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   7 ILEFSKVALSF-GDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVIN-----DVPAEKRR 80
Cdd:TIGR02673   1 MIEFHNVSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNrlrgrQLPLLRRR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  81 VNTVFQNYSLFPNMNVFDNVAFGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLL 160
Cdd:TIGR02673  81 IGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLL 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2753759418 161 LDEPLSALDYKLRKELQQELRNIQKRlGITFVFVTHDQEEALAMSDWIFVMHDG 214
Cdd:TIGR02673 161 ADEPTGNLDPDLSERILDLLKRLNKR-GTTVIVATHDLSLVDRVAHRVIILDDG 213
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
 8-232 1.31e-54

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: 180.07  E-value: 1.31e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   8 LEFSKVALSFGD-TEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEK-----RRV 81
Cdd:cd03256     1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrqlrRQI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  82 NTVFQNYSLFPNMNVFDNVAFGpRLKKMS----------EKDIQdKVKEMLGLVKLSGFERREISELSGGQQQRVAIARA 151
Cdd:cd03256    81 GMIFQQFNLIERLSVLENVLSG-RLGRRStwrslfglfpKEEKQ-RALAALERVGLLDKAYQRADQLSGGQQQRVAIARA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 152 LANDPEVLLLDEPLSALDYKLRKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDEPIN 231
Cdd:cd03256   159 LMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTDEVLD 238


                  .
gi 2753759418 232 H 232
Cdd:cd03256   239 E 239
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
 8-216 3.26e-54

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: 176.82  E-value: 3.26e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   8 LEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAE-KRRVNTVFQ 86
Cdd:cd03230     1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEvKRRIGYLPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  87 NYSLFPNMNVFDNVafgprlkkmsekdiqdkvkemlglvklsgferreisELSGGQQQRVAIARALANDPEVLLLDEPLS 166
Cdd:cd03230    81 EPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTS 124

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2753759418 167 ALDYKLRKELQQELRNIQKRlGITFVFVTHDQEEALAMSDWIFVMHDGLI 216
Cdd:cd03230   125 GLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
ECF_ATPase_1 TIGR04520
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
 8-226 1.49e-53

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: 178.39  E-value: 1.49e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   8 LEFSKVALSFGDTE--VLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEG------QVINDVpaeKR 79
Cdd:TIGR04520   1 IEVENVSFSYPESEkpALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGldtldeENLWEI---RK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  80 RVNTVFQNyslfPNmNVF------DNVAFGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALA 153
Cdd:TIGR04520  78 KVGMVFQN----PD-NQFvgatveDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLA 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2753759418 154 NDPEVLLLDEPLSALDYKLRKELQQELRNIQKRLGITFVFVTHDQEEAlAMSDWIFVMHDGLIQQNGTPEDIY 226
Cdd:TIGR04520 153 MRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEA-VLADRVIVMNKGKIVAEGTPREIF 224
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
 16-260 2.30e-53

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: 176.97  E-value: 2.30e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  16 SFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAE-KRRVNTVFQNYSLFPNM 94
Cdd:COG4555    10 KYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREaRRQIGVLPDERGLYDRL 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  95 NVFDNVAFGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDEPLSALDYKLRK 174
Cdd:COG4555    90 TVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARR 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 175 ELQQELRNIqKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDEpinhfvadfIGETNIvpgimkYDYLV 254
Cdd:COG4555   170 LLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREE---------IGEENL------EDAFV 233


                  ....*.
gi 2753759418 255 HFVGKD 260
Cdd:COG4555   234 ALIGSE 239
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
7-205 2.68e-53

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 177.20  E-value: 2.68e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   7 ILEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEKrrvNTVFQ 86
Cdd:PRK11248    1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER---GVVFQ 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  87 NYSLFPNMNVFDNVAFGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDEPLS 166
Cdd:PRK11248   78 NEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFG 157

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2753759418 167 ALDYKLRKELQQELRNIQKRLGITFVFVTHDQEEALAMS 205
Cdd:PRK11248  158 ALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMA 196
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
 9-219 8.05e-53

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: 174.64  E-value: 8.05e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   9 EFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQvinDVPAEKRRVNTVFQNY 88
Cdd:cd03235     1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK---PLEKERKRIGYVPQRR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  89 SL---FPnMNVFDNVAFGPR-----LKKMSEKDIQdKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLL 160
Cdd:cd03235    78 SIdrdFP-ISVRDVVLMGLYghkglFRRLSKADKA-KVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLL 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2753759418 161 LDEPLSALDYKLRKELQQELRNIQkRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQN 219
Cdd:cd03235   156 LDEPFAGVDPKTQEDIYELLRELR-REGMTILVVTHDLGLVLEYFDRVLLLNRTVVASG 213
HisP COG4598
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
16-229 3.31e-51

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


Pssm-ID: 443652 [Multi-domain]  Cd Length: 259  Bit Score: 171.91  E-value: 3.31e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  16 SFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVI--------NDVPAEKR-------R 80
Cdd:COG4598    17 SFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIrlkpdrdgELVPADRRqlqrirtR 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  81 VNTVFQNYSLFPNMNVFDNVAFGP-RLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVL 159
Cdd:COG4598    97 LGMVFQSFNLWSHMTVLENVIEAPvHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIARALAMEPEVM 176

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2753759418 160 LLDEPLSALDyklrKELQQE-LRNIQK--RLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDEP 229
Cdd:COG4598   177 LFDEPTSALD----PELVGEvLKVMRDlaEEGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGNP 245
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
 23-214 4.94e-51

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: 170.72  E-value: 4.94e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  23 LKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDvPAEKRRVntVFQNYSLFPNMNVFDNVAF 102
Cdd:TIGR01184   1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITE-PGPDRMV--VFQNYSLLPWLTVRENIAL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 103 GPR--LKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDEPLSALDYKLRKELQQEL 180
Cdd:TIGR01184  78 AVDrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEEL 157

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2753759418 181 RNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDG 214
Cdd:TIGR01184 158 MQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
 9-220 5.38e-51

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: 168.77  E-value: 5.38e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   9 EFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEK--RRVNTVFQ 86
Cdd:cd03214     1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKElaRKIAYVPQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  87 nyslfpnmnvfdnvafgprlkkmsekdiqdkvkeMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDEPLS 166
Cdd:cd03214    81 ----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTS 126

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2753759418 167 ALDYKLRKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNG 220
Cdd:cd03214   127 HLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
3a0107s01c2 TIGR00972
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ...
 7-238 7.48e-51

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: 170.55  E-value: 7.48e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   7 ILEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILK-------LISGQlqADAGKIFFEGQVIN----DVP 75
Cdd:TIGR00972   1 AIEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRslnrmndLVPGV--RIEGKVLFDGQDIYdkkiDVV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  76 AEKRRVNTVFQNYSLFPnMNVFDNVAFGPRLKKM-SEKDIQDKVKEMLGLVKL----------SGFErreiseLSGGQQQ 144
Cdd:TIGR00972  79 ELRRRVGMVFQKPNPFP-MSIYDNIAYGPRLHGIkDKKELDEIVEESLKKAALwdevkdrlhdSALG------LSGGQQQ 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 145 RVAIARALANDPEVLLLDEPLSALDYKLRKELQQELRNIQKRLgiTFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPED 224
Cdd:TIGR00972 152 RLCIARALAVEPEVLLLDEPTSALDPIATGKIEELIQELKKKY--TIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQ 229

                         250
                  ....*....|....
gi 2753759418 225 IYDEPINHFVADFI 238
Cdd:TIGR00972 230 IFTNPKEKRTEDYI 243
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
 7-229 2.18e-50

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: 172.60  E-value: 2.18e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   7 ILEFSKvalSFGDTEVlkEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVIND------VPAEKRR 80
Cdd:TIGR02142   2 SARFSK---RLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgifLPPEKRR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  81 VNTVFQNYSLFPNMNVFDNVAFGPRLKKMSEKDIQ-DKVKEMLGLVKLSgfeRREISELSGGQQQRVAIARALANDPEVL 159
Cdd:TIGR02142  77 IGYVFQEARLFPHLSVRGNLRYGMKRARPSERRISfERVIELLGIGHLL---GRLPGRLSGGEKQRVAIGRALLSSPRLL 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 160 LLDEPLSALDYKLRKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDEP 229
Cdd:TIGR02142 154 LMDEPLAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASP 223
ABC_phnC TIGR02315
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ...
 7-232 1.97e-49

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: 166.70  E-value: 1.97e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   7 ILEFSKVALSFG-DTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEK-----RR 80
Cdd:TIGR02315   1 MLEVENLSKVYPnGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKlrklrRR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  81 VNTVFQNYSLFPNMNVFDNV-----AFGPRLKKM----SEKDIQdKVKEMLGLVKLSGFERREISELSGGQQQRVAIARA 151
Cdd:TIGR02315  81 IGMIFQHYNLIERLTVLENVlhgrlGYKPTWRSLlgrfSEEDKE-RALSALERVGLADKAYQRADQLSGGQQQRVAIARA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 152 LANDPEVLLLDEPLSALDYKLRKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDEPIN 231
Cdd:TIGR02315 160 LAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDDEVLR 239


                  .
gi 2753759418 232 H 232
Cdd:TIGR02315 240 H 240
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
 1-238 7.89e-49

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


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 165.60  E-value: 7.89e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   1 MVEKMPILEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILK-------LISGQlQADaGKIFFEGQVIN- 72
Cdd:COG1117     5 ASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRclnrmndLIPGA-RVE-GEILLDGEDIYd 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  73 ---DVPAEKRRVNTVFQNYSLFPnMNVFDNVAFGPRLKKM-SEKDIQDKVKEML---GL---VK--L--SGFErreiseL 138
Cdd:COG1117    83 pdvDVVELRRRVGMVFQKPNPFP-KSIYDNVAYGLRLHGIkSKSELDEIVEESLrkaALwdeVKdrLkkSALG------L 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 139 SGGQQQRVAIARALANDPEVLLLDEPLSALD----YKLrKELQQELRniqKRLgiTFVFVTHDQEEALAMSDWIFVMHDG 214
Cdd:COG1117   156 SGGQQQRLCIARALAVEPEVLLMDEPTSALDpistAKI-EELILELK---KDY--TIVIVTHNMQQAARVSDYTAFFYLG 229

                         250       260
                  ....*....|....*....|....*
gi 2753759418 215 -LIQQNGTpEDIYDEPINHFVADFI 238
Cdd:COG1117   230 eLVEFGPT-EQIFTNPKDKRTEDYI 253
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
 23-229 1.23e-48

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 166.35  E-value: 1.23e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  23 LKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEK------RRVNTVFQnyslFPNMNV 96
Cdd:PRK13634   23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKklkplrKKVGIVFQ----FPEHQL 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  97 FD-----NVAFGPRLKKMSEKDIQDKVKEMLGLVKLSGfERREIS--ELSGGQQQRVAIARALANDPEVLLLDEPLSALD 169
Cdd:PRK13634   99 FEetvekDICFGPMNFGVSEEDAKQKAREMIELVGLPE-ELLARSpfELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLD 177

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 170 YKLRKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDEP 229
Cdd:PRK13634  178 PKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP 237
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
 9-214 1.55e-48

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: 161.64  E-value: 1.55e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   9 EFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEKRRvntvfqny 88
Cdd:cd00267     1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELR-------- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  89 slfpnmnvfDNVAFgprlkkmsekdiqdkvkemlglvklsgferreISELSGGQQQRVAIARALANDPEVLLLDEPLSAL 168
Cdd:cd00267    73 ---------RRIGY--------------------------------VPQLSGGQRQRVALARALLLNPDLLLLDEPTSGL 111

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2753759418 169 DYKLRKELQQELRNIQKRlGITFVFVTHDQEEALAMSDWIFVMHDG 214
Cdd:cd00267   112 DPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDG 156
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
 8-220 2.34e-48

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: 163.05  E-value: 2.34e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   8 LEFSKVALSFGDTEVlkEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEKRRVNTVFQN 87
Cdd:cd03298     1 VRLDKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  88 YSLFPNMNVFDNVAFG--PRLKkMSEKDiQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDEPL 165
Cdd:cd03298    79 NNLFAHLTVEQNVGLGlsPGLK-LTAED-RQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPF 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2753759418 166 SALDYKLRKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNG 220
Cdd:cd03298   157 AALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
 8-225 1.15e-47

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: 172.33  E-value: 1.15e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   8 LEFSKVALSFGDTE--VLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDV-PAEKRR-VNT 83
Cdd:COG2274   474 IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIdPASLRRqIGV 553

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  84 VFQNYSLFpNMNVFDNVAFGprLKKMSEKDIQdKVKEMLGL----VKL-SGFERReISE----LSGGQQQRVAIARALAN 154
Cdd:COG2274   554 VLQDVFLF-SGTIRENITLG--DPDATDEEII-EAARLAGLhdfiEALpMGYDTV-VGEggsnLSGGQRQRLAIARALLR 628

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2753759418 155 DPEVLLLDEPLSALDYKLRKELQQELRNIQKrlGITFVFVTHDqEEALAMSDWIFVMHDGLIQQNGTPEDI 225
Cdd:COG2274   629 NPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHR-LSTIRLADRIIVLDKGRIVEDGTHEEL 696
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 23-166 1.28e-47

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: 158.97  E-value: 1.28e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  23 LKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVIN--DVPAEKRRVNTVFQNYSLFPNMNVFDNV 100
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTddERKSLRKEIGYVFQDPQLFPRLTVRENL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 101 AFGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREI----SELSGGQQQRVAIARALANDPEVLLLDEPLS 166
Cdd:pfam00005  81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVgerpGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
 8-216 1.66e-47

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: 160.65  E-value: 1.66e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   8 LEFSKVALSF-GDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVIND-----VPAEKRRV 81
Cdd:cd03292     1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDlrgraIPYLRRKI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  82 NTVFQNYSLFPNMNVFDNVAFGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLL 161
Cdd:cd03292    81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2753759418 162 DEPLSALDYKLRKELQQELRNIQKRlGITFVFVTHDQEEALAMSDWIFVMHDGLI 216
Cdd:cd03292   161 DEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
 7-229 5.22e-47

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: 162.92  E-value: 5.22e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   7 ILEFSKVALSF----GDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQA---DAGKIFFEGQVINDVPAEK- 78
Cdd:COG0444     1 LLEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKEl 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  79 -----RRVNTVFQN-Y-SLFPNMNVFDNVAFGPRL-KKMSEKDIQDKVKEMLGLVKLSGFERREIS---ELSGGQQQRVA 147
Cdd:COG0444    81 rkirgREIQMIFQDpMtSLNPVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLPDPERRLDRyphELSGGMRQRVM 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 148 IARALANDPEVLLLDEPLSALDYKLRKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYD 227
Cdd:COG0444   161 IARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELFE 240


                  ..
gi 2753759418 228 EP 229
Cdd:COG0444   241 NP 242
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
 8-214 1.16e-46

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: 157.16  E-value: 1.16e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   8 LEFSKVALSFGDT--EVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEKRR--VNT 83
Cdd:cd03228     1 IEFKNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRknIAY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  84 VFQNYSLFpNMNVFDNVafgprlkkmsekdiqdkvkemlglvklsgferreiseLSGGQQQRVAIARALANDPEVLLLDE 163
Cdd:cd03228    81 VPQDPFLF-SGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDE 122

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2753759418 164 PLSALDYKLRKELQQELRNIQKrlGITFVFVTHDqEEALAMSDWIFVMHDG 214
Cdd:cd03228   123 ATSALDPETEALILEALRALAK--GKTVIVIAHR-LSTIRDADRIIVLDDG 170
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
 9-241 1.25e-46

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 162.28  E-value: 1.25e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   9 EFSKVALSF----GDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVI-----NDVPAEKR 79
Cdd:PRK11153    3 ELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLtalseKELRKARR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  80 RVNTVFQNYSLFPNMNVFDNVAFGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVL 159
Cdd:PRK11153   83 QIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVL 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 160 LLDEPLSALDYKLRKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDEPiNHFVA-DFI 238
Cdd:PRK11153  163 LCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHP-KHPLTrEFI 241


                  ...
gi 2753759418 239 GET 241
Cdd:PRK11153  242 QST 244
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
 26-229 2.02e-46

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


Pssm-ID: 443658 [Multi-domain]  Cd Length: 329  Bit Score: 161.44  E-value: 2.02e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  26 IDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEK-----RRVNTVFQN-Y-SLFPNMNVFD 98
Cdd:COG4608    37 VSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRElrplrRRMQMVFQDpYaSLNPRMTVGD 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  99 NVAFGPRLKKM-SEKDIQDKVKEMLGLVKLS-GFERREISELSGGQQQRVAIARALANDPEVLLLDEPLSALDYKLRKEL 176
Cdd:COG4608   117 IIAEPLRIHGLaSKAERRERVAELLELVGLRpEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQV 196

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2753759418 177 QQELRNIQKRLGITFVFVTHDqeeaLAM----SDWIFVMHDGLIQQNGTPEDIYDEP 229
Cdd:COG4608   197 LNLLEDLQDELGLTYLFISHD----LSVvrhiSDRVAVMYLGKIVEIAPRDELYARP 249
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
 6-203 2.68e-46

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: 157.26  E-value: 2.68e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   6 PILEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAE-KRRVNTV 84
Cdd:COG4133     1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDyRRRLAYL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  85 FQNYSLFPNMNVFDNVAFGPRLKKMSEKDIQdkVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDEP 164
Cdd:COG4133    81 GHADGLKPELTVRENLRFWAALYGLRADREA--IDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEP 158

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2753759418 165 LSALDYKLRKELQQELRNiQKRLGITFVFVTHDQEEALA 203
Cdd:COG4133   159 FTALDAAGVALLAELIAA-HLARGGAVLLTTHQPLELAA 196
L_ocin_972_ABC TIGR03608
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ...
 16-199 1.86e-45

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: 155.08  E-value: 1.86e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  16 SFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQ---VINDVPAEKRRVNT---VFQNYS 89
Cdd:TIGR03608   7 KFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQetpPLNSKKASKFRREKlgyLFQNFA 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  90 LFPNMNVFDNVAFGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDEPLSALD 169
Cdd:TIGR03608  87 LIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEPTGSLD 166

                         170       180       190
                  ....*....|....*....|....*....|
gi 2753759418 170 YKLRKELQQELRNIQKRlGITFVFVTHDQE 199
Cdd:TIGR03608 167 PKNRDEVLDLLLELNDE-GKTIIIVTHDPE 195
cbiO PRK13637
energy-coupling factor transporter ATPase;
5-228 3.00e-45

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 157.13  E-value: 3.00e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   5 MPILEFSKVALsfgdtevlKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAE----KRR 80
Cdd:PRK13637   13 MEGTPFEKKAL--------DNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKlsdiRKK 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  81 VNTVFQ--NYSLFPNmNVFDNVAFGPRLKKMSEKDIQDKVKEMLGLVKLS--GFERREISELSGGQQQRVAIARALANDP 156
Cdd:PRK13637   85 VGLVFQypEYQLFEE-TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEP 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2753759418 157 EVLLLDEPLSALDYKLRKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDE 228
Cdd:PRK13637  164 KILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKE 235
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
5-221 6.35e-45

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


Pssm-ID: 443326 [Multi-domain]  Cd Length: 242  Bit Score: 155.17  E-value: 6.35e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   5 MPIlEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLI-------SGQLQAdAGKIF-FEGQV-INDVP 75
Cdd:COG4161     1 MSI-QLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLnlletpdSGQLNI-AGHQFdFSQKPsEKAIR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  76 AEKRRVNTVFQNYSLFPNMNVFDNVAFGP-RLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALAN 154
Cdd:COG4161    79 LLRQKVGMVFQQYNLWPHLTVMENLIEAPcKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMM 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2753759418 155 DPEVLLLDEPLSALDYKLRKELQQELRNIQKrLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGT 221
Cdd:COG4161   159 EPQVLLFDEPTAALDPEITAQVVEIIRELSQ-TGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD 224
CeuD COG4604
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ...
 9-230 1.03e-44

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


Pssm-ID: 443654 [Multi-domain]  Cd Length: 252  Bit Score: 154.86  E-value: 1.03e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   9 EFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEK--RRVNTVFQ 86
Cdd:COG4604     3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRElaKRLAILRQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  87 NYSLFPNMNVFDNVAFG--PRLK-KMSEKDiQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDE 163
Cdd:COG4604    83 ENHINSRLTVRELVAFGrfPYSKgRLTAED-REIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDE 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2753759418 164 PLSALDYKLRKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDEPI 230
Cdd:COG4604   162 PLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIITPEV 228
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
 4-228 1.06e-44

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 155.15  E-value: 1.06e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   4 KMPILEFSKVALSFGDTE--VLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEKRR- 80
Cdd:PRK13632    4 KSVMIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRk 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  81 -VNTVFQNY-SLFPNMNVFDNVAFGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEV 158
Cdd:PRK13632   84 kIGIIFQNPdNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEI 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 159 LLLDEPLSALDYKLRKELQQELRNIQKRLGITFVFVTHDQEEALaMSDWIFVMHDGLIQQNGTPEDIYDE 228
Cdd:PRK13632  164 IIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEILNN 232
cbiO PRK13650
energy-coupling factor transporter ATPase;
23-226 1.96e-44

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 154.89  E-value: 1.96e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  23 LKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQ--VINDVPAEKRRVNTVFQNY-SLFPNMNVFDN 99
Cdd:PRK13650   23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDllTEENVWDIRHKIGMVFQNPdNQFVGATVEDD 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 100 VAFGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDEPLSALDYKLRKELQQE 179
Cdd:PRK13650  103 VAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKT 182

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2753759418 180 LRNIQKRLGITFVFVTHDQEEaLAMSDWIFVMHDGLIQQNGTPEDIY 226
Cdd:PRK13650  183 IKGIRDDYQMTVISITHDLDE-VALSDRVLVMKNGQVESTSTPRELF 228
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
5-283 2.61e-44

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 159.80  E-value: 2.61e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   5 MPILEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVI---NDVPAEKRRV 81
Cdd:COG1129     2 EPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVrfrSPRDAQAAGI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  82 NTVFQNYSLFPNMNVFDNVAFG---PRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEV 158
Cdd:COG1129    82 AIIHQELNLVPNLSVAENIFLGrepRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 159 LLLDEPLSALDyklRKELQQELRNIQ--KRLGITFVFVTHDQEEALAMSDWIFVMHDGliqqngtpediydepinHFVAD 236
Cdd:COG1129   162 LILDEPTASLT---EREVERLFRIIRrlKAQGVAIIYISHRLDEVFEIADRVTVLRDG-----------------RLVGT 221

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 2753759418 237 F-IGETNIvpgimkyDYLV-HFVGKDFENVDAGmRPNERVEVVLRPEDL 283
Cdd:COG1129   222 GpVAELTE-------DELVrLMVGRELEDLFPK-RAAAPGEVVLEVEGL 262
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
 5-229 4.33e-44

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 153.14  E-value: 4.33e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   5 MPILEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISG--QLQADA---GKIFFEGQVI--NDVPAE 77
Cdd:PRK14247    1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRliELYPEArvsGEVYLDGQDIfkMDVIEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  78 KRRVNTVFQNYSLFPNMNVFDNVAFGPRLKKM--SEKDIQDKVKEMLGLVKLSGFERREI----SELSGGQQQRVAIARA 151
Cdd:PRK14247   81 RRRVQMVFQIPNPIPNLSIFENVALGLKLNRLvkSKKELQERVRWALEKAQLWDEVKDRLdapaGKLSGGQQQRLCIARA 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2753759418 152 LANDPEVLLLDEPLSALDYKLRKELQQELRNIQKRLgiTFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDEP 229
Cdd:PRK14247  161 LAFQPEVLLADEPTANLDPENTAKIESLFLELKKDM--TIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNP 236
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
 6-223 1.10e-43

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


Pssm-ID: 443338 [Multi-domain]  Cd Length: 233  Bit Score: 151.43  E-value: 1.10e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   6 PILEFSKVALSFGDTE----VLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEKR-- 79
Cdd:COG4181     7 PIIELRGLTKTVGTGAgeltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARar 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  80 ----RVNTVFQNYSLFPNMNVFDNVAFgPrLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALAND 155
Cdd:COG4181    87 lrarHVGFVFQSFQLLPTLTALENVML-P-LELAGRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATE 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2753759418 156 PEVLLLDEPLSALDYKLRKELQQELRNIQKRLGITFVFVTHDQEEAlAMSDWIFVMHDGLIQQNGTPE 223
Cdd:COG4181   165 PAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALA-ARCDRVLRLRAGRLVEDTAAT 231
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
2-243 1.67e-43

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


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 155.58  E-value: 1.67e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   2 VEKMPILEfsKVALSFGdtevLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVP------ 75
Cdd:PRK10070   29 LSKEQILE--KTGLSLG----VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISdaelre 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  76 AEKRRVNTVFQNYSLFPNMNVFDNVAFGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALAND 155
Cdd:PRK10070  103 VRRKKIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAIN 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 156 PEVLLLDEPLSALDYKLRKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDEPINHFVA 235
Cdd:PRK10070  183 PDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVR 262


                  ....*...
gi 2753759418 236 DFIGETNI 243
Cdd:PRK10070  263 TFFRGVDI 270
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
 8-220 4.06e-43

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: 149.27  E-value: 4.06e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   8 LEFSKVALSFGDTEVLKEIDLVLESGkFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEKRR-VNTVFQ 86
Cdd:cd03264     1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRrIGYLPQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  87 NYSLFPNMNVFDNVAFGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDEPLS 166
Cdd:cd03264    80 EFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2753759418 167 ALDYKLRkelqQELRNIQKRLG--ITFVFVTHDQEEALAMSDWIFVMHDGLIQQNG 220
Cdd:cd03264   160 GLDPEER----IRFRNLLSELGedRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
8-224 9.42e-43

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 156.86  E-value: 9.42e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   8 LEFSKValSF---GDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEK--RRVN 82
Cdd:COG1132   340 IEFENV--SFsypGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESlrRQIG 417

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  83 TVFQNYSLFpNMNVFDNVAFGprlkkmsEKDI-QDKVKEMLGLVKLSGFERR-------EISE----LSGGQQQRVAIAR 150
Cdd:COG1132   418 VVPQDTFLF-SGTIRENIRYG-------RPDAtDEEVEEAAKAAQAHEFIEAlpdgydtVVGErgvnLSGGQRQRIAIAR 489

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2753759418 151 ALANDPEVLLLDEPLSALDYKLRKELQQELRNIQKrlGITFVFVTHdQEEALAMSDWIFVMHDGLIQQNGTPED 224
Cdd:COG1132   490 ALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAH-RLSTIRNADRILVLDDGRIVEQGTHEE 560
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
27-225 1.61e-42

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 148.19  E-value: 1.61e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  27 DLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEKRRVNTVFQNYSLFPNMNVFDNVAFG--P 104
Cdd:PRK10771   19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQENNLFSHLTVAQNIGLGlnP 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 105 RLKKMSEKdiQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDEPLSALDYKLRKELQQELRNIQ 184
Cdd:PRK10771   99 GLKLNAAQ--REKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVC 176

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2753759418 185 KRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDI 225
Cdd:PRK10771  177 QERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
 8-225 1.73e-42

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


Pssm-ID: 213191 [Multi-domain]  Cd Length: 222  Bit Score: 147.97  E-value: 1.73e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   8 LEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEKR-R--VNTV 84
Cdd:cd03224     1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERaRagIGYV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  85 FQNYSLFPNMNVFDNVAFGPRLKKmsEKDIQDKVKEMLGLV-KLSGFERREISELSGGQQQRVAIARALANDPEVLLLDE 163
Cdd:cd03224    81 PEGRRIFPELTVEENLLLGAYARR--RAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDE 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2753759418 164 PLSALDYKLRKELQQELRNIqKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDI 225
Cdd:cd03224   159 PSEGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
 7-229 1.74e-42

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 149.46  E-value: 1.74e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   7 ILEFSKVALSFGD-TEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVIN----DVPAEKRRV 81
Cdd:PRK13639    1 ILETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydkkSLLEVRKTV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  82 NTVFQNyslfPNMNVF-----DNVAFGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDP 156
Cdd:PRK13639   81 GIVFQN----PDDQLFaptveEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKP 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2753759418 157 EVLLLDEPLSALDYKLRKELQQELRNIQKRlGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDEP 229
Cdd:PRK13639  157 EIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDI 228
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
 18-229 2.16e-42

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: 155.23  E-value: 2.16e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  18 GDTEVLKEIDLVLESGKFYTLLGPSGSGKST----ILKLISGQlqadaGKIFFEGQVINDVPAE-----KRRVNTVFQN- 87
Cdd:COG4172   297 GHVKAVDGVSLTLRRGETLGLVGESGSGKSTlglaLLRLIPSE-----GEIRFDGQDLDGLSRRalrplRRRMQVVFQDp 371

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  88 Y-SLFPNMNVFDNVAFGPRL--KKMSEKDIQDKVKEMLGLVKLSGFER-REISELSGGQQQRVAIARALANDPEVLLLDE 163
Cdd:COG4172   372 FgSLSPRMTVGQIIAEGLRVhgPGLSAAERRARVAEALEEVGLDPAARhRYPHEFSGGQRQRIAIARALILEPKLLVLDE 451

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 164 PLSALDYKLRKELQQELRNIQKRLGITFVFVTHDqeeaL----AMSDWIFVMHDGLIQQNGTPEDIYDEP 229
Cdd:COG4172   452 PTSALDVSVQAQILDLLRDLQREHGLAYLFISHD----LavvrALAHRVMVMKDGKVVEQGPTEQVFDAP 517
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
 8-216 2.78e-41

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 145.98  E-value: 2.78e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   8 LEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEKRrvnTVFQN 87
Cdd:PRK11247   13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTR---LMFQD 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  88 YSLFPNMNVFDNVAFGPRlkkmseKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDEPLSA 167
Cdd:PRK11247   90 ARLLPWKKVIDNVGLGLK------GQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 163

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2753759418 168 LDYKLRKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLI 216
Cdd:PRK11247  164 LDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
 6-224 3.28e-41

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 145.68  E-value: 3.28e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   6 PILEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEK--RRVNT 83
Cdd:PRK13548    1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElaRRRAV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  84 VFQNYSL-FPnMNVFDNVAFG--PRLKkmSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALA------N 154
Cdd:PRK13548   81 LPQHSSLsFP-FTVEEVVAMGraPHGL--SRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdG 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2753759418 155 DPEVLLLDEPLSALDykLRKelQQELRNIQKRL----GITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPED 224
Cdd:PRK13548  158 PPRWLLLDEPTSALD--LAH--QHHVLRLARQLaherGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAE 227
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
 5-229 3.35e-41

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 145.66  E-value: 3.35e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   5 MPILEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLIS------------GQLQADAGKIFfeGQVIN 72
Cdd:PRK11264    1 MSAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINlleqpeagtirvGDITIDTARSL--SQQKG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  73 DVPAEKRRVNTVFQNYSLFPNMNVFDNVAFGPRL-KKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARA 151
Cdd:PRK11264   79 LIRQLRQHVGFVFQNFNLFPHRTVLENIIEGPVIvKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 152 LANDPEVLLLDEPLSALDYKLRKELQQELRNI--QKRlgiTFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDEP 229
Cdd:PRK11264  159 LAMRPEVILFDEPTSALDPELVGEVLNTIRQLaqEKR---TMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADP 235
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
6-226 6.03e-41

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 145.54  E-value: 6.03e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   6 PILEFSKVALSFGDTE--VLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVIND--VPAEKRRV 81
Cdd:PRK13635    4 EIIRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEetVWDVRRQV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  82 NTVFQNY-SLFPNMNVFDNVAFGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLL 160
Cdd:PRK13635   84 GMVFQNPdNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIII 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2753759418 161 LDEPLSALDYKLRKELQQELRNIQKRLGITFVFVTHDQEEAlAMSDWIFVMHDGLIQQNGTPEDIY 226
Cdd:PRK13635  164 LDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEA-AQADRVIVMNKGEILEEGTPEEIF 228
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
 5-229 8.41e-41

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: 143.97  E-value: 8.41e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   5 MPILEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEK------ 78
Cdd:COG0410     1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRiarlgi 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  79 ------RRVntvfqnyslFPNMNVFDNVAFGPRLKKmSEKDIQDKVKEMLGLvklsgF----ERREI--SELSGGQQQRV 146
Cdd:COG0410    81 gyvpegRRI---------FPSLTVEENLLLGAYARR-DRAEVRADLERVYEL-----FprlkERRRQraGTLSGGEQQML 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 147 AIARALANDPEVLLLDEPLSALDYKLRKELQQELRNIqKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIY 226
Cdd:COG0410   146 AIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRL-NREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELL 224


                  ...
gi 2753759418 227 DEP 229
Cdd:COG0410   225 ADP 227
ABC_ATP_DarD NF038007
darobactin export ABC transporter ATP-binding protein;
20-214 9.79e-41

darobactin export ABC transporter ATP-binding protein;


Pssm-ID: 411600 [Multi-domain]  Cd Length: 218  Bit Score: 143.32  E-value: 9.79e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  20 TEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQ-VINDVPAEK---RR--VNTVFQNYSLFPN 93
Cdd:NF038007   18 TKVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKeVTNLSYSQKiilRRelIGYIFQSFNLIPH 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  94 MNVFDNVAFGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDEPLSALDYKLR 173
Cdd:NF038007   98 LSIFDNVALPLKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNPALLLADEPTGNLDSKNA 177

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2753759418 174 KELQQELRNIQKRlGITFVFVTHDQeEALAMSDWIFVMHDG 214
Cdd:NF038007  178 RAVLQQLKYINQK-GTTIIMVTHSD-EASTYGNRIINMKDG 216
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
 5-225 1.22e-40

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


Pssm-ID: 440736 [Multi-domain]  Cd Length: 250  Bit Score: 144.07  E-value: 1.22e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   5 MPILEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAG---KIFFE--GQVinDVPAEKR 79
Cdd:COG1119     1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGndvRLFGErrGGE--DVWELRK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  80 R---VNTVFQNYsLFPNMNVFDNVAFGP-----RLKKMSEKDIQdKVKEMLGLVKLSGFERREISELSGGQQQRVAIARA 151
Cdd:COG1119    79 RiglVSPALQLR-FPRDETVLDVVLSGFfdsigLYREPTDEQRE-RARELLELLGLAHLADRPFGTLSQGEQRRVLIARA 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2753759418 152 LANDPEVLLLDEPLSALDYKLRKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDI 225
Cdd:COG1119   157 LVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEV 230
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
 16-221 1.67e-40

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 143.23  E-value: 1.67e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  16 SFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLI-------SGQLQAdAGKIFFEGQVIND--VPAEKRRVNTVFQ 86
Cdd:PRK11124   11 FYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLnllemprSGTLNI-AGNHFDFSKTPSDkaIRELRRNVGMVFQ 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  87 NYSLFPNMNVFDNVAFGP-RLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDEPL 165
Cdd:PRK11124   90 QYNLWPHLTVQQNLIEAPcRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPT 169

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2753759418 166 SALD-------YKLRKELQQElrniqkrlGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGT 221
Cdd:PRK11124  170 AALDpeitaqiVSIIRELAET--------GITQVIVTHEVEVARKTASRVVYMENGHIVEQGD 224
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
 8-224 1.77e-40

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: 150.29  E-value: 1.77e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   8 LEFSKVALSFGD-TEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAE--KRRVNTV 84
Cdd:COG4988   337 IELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPAswRRQIAWV 416

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  85 FQNYSLFPnMNVFDNVAFGprLKKMSEKDIQdkvkEMLGLVKLSGFERR-------EISE----LSGGQQQRVAIARALA 153
Cdd:COG4988   417 PQNPYLFA-GTIRENLRLG--RPDASDEELE----AALEAAGLDEFVAAlpdgldtPLGEggrgLSGGQAQRLALARALL 489

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2753759418 154 NDPEVLLLDEPLSALDYKLRKELQQELRNIQKrlGITFVFVTHDqEEALAMSDWIFVMHDGLIQQNGTPED 224
Cdd:COG4988   490 RDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHR-LALLAQADRILVLDDGRIVEQGTHEE 557
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
 8-214 3.20e-40

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: 139.87  E-value: 3.20e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   8 LEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVI---NDVPAEKRRVNTV 84
Cdd:cd03216     1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVsfaSPRDARRAGIAMV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  85 FQnyslfpnmnvfdnvafgprlkkmsekdiqdkvkemlglvklsgferreiseLSGGQQQRVAIARALANDPEVLLLDEP 164
Cdd:cd03216    81 YQ---------------------------------------------------LSVGERQMVEIARALARNARLLILDEP 109

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2753759418 165 LSALDYKLRKELQQELRNIQKRlGITFVFVTHDQEEALAMSDWIFVMHDG 214
Cdd:cd03216   110 TAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDG 158
COG4559 COG4559
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
8-230 3.76e-40

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


Pssm-ID: 443620 [Multi-domain]  Cd Length: 258  Bit Score: 142.95  E-value: 3.76e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   8 LEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAE---KRRvnTV 84
Cdd:COG4559     2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWelaRRR--AV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  85 F-QNYSL-FPnMNVFDNVAFG--PRLKkmSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALA------- 153
Cdd:COG4559    80 LpQHSSLaFP-FTVEEVVALGraPHGS--SAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvd 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 154 NDPEVLLLDEPLSALDYKlrkeLQQELRNIQKRL---GITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDEPI 230
Cdd:COG4559   157 GGPRWLFLDEPTSALDLA----HQHAVLRLARQLarrGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDEL 232
LolD_lipo_ex TIGR02211
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ...
 19-216 5.23e-40

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: 141.33  E-value: 5.23e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  19 DTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEKR------RVNTVFQNYSLFP 92
Cdd:TIGR02211  17 DTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERaklrnkKLGFIYQFHHLLP 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  93 NMNVFDNVAFGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDEPLSALDYKL 172
Cdd:TIGR02211  97 DFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLVLADEPTGNLDNNN 176

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2753759418 173 RKELQQELRNIQKRLGITFVFVTHDQEEALAMsDWIFVMHDGLI 216
Cdd:TIGR02211 177 AKIIFDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDGQL 219
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
 1-227 5.68e-40

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 142.97  E-value: 5.68e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   1 MVEKMPILEFSKVALSF-GDTE-VLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEK 78
Cdd:PRK13648    1 MEDKNSIIVFKNVSFQYqSDASfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  79 RR--VNTVFQN-YSLFPNMNVFDNVAFGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALAND 155
Cdd:PRK13648   81 LRkhIGIVFQNpDNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALN 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2753759418 156 PEVLLLDEPLSALDYKLRKELQQELRNIQKRLGITFVFVTHDQEEALAmSDWIFVMHDGLIQQNGTPEDIYD 227
Cdd:PRK13648  161 PSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFD 231
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
7-229 5.81e-40

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 142.98  E-value: 5.81e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   7 ILEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQvinDVPAEKR------- 79
Cdd:PRK11831    7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGE---NIPAMSRsrlytvr 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  80 -RVNTVFQNYSLFPNMNVFDNVAFGPR-LKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPE 157
Cdd:PRK11831   84 kRMSMLFQSGALFTDMNVFDNVAYPLReHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPD 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2753759418 158 VLLLDEPLSALDYKLRKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDEP 229
Cdd:PRK11831  164 LIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANP 235
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
 16-222 5.85e-40

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: 141.10  E-value: 5.85e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  16 SFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVIN-DVPAEKRRVNTVFQNYSLFPNM 94
Cdd:cd03263    11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRtDRKAARQSLGYCPQFDALFDEL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  95 NVFDNVAFGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDEPLSALDYKLRK 174
Cdd:cd03263    91 TVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRR 170

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2753759418 175 ELQQELRNIQKRLgiTFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTP 222
Cdd:cd03263   171 AIWDLILEVRKGR--SIILTTHSMDEAEALCDRIAIMSDGKLRCIGSP 216
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
 8-214 7.77e-40

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: 140.49  E-value: 7.77e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   8 LEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINdvPAEKRRVNTVFQN 87
Cdd:cd03269     1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD--IAARNRIGYLPEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  88 YSLFPNMNVFDNVAFGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDEPLSA 167
Cdd:cd03269    79 RGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSG 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2753759418 168 LDYKLRKELQQELRNiQKRLGITFVFVTHDQEEALAMSDWIFVMHDG 214
Cdd:cd03269   159 LDPVNVELLKDVIRE-LARAGKTVILSTHQMELVEELCDRVLLLNKG 204
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
 16-225 7.99e-40

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


Pssm-ID: 213232 [Multi-domain]  Cd Length: 220  Bit Score: 140.97  E-value: 7.99e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  16 SFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAE-KRRVNTVFQNYSLFPNM 94
Cdd:cd03265     9 KYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREvRRRIGIVFQDLSVDDEL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  95 NVFDNVAFGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDEPLSALDYKLRK 174
Cdd:cd03265    89 TGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRA 168

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2753759418 175 ELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDI 225
Cdd:cd03265   169 HVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
 5-229 3.06e-39

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: 146.75  E-value: 3.06e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   5 MPILEFSKVALSFGD----TEVLKEIDLVLESGKFYTLLGPSGSGKS----TILKLISGQLQADAGKIFFEGQVINDVPA 76
Cdd:COG4172     4 MPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  77 EK------RRVNTVFQN--YSLFPNMNVFDNVAFGPRL-KKMSEKDIQDKVKEMLGLVKLSGFERREIS---ELSGGQQQ 144
Cdd:COG4172    84 RElrrirgNRIAMIFQEpmTSLNPLHTIGKQIAEVLRLhRGLSGAAARARALELLERVGIPDPERRLDAyphQLSGGQRQ 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 145 RVAIARALANDPEVLLLDEPLSALDYKLRKELQQELRNIQKRLGITFVFVTHDqeeaLA----MSDWIFVMHDGLIQQNG 220
Cdd:COG4172   164 RVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHD----LGvvrrFADRVAVMRQGEIVEQG 239


                  ....*....
gi 2753759418 221 TPEDIYDEP 229
Cdd:COG4172   240 PTAELFAAP 248
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
5-230 3.12e-39

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 143.09  E-value: 3.12e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   5 MPILEFSKvalSFGDTEVlkEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVIND------VPAEK 78
Cdd:PRK11144    1 MLELNFKQ---QLGDLCL--TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDaekgicLPPEK 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  79 RRVNTVFQNYSLFPNMNVFDNVAFGprlkkMSEKDIQ--DKVKEMLGLVKLsgFERREISeLSGGQQQRVAIARALANDP 156
Cdd:PRK11144   76 RRIGYVFQDARLFPHYKVRGNLRYG-----MAKSMVAqfDKIVALLGIEPL--LDRYPGS-LSGGEKQRVAIGRALLTAP 147

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2753759418 157 EVLLLDEPLSALDYKLRKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDEPI 230
Cdd:PRK11144  148 ELLLMDEPLASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSA 221
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
 22-220 4.27e-39

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: 139.04  E-value: 4.27e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  22 VLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAE-KRRVNTVFQNYSLFPNMNVFDNV 100
Cdd:cd03266    20 AVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEaRRRLGFVSDSTGLYDRLTARENL 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 101 AFGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDEPLSALDYKLRKELQQEL 180
Cdd:cd03266   100 EYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFI 179

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2753759418 181 RNiQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNG 220
Cdd:cd03266   180 RQ-LRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
cbiO PRK13640
energy-coupling factor transporter ATPase;
7-229 5.13e-39

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 140.71  E-value: 5.13e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   7 ILEFSKVALSFGDTE--VLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADA---GKIFFEGQVIND--VPAEKR 79
Cdd:PRK13640    5 IVEFKHVSFTYPDSKkpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTAktVWDIRE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  80 RVNTVFQNY-SLFPNMNVFDNVAFGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEV 158
Cdd:PRK13640   85 KVGIVFQNPdNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKI 164

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2753759418 159 LLLDEPLSALDYKLRKELQQELRNIQKRLGITFVFVTHDQEEAlAMSDWIFVMHDGLIQQNGTPEDIYDEP 229
Cdd:PRK13640  165 IILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKV 234
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
 16-216 5.82e-39

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: 138.12  E-value: 5.82e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  16 SFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEKRRVNTVFQNYSLFPNMN 95
Cdd:cd03268     9 TYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIEAPGFYPNLT 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  96 VFDNVAFGPRLKKMSEKDIQdkvkEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDEPLSALDYKLRKE 175
Cdd:cd03268    89 ARENLRLLARLLGIRKKRID----EVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKE 164

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2753759418 176 LQQELRNIQKRlGITFVFVTHDQEEALAMSDWIFVMHDGLI 216
Cdd:cd03268   165 LRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKL 204
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 7-228 6.38e-39

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


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 140.63  E-value: 6.38e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   7 ILEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINdvPAEKRRVNtvfq 86
Cdd:COG4152     1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD--PEDRRRIG---- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  87 nY-----SLFPNMNVFDNVAFGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLL 161
Cdd:COG4152    75 -YlpeerGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLIL 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2753759418 162 DEPLSALDYKLRKELQQELRNiQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDE 228
Cdd:COG4152   154 DEPFSGLDPVNVELLKDVIRE-LAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQ 219
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
 6-229 9.05e-39

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: 145.68  E-value: 9.05e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   6 PILEFSKVALSF--GDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEK--RRV 81
Cdd:COG4987   332 PSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDlrRRI 411

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  82 NTVFQNYSLFpNMNVFDNVAFG-PRLkkmSEkdiqDKVKEMLGLVKLSGFERRE-------ISE----LSGGQQQRVAIA 149
Cdd:COG4987   412 AVVPQRPHLF-DTTLRENLRLArPDA---TD----EELWAALERVGLGDWLAALpdgldtwLGEggrrLSGGERRRLALA 483

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 150 RALANDPEVLLLDEPLSALDYKLRKELQQELRNIQKrlGITFVFVTHDqEEALAMSDWIFVMHDGLIQQNGTPEDIYDEP 229
Cdd:COG4987   484 RALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHR-LAGLERMDRILVLEDGRIVEQGTHEELLAQN 560
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
4-229 5.57e-38

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 137.41  E-value: 5.57e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   4 KMPILEFSKvalSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVP-------- 75
Cdd:PRK10619    5 KLNVIDLHK---RYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRdkdgqlkv 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  76 AEKR-------RVNTVFQNYSLFPNMNVFDNVAFGP-RLKKMSEKDIQDKVKEMLGLVKLSGFERREI-SELSGGQQQRV 146
Cdd:PRK10619   82 ADKNqlrllrtRLTMVFQHFNLWSHMTVLENVMEAPiQVLGLSKQEARERAVKYLAKVGIDERAQGKYpVHLSGGQQQRV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 147 AIARALANDPEVLLLDEPLSALDYKLRKELqqeLRNIQK--RLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPED 224
Cdd:PRK10619  162 SIARALAMEPEVLLFDEPTSALDPELVGEV---LRIMQQlaEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQ 238


                  ....*
gi 2753759418 225 IYDEP 229
Cdd:PRK10619  239 LFGNP 243
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
 8-229 5.98e-38

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: 136.52  E-value: 5.98e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   8 LEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEKR-RVNTVF- 85
Cdd:cd03218     1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRaRLGIGYl 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  86 -QNYSLFPNMNVFDNVAFGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDEP 164
Cdd:cd03218    81 pQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2753759418 165 LSALDYKLRKELQQELRNIQKRlGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDEP 229
Cdd:cd03218   161 FAGVDPIAVQDIQKIIKILKDR-GIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANE 224
cbiO PRK13649
energy-coupling factor transporter ATPase;
23-250 1.05e-37

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 137.18  E-value: 1.05e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  23 LKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVIN------DVPAEKRRVNTVFQnyslFPNMNV 96
Cdd:PRK13649   23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITstsknkDIKQIRKKVGLVFQ----FPESQL 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  97 FD-----NVAFGPRLKKMSEKDIQDKVKEMLGLVKLSG--FERREIsELSGGQQQRVAIARALANDPEVLLLDEPLSALD 169
Cdd:PRK13649   99 FEetvlkDVAFGPQNFGVSQEEAEALAREKLALVGISEslFEKNPF-ELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 170 YKLRKELQQELRNIQkRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDEpinhfvADFIGETNI-VPGIM 248
Cdd:PRK13649  178 PKGRKELMTLFKKLH-QSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD------VDFLEEKQLgVPKIT 250


                  ..
gi 2753759418 249 KY 250
Cdd:PRK13649  251 KF 252
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
20-221 1.13e-37

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 135.71  E-value: 1.13e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  20 TEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPA------EKRRVNTVFQNYSLFPN 93
Cdd:PRK11629   22 TDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSaakaelRNQKLGFIYQFHHLLPD 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  94 MNVFDNVAFGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDEPLSALDYKLR 173
Cdd:PRK11629  102 FTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNA 181

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2753759418 174 KELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIfVMHDGLIQQNGT 221
Cdd:PRK11629  182 DSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQL-EMRDGRLTAELS 228
SapF COG4167
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
18-229 1.32e-37

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


Pssm-ID: 443328 [Multi-domain]  Cd Length: 265  Bit Score: 136.51  E-value: 1.32e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  18 GDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVIN--DVPAEKRRVNTVFQ--NYSLFPN 93
Cdd:COG4167    24 QQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEygDYKYRCKHIRMIFQdpNTSLNPR 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  94 MNVFDNVAFGPRLK-KMSEKDIQDKVKEMLGLVKLSGfERRE--ISELSGGQQQRVAIARALANDPEVLLLDEPLSALDY 170
Cdd:COG4167   104 LNIGQILEEPLRLNtDLTAEEREERIFATLRLVGLLP-EHANfyPHMLSSGQKQRVALARALILQPKIIIADEALAALDM 182

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2753759418 171 KLRKELQQELRNIQKRLGITFVFVTHDqeeaLAM----SDWIFVMHDGLIQQNGTPEDIYDEP 229
Cdd:COG4167   183 SVRSQIINLMLELQEKLGISYIYVSQH----LGIvkhiSDKVLVMHQGEVVEYGKTAEVFANP 241
thiQ TIGR01277
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ...
 25-220 1.74e-37

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: 134.60  E-value: 1.74e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  25 EIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEKRRVNTVFQNYSLFPNMNVFDNVAFG- 103
Cdd:TIGR01277  16 EFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSMLFQENNLFAHLTVRQNIGLGl 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 104 -PRLKKMSEKdiQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDEPLSALDYKLRKELQQELRN 182
Cdd:TIGR01277  96 hPGLKLNAEQ--QEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQ 173

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2753759418 183 IQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNG 220
Cdd:TIGR01277 174 LCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
nickel_nikE TIGR02769
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ...
 22-216 3.30e-37

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


Pssm-ID: 131816 [Multi-domain]  Cd Length: 265  Bit Score: 135.32  E-value: 3.30e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  22 VLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEKRR-----VNTVFQN-YSLF-PNM 94
Cdd:TIGR02769  26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRafrrdVQLVFQDsPSAVnPRM 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  95 NVFDNVAFGPR-LKKMSEKDIQDKVKEMLGLVKL-SGFERREISELSGGQQQRVAIARALANDPEVLLLDEPLSALDYKL 172
Cdd:TIGR02769 106 TVRQIIGEPLRhLTSLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVL 185

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2753759418 173 RKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLI 216
Cdd:TIGR02769 186 QAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
 5-225 3.41e-37

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 138.82  E-value: 3.41e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   5 MPILEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEK--RRVN 82
Cdd:PRK09536    1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAasRRVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  83 TVFQNYSLFPNMNVFDNVAFG--PRLKKMSEKDIQDK--VKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEV 158
Cdd:PRK09536   81 SVPQDTSLSFEFDVRQVVEMGrtPHRSRFDTWTETDRaaVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPV 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 159 LLLDEPLSALD--YKLRK-ELQQELRNIQKrlgiTFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDI 225
Cdd:PRK09536  161 LLLDEPTASLDinHQVRTlELVRRLVDDGK----TAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADV 226
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 22-228 1.08e-36

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


Pssm-ID: 440718 [Multi-domain]  Cd Length: 264  Bit Score: 134.06  E-value: 1.08e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  22 VLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEKR--RVNTVFQNYSL--FPNMNVF 97
Cdd:COG1101    21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRakYIGRVFQDPMMgtAPSMTIE 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  98 DNVA----------FGPRLKKMSEKDIQDKVKEmLGLvklsGFERR---EISELSGGQQQRVAIARALANDPEVLLLDEP 164
Cdd:COG1101   101 ENLAlayrrgkrrgLRRGLTKKRRELFRELLAT-LGL----GLENRldtKVGLLSGGQRQALSLLMATLTKPKLLLLDEH 175

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2753759418 165 LSALDYKlRKELQQEL-RNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLI--------QQNGTPEDIYDE 228
Cdd:COG1101   176 TAALDPK-TAALVLELtEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRIildvsgeeKKKLTVEDLLEL 247
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
 3-214 1.42e-36

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 139.01  E-value: 1.42e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   3 EKMPILEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQ--VINDvPAEKRR 80
Cdd:COG3845     1 MMPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKpvRIRS-PRDAIA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  81 --VNTVFQNYSLFPNMNVFDNVAFG---PRLKKMSEKDIQDKVKEmlgLVKLSGFE---RREISELSGGQQQRVAIARAL 152
Cdd:COG3845    80 lgIGMVHQHFMLVPNLTVAENIVLGlepTKGGRLDRKAARARIRE---LSERYGLDvdpDAKVEDLSVGEQQRVEILKAL 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2753759418 153 ANDPEVLLLDEPLSALDYKLRKELQQELRNIqKRLGITFVFVTHDQEEALAMSDWIFVMHDG 214
Cdd:COG3845   157 YRGARILILDEPTAVLTPQEADELFEILRRL-AAEGKSIIFITHKLREVMAIADRVTVLRRG 217
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
8-230 2.47e-36

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 134.96  E-value: 2.47e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   8 LEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEG-QVINDVPAEKRRVNTVFQ 86
Cdd:PRK13536   42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGvPVPARARLARARIGVVPQ 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  87 NYSLFPNMNVFDNVAFGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDEPLS 166
Cdd:PRK13536  122 FDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTT 201

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2753759418 167 ALDYKLRKELQQELRNIQKRlGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDEPI 230
Cdd:PRK13536  202 GLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDEHI 264
urea_trans_UrtE TIGR03410
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ...
 8-235 3.57e-36

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: 131.49  E-value: 3.57e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   8 LEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEKRR---VNTV 84
Cdd:TIGR03410   1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERAragIAYV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  85 FQNYSLFPNMNVFDNVAFGPRLKKMSEKDIQDKV-------KEMLGlvklsgferREISELSGGQQQRVAIARALANDPE 157
Cdd:TIGR03410  81 PQGREIFPRLTVEENLLTGLAALPRRSRKIPDEIyelfpvlKEMLG---------RRGGDLSGGQQQQLAIARALVTRPK 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2753759418 158 VLLLDEPLSALDYKLRKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDEPINHFVA 235
Cdd:TIGR03410 152 LLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDELDEDKVRRYLA 229
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
22-228 6.78e-36

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 132.52  E-value: 6.78e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  22 VLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEG---QVINDVPAEKRRVNTVFQNyslfPNMN--- 95
Cdd:PRK13633   25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtSDEENLWDIRNKAGMVFQN----PDNQiva 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  96 --VFDNVAFGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDEPLSALDYKLR 173
Cdd:PRK13633  101 tiVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGR 180

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2753759418 174 KELQQELRNIQKRLGITFVFVTHDQEEAlAMSDWIFVMHDGLIQQNGTPEDIYDE 228
Cdd:PRK13633  181 REVVNTIKELNKKYGITIILITHYMEEA-VEADRIIVMDSGKVVMEGTPKEIFKE 234
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
7-225 1.49e-35

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 130.52  E-value: 1.49e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   7 ILEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEK--RRVNTV 84
Cdd:PRK11231    2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQlaRRLALL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  85 FQNYSLFPNMNVFDNVAFG--PRLK---KMSEKDiQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVL 159
Cdd:PRK11231   82 PQHHLTPEGITVRELVAYGrsPWLSlwgRLSAED-NARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVV 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2753759418 160 LLDEPLSALDYKLRKELQQELRNIQKRlGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDI 225
Cdd:PRK11231  161 LLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEV 225
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
 5-229 1.52e-35

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 131.46  E-value: 1.52e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   5 MPILEFSKVALSF-GDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVIN--DVPAEKRRV 81
Cdd:PRK13652    1 MHLIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITkeNIREVRKFV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  82 NTVFQNyslfPNMNVFD-----NVAFGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDP 156
Cdd:PRK13652   81 GLVFQN----PDDQIFSptveqDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEP 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2753759418 157 EVLLLDEPLSALDYKLRKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDEP 229
Cdd:PRK13652  157 QVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
heterocyst_DevA TIGR02982
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ...
 21-216 2.08e-35

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: 129.37  E-value: 2.08e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  21 EVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEK-----RRVNTVFQNYSLFPNMN 95
Cdd:TIGR02982  19 QVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQlvqlrRRIGYIFQAHNLLGFLT 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  96 VFDNVAFGPRL-KKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDEPLSALDYKLRK 174
Cdd:TIGR02982  99 ARQNVQMALELqPNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHPKLVLADEPTAALDSKSGR 178

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2753759418 175 ELQQELRNIQKRLGITFVFVTHDQeEALAMSDWIFVMHDGLI 216
Cdd:TIGR02982 179 DVVELMQKLAKEQGCTILMVTHDN-RILDVADRILQMEDGKL 219
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
 6-229 3.34e-35

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


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 129.72  E-value: 3.34e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   6 PILEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVP----AEKRRV 81
Cdd:PRK11300    4 PLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPghqiARMGVV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  82 NTvFQNYSLFPNMNVFDN--VAFGPRLK-------------KMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRV 146
Cdd:PRK11300   84 RT-FQHVRLFREMTVIENllVAQHQQLKtglfsgllktpafRRAESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRL 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 147 AIARALANDPEVLLLDEPLSALDYKLRKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIY 226
Cdd:PRK11300  163 EIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIR 242


                  ...
gi 2753759418 227 DEP 229
Cdd:PRK11300  243 NNP 245
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
 5-229 4.23e-35

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


Pssm-ID: 440752 [Multi-domain]  Cd Length: 240  Bit Score: 128.99  E-value: 4.23e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   5 MPILEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEKR-R--V 81
Cdd:COG1137     1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRaRlgI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  82 NTVFQNYSLFPNMNVFDNVAFGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLL 161
Cdd:COG1137    81 GYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2753759418 162 DEPLSALDYKLRKELQQELRNIQKRlGITfVFVT-HDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDEP 229
Cdd:COG1137   161 DEPFAGVDPIAVADIQKIIRHLKER-GIG-VLITdHNVRETLGICDRAYIISEGKVLAEGTPEEILNNP 227
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
6-230 6.75e-35

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 130.31  E-value: 6.75e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   6 PILEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVI-NDVPAEKRRVNTV 84
Cdd:PRK13537    6 APIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVpSRARHARQRVGVV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  85 FQNYSLFPNMNVFDNVAFGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDEP 164
Cdd:PRK13537   86 PQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEP 165

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2753759418 165 LSALDYKLRKELQQELRNIQKRlGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDEPI 230
Cdd:PRK13537  166 TTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESEI 230
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
 9-224 2.05e-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: 2.05e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   9 EFSKVALSF---GDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEKRR--VNT 83
Cdd:cd03249     2 EFKNVSFRYpsrPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRsqIGL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  84 VFQNYSLFpNMNVFDNVAFG--PRLKKMSEK------------DIQDKVKEMLGlvklsgfERReiSELSGGQQQRVAIA 149
Cdd:cd03249    82 VSQEPVLF-DGTIAENIRYGkpDATDEEVEEaakkanihdfimSLPDGYDTLVG-------ERG--SQLSGGQKQRIAIA 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2753759418 150 RALANDPEVLLLDEPLSALDYKLRKELQQELRNIqkRLGITFVFVTHdQEEALAMSDWIFVMHDGLIQQNGTPED 224
Cdd:cd03249   152 RALLRNPKILLLDEATSALDAESEKLVQEALDRA--MKGRTTIVIAH-RLSTIRNADLIAVLQNGQVVEQGTHDE 223
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
 6-238 3.08e-34

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 127.20  E-value: 3.08e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   6 PILEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLIS--GQLQAD---AGKIFFEGQVI----NDVPA 76
Cdd:PRK14239    4 PILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPEvtiTGSIVYNGHNIysprTDTVD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  77 EKRRVNTVFQNYSLFPnMNVFDNVAFGPRLKKMSEKDIQDKVKEMlGLVKLSGFErrEISE--------LSGGQQQRVAI 148
Cdd:PRK14239   84 LRKEIGMVFQQPNPFP-MSIYENVVYGLRLKGIKDKQVLDEAVEK-SLKGASIWD--EVKDrlhdsalgLSGGQQQRVCI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 149 ARALANDPEVLLLDEPLSALDYKLRKELQQELRNIQKRLgiTFVFVTHDQEEALAMSDWIFVMHDG-LIQQNGTpEDIYD 227
Cdd:PRK14239  160 ARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGdLIEYNDT-KQMFM 236

                         250
                  ....*....|.
gi 2753759418 228 EPINHFVADFI 238
Cdd:PRK14239  237 NPKHKETEDYI 247
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
 1-200 4.73e-34

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 125.98  E-value: 4.73e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   1 MVEKMPILEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEKRR 80
Cdd:PRK10247    1 MQENSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  81 --VNTVFQNYSLFPNmNVFDNVAFgP---RLKKMSEKDIQDkvkemlglvKLSGFE------RREISELSGGQQQRVAIA 149
Cdd:PRK10247   81 qqVSYCAQTPTLFGD-TVYDNLIF-PwqiRNQQPDPAIFLD---------DLERFAlpdtilTKNIAELSGGEKQRISLI 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2753759418 150 RALANDPEVLLLDEPLSALDYKLRKELQQELRNIQKRLGITFVFVTHDQEE 200
Cdd:PRK10247  150 RNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE 200
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
 7-228 5.03e-34

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 127.27  E-value: 5.03e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   7 ILEFSKVALSFGD-TEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVInDVPAE-----KRR 80
Cdd:PRK13636    5 ILKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKglmklRES 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  81 VNTVFQ--NYSLFpNMNVFDNVAFGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEV 158
Cdd:PRK13636   84 VGMVFQdpDNQLF-SASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKV 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 159 LLLDEPLSALDYKLRKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDE 228
Cdd:PRK13636  163 LVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAE 232
cbiO PRK13643
energy-coupling factor transporter ATPase;
7-228 8.78e-34

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 127.16  E-value: 8.78e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   7 ILEFSKVALSFGD-----TEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEK--- 78
Cdd:PRK13643    1 MIKFEKVNYTYQPnspfaSRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeik 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  79 ---RRVNTVFQnyslFPNMNVFD-----NVAFGPRLKKMSEKDIQDKVKEMLGLVKLSG-FERREISELSGGQQQRVAIA 149
Cdd:PRK13643   81 pvrKKVGVVFQ----FPESQLFEetvlkDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADeFWEKSPFELSGGQMRRVAIA 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2753759418 150 RALANDPEVLLLDEPLSALDYKLRKELQQELRNIQKRlGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDE 228
Cdd:PRK13643  157 GILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQE 234
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
22-216 1.04e-33

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 126.34  E-value: 1.04e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  22 VLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVIN-----DVPAEKRRVNTVFQnyslfpnmnv 96
Cdd:PRK10419   27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAklnraQRKAFRRDIQMVFQ---------- 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  97 fDNV-AFGPR-------------LKKMSEKDIQDKVKEMLGLVKL--SGFERREiSELSGGQQQRVAIARALANDPEVLL 160
Cdd:PRK10419   97 -DSIsAVNPRktvreiireplrhLLSLDKAERLARASEMLRAVDLddSVLDKRP-PQLSGGQLQRVCLARALAVEPKLLI 174

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2753759418 161 LDEPLSALDYKLRKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLI 216
Cdd:PRK10419  175 LDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
 12-216 1.20e-33

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: 124.29  E-value: 1.20e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  12 KVALSFGD-TEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINdvpaEKRRVNTVF---QN 87
Cdd:cd03226     4 NISFSYKKgTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK----AKERRKSIGyvmQD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  88 --YSLFPNmNVFDNVAFGPRLKKMSEKDIQDKVKEMlglvKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDEPL 165
Cdd:cd03226    80 vdYQLFTD-SVREELLLGLKELDAGNEQAETVLKDL----DLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPT 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2753759418 166 SALDYKLRKELQQELRNIQKRlGITFVFVTHDQEEALAMSDWIFVMHDGLI 216
Cdd:cd03226   155 SGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAI 204
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
7-197 2.05e-33

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 124.22  E-value: 2.05e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   7 ILEFSKVALSF-GDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVIN-----DVPAEKRR 80
Cdd:PRK10908    1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITrlknrEVPFLRRQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  81 VNTVFQNYSLFPNMNVFDNVAFGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLL 160
Cdd:PRK10908   81 IGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLL 160

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2753759418 161 LDEPLSALDYKLRKELqqeLRNIQK--RLGITFVFVTHD 197
Cdd:PRK10908  161 ADEPTGNLDDALSEGI---LRLFEEfnRVGVTVLMATHD 196
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
7-233 2.42e-33

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 125.13  E-value: 2.42e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   7 ILEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQAD----------AGKIFFEGQVINDVPA 76
Cdd:PRK09984    4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDksagshiellGRTVQREGRLARDIRK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  77 EKRRVNTVFQNYSLFPNMNVFDNVAFGPR---------LKKMSEKDIQDKVKEmLGLVKLSGFERREISELSGGQQQRVA 147
Cdd:PRK09984   84 SRANTGYIFQQFNLVNRLSVLENVLIGALgstpfwrtcFSWFTREQKQRALQA-LTRVGMVHFAHQRVSTLSGGQQQRVA 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 148 IARALANDPEVLLLDEPLSALDYKLRKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYD 227
Cdd:PRK09984  163 IARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQFDN 242


                  ....*.
gi 2753759418 228 EPINHF 233
Cdd:PRK09984  243 ERFDHL 248
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
 19-230 4.17e-33

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 124.85  E-value: 4.17e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  19 DTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAE--KRRVNTVFQNY--SLFpNM 94
Cdd:PRK13647   17 GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKwvRSKVGLVFQDPddQVF-SS 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  95 NVFDNVAFGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDEPLSALDYKLRK 174
Cdd:PRK13647   96 TVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQE 175

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2753759418 175 ELQQELRNIQKRlGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDEPI 230
Cdd:PRK13647  176 TLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDEDI 230
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
 8-227 4.25e-33

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: 123.49  E-value: 4.25e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   8 LEFSKVALSFGDTE--VLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDV--PAEKRRVNT 83
Cdd:cd03251     1 VEFKNVTFRYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYtlASLRRQIGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  84 VFQNYSLFpNMNVFDNVAFGPRlkKMSEKDI---------QDKVKEM-LGLVKLSGfERReiSELSGGQQQRVAIARALA 153
Cdd:cd03251    81 VSQDVFLF-NDTVAENIAYGRP--GATREEVeeaaraanaHEFIMELpEGYDTVIG-ERG--VKLSGGQRQRIAIARALL 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2753759418 154 NDPEVLLLDEPLSALDYKLRKELQQELRNIQKRLgITFVfVTHdQEEALAMSDWIFVMHDGLIQQNGTPEDIYD 227
Cdd:cd03251   155 KDPPILILDEATSALDTESERLVQAALERLMKNR-TTFV-IAH-RLSTIENADRIVVLEDGKIVERGTHEELLA 225
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
 8-223 4.57e-33

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: 123.49  E-value: 4.57e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   8 LEFSKVALSFGDT-EVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDV--PAEKRRVNTV 84
Cdd:cd03253     1 IEFENVTFAYDPGrPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVtlDSLRRAIGVV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  85 FQNYSLFpNMNVFDNVAFGpRLKKMSEK--------DIQDKVKEM-------LGlvklsgfERReiSELSGGQQQRVAIA 149
Cdd:cd03253    81 PQDTVLF-NDTIGYNIRYG-RPDATDEEvieaakaaQIHDKIMRFpdgydtiVG-------ERG--LKLSGGEKQRVAIA 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2753759418 150 RALANDPEVLLLDEPLSALDYKLRKELQQELRNIQKrlGITFVFVTHDQEEaLAMSDWIFVMHDGLIQQNGTPE 223
Cdd:cd03253   150 RAILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLST-IVNADKIIVLKDGRIVERGTHE 220
cbiO PRK13644
energy-coupling factor transporter ATPase;
7-229 7.08e-33

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 124.33  E-value: 7.08e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   7 ILEFSKVALSFGD-TEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVIND---VPAEKRRVN 82
Cdd:PRK13644    1 MIRLENVSYSYPDgTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDfskLQGIRKLVG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  83 TVFQN-YSLFPNMNVFDNVAFGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLL 161
Cdd:PRK13644   81 IVFQNpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIF 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 162 DEPLSALDYKLRKELqqeLRNIQK--RLGITFVFVTHDQEEaLAMSDWIFVMHDGLIQQNGTPEDIYDEP 229
Cdd:PRK13644  161 DEVTSMLDPDSGIAV---LERIKKlhEKGKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDV 226
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
 7-238 1.05e-32

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 123.23  E-value: 1.05e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   7 ILEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLIS-------GQLQADaGKIFFEGQVINDVPAEKR 79
Cdd:PRK14246   10 VFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNrlieiydSKIKVD-GKVLYFGKDIFQIDAIKL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  80 R--VNTVFQNYSLFPNMNVFDNVAFGPRLKKMSEK-DIQDKVKEMLGLVKL--SGFER--REISELSGGQQQRVAIARAL 152
Cdd:PRK14246   89 RkeVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKEKrEIKKIVEECLRKVGLwkEVYDRlnSPASQLSGGQQQRLTIARAL 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 153 ANDPEVLLLDEPLSALDYKLRKELQQELRNIQKRlgITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDEPINH 232
Cdd:PRK14246  169 ALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNE 246


                  ....*.
gi 2753759418 233 FVADFI 238
Cdd:PRK14246  247 LTEKYV 252
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
 9-223 1.12e-32

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: 122.33  E-value: 1.12e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   9 EFSKVALSFGDTE-VLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAE--KRRVNTVF 85
Cdd:cd03254     4 EFENVNFSYDEKKpVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKslRSMIGVVL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  86 QNYSLFPNmNVFDNVAFGprlkkmSEKDIQDKVKEMLGLVKLSGFERR-------EISE----LSGGQQQRVAIARALAN 154
Cdd:cd03254    84 QDTFLFSG-TIMENIRLG------RPNATDEEVIEAAKEAGAHDFIMKlpngydtVLGEnggnLSQGERQLLAIARAMLR 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2753759418 155 DPEVLLLDEPLSALDYKLRKELQQELRNIQKrlGITFVFVTHdQEEALAMSDWIFVMHDGLIQQNGTPE 223
Cdd:cd03254   157 DPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAH-RLSTIKNADKILVLDDGKIIEEGTHD 222
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
 7-206 2.17e-32

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 122.58  E-value: 2.17e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   7 ILEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILK-------LISGqLQADaGKIFFEGQVINDV---PA 76
Cdd:PRK14243   10 VLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPG-FRVE-GKVTFHGKNLYAPdvdPV 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  77 E-KRRVNTVFQNYSLFPNmNVFDNVAFGPR-------LKKMSEKDIQ-----DKVKEMLglvKLSGferreiSELSGGQQ 143
Cdd:PRK14243   88 EvRRRIGMVFQKPNPFPK-SIYDNIAYGARingykgdMDELVERSLRqaalwDEVKDKL---KQSG------LSLSGGQQ 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2753759418 144 QRVAIARALANDPEVLLLDEPLSALD--YKLR-KELQQELRNiqkrlGITFVFVTHDQEEALAMSD 206
Cdd:PRK14243  158 QRLCIARAIAVQPEVILMDEPCSALDpiSTLRiEELMHELKE-----QYTIIIVTHNMQQAARVSD 218
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
 8-216 3.41e-32

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: 120.77  E-value: 3.41e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   8 LEFSKVALSFGDTE--VLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDV-PAEKRR-VNT 83
Cdd:cd03245     3 IEFRNVSFSYPNQEipALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLdPADLRRnIGY 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  84 VFQNYSLFpNMNVFDNVAFGPRLkkMSEKDIQdKVKEMLGLVKLS-----GFERrEISE----LSGGQQQRVAIARALAN 154
Cdd:cd03245    83 VPQDVTLF-YGTLRDNITLGAPL--ADDERIL-RAAELAGVTDFVnkhpnGLDL-QIGErgrgLSGGQRQAVALARALLN 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2753759418 155 DPEVLLLDEPLSALDYKLRKELQQELRniQKRLGITFVFVTHDQeEALAMSDWIFVMHDGLI 216
Cdd:cd03245   158 DPPILLLDEPTSAMDMNSEERLKERLR--QLLGDKTLIIITHRP-SLLDLVDRIIVMDSGRI 216
cbiO PRK13641
energy-coupling factor transporter ATPase;
23-229 3.69e-32

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 122.63  E-value: 3.69e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  23 LKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEK------RRVNTVFQnyslFPNMNV 96
Cdd:PRK13641   23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKnlkklrKKVSLVFQ----FPEAQL 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  97 FDN-----VAFGPRLKKMSEKDIQDKVKEMLGLVKLS-GFERREISELSGGQQQRVAIARALANDPEVLLLDEPLSALDY 170
Cdd:PRK13641   99 FENtvlkdVEFGPKNFGFSEDEAKEKALKWLKKVGLSeDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDP 178

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2753759418 171 KLRKELQQELRNIQKRlGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDEP 229
Cdd:PRK13641  179 EGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
 23-229 4.77e-32

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 123.28  E-value: 4.77e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  23 LKEIDLV---LESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEKRR-----VNTVFQN--YSLFP 92
Cdd:PRK15079   34 LKAVDGVtlrLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRavrsdIQMIFQDplASLNP 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  93 NMNVFDNVA-----FGPrlkKMSEKDIQDKVKEML---GLvkLSGFERREISELSGGQQQRVAIARALANDPEVLLLDEP 164
Cdd:PRK15079  114 RMTIGEIIAeplrtYHP---KLSRQEVKDRVKAMMlkvGL--LPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEP 188

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2753759418 165 LSALDYKLRKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDEP 229
Cdd:PRK15079  189 VSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNP 253
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
 1-238 5.17e-32

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 121.68  E-value: 5.17e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   1 MVEKMPILEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLIS--GQLQADA---GKIFFEGQVIND-- 73
Cdd:PRK14258    1 MSKLIPAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNrmNELESEVrveGRVEFFNQNIYErr 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  74 --VPAEKRRVNTVFQNYSLFPnMNVFDNVAFGPRLKKMSEK-DIQDKVKEMLGLVKLSGFERREIS----ELSGGQQQRV 146
Cdd:PRK14258   81 vnLNRLRRQVSMVHPKPNLFP-MSVYDNVAYGVKIVGWRPKlEIDDIVESALKDADLWDEIKHKIHksalDLSGGQQQRL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 147 AIARALANDPEVLLLDEPLSALDYKLRKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHD-----GLIQQNGT 221
Cdd:PRK14258  160 CIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGL 239

                         250
                  ....*....|....*..
gi 2753759418 222 PEDIYDEPINHFVADFI 238
Cdd:PRK14258  240 TKKIFNSPHDSRTREYV 256
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
16-203 5.70e-32

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 119.26  E-value: 5.70e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  16 SFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIffegqvindVPAEKRRVNTVFQNYSL---FP 92
Cdd:NF040873    1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV---------RRAGGARVAYVPQRSEVpdsLP 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  93 nMNVFDNVAFG--PRLKKMSEKDIQDK--VKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDEPLSAL 168
Cdd:NF040873   72 -LTVRDLVAMGrwARRGLWRRLTRDDRaaVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2753759418 169 DYKLRKELQQELRNIQKRlGITFVFVTHDQEEALA 203
Cdd:NF040873  151 DAESRERIIALLAEEHAR-GATVVVVTHDLELVRR 184
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
 8-214 1.24e-31

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: 117.70  E-value: 1.24e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   8 LEFSKVALSFGDTE--VLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDV-PAEKRR-VNT 83
Cdd:cd03246     1 LEVENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWdPNELGDhVGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  84 VFQNYSLFPNmNVFDNVafgprlkkmsekdiqdkvkemlglvklsgferreiseLSGGQQQRVAIARALANDPEVLLLDE 163
Cdd:cd03246    81 LPQDDELFSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDE 122

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2753759418 164 PLSALDYKLRKELQQELRNIQKRlGITFVFVTHdQEEALAMSDWIFVMHDG 214
Cdd:cd03246   123 PNSHLDVEGERALNQAIAALKAA-GATRIVIAH-RPETLASADRILVLEDG 171
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
 5-201 1.61e-31

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 119.11  E-value: 1.61e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   5 MP---ILEFSKVALSFGDTE----VLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAE 77
Cdd:PRK10584    1 MPaenIVEVHHLKKSVGQGEhelsILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  78 KR------RVNTVFQNYSLFPNMNVFDNVAFGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARA 151
Cdd:PRK10584   81 ARaklrakHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARA 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2753759418 152 LANDPEVLLLDEPLSALDYKLRKELQQELRNIQKRLGITFVFVTHDQEEA 201
Cdd:PRK10584  161 FNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLA 210
cbiO PRK13646
energy-coupling factor transporter ATPase;
21-226 2.08e-31

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 120.65  E-value: 2.08e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  21 EVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEK------RRVNTVFQnyslFPNM 94
Cdd:PRK13646   21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKyirpvrKRIGMVFQ----FPES 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  95 NVF-DNVA----FGPRLKKMSEKDIQDKVKEMLglVKLsGFERREIS----ELSGGQQQRVAIARALANDPEVLLLDEPL 165
Cdd:PRK13646   97 QLFeDTVEreiiFGPKNFKMNLDEVKNYAHRLL--MDL-GFSRDVMSqspfQMSGGQMRKIAIVSILAMNPDIIVLDEPT 173

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2753759418 166 SALDYKLRKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIY 226
Cdd:PRK13646  174 AGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELF 234
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
 6-230 2.98e-31

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 124.01  E-value: 2.98e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   6 PILEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQV---INDVPAEKRRVN 82
Cdd:PRK15439   10 PLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPcarLTPAKAHQLGIY 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  83 TVFQNYSLFPNMNVFDNVAFGPRLKKMSEKDIQDKVKEMLGLVKLSGferrEISELSGGQQQRVAIARALANDPEVLLLD 162
Cdd:PRK15439   90 LVPQEPLLFPNLSVKENILFGLPKRQASMQKMKQLLAALGCQLDLDS----SAGSLEVADRQIVEILRGLMRDSRILILD 165

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2753759418 163 EPLSALDYKLRKELQQELRNIQKrLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDEPI 230
Cdd:PRK15439  166 EPTASLTPAETERLFSRIRELLA-QGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDDI 232
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
 8-227 1.00e-30

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: 123.29  E-value: 1.00e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   8 LEFSKVALSFGDTE--VLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAE--KRRVNT 83
Cdd:TIGR02203 331 VEFRNVTFRYPGRDrpALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLAslRRQVAL 410

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  84 VFQNYSLFpNMNVFDNVAFGpRLKKMSEKDI---------QDKVKEM-LGL---VKLSGferreiSELSGGQQQRVAIAR 150
Cdd:TIGR02203 411 VSQDVVLF-NDTIANNIAYG-RTEQADRAEIeralaaayaQDFVDKLpLGLdtpIGENG------VLLSGGQRQRLAIAR 482

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2753759418 151 ALANDPEVLLLDEPLSALDYKLRKELQQELRNIQKrlGITFVFVTHdQEEALAMSDWIFVMHDGLIQQNGTPEDIYD 227
Cdd:TIGR02203 483 ALLKDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAH-RLSTIEKADRIVVMDDGRIVERGTHNELLA 556
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
 6-211 1.77e-30

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: 122.01  E-value: 1.77e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   6 PILEFSKVALSFGDT-EVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAE--KRRVN 82
Cdd:TIGR02857 320 SSLEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADswRDQIA 399

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  83 TVFQNYSLFPNmNVFDNVAFGPRLKKMSEkdiqdkVKEMLGLVKLSGFER-------REISE----LSGGQQQRVAIARA 151
Cdd:TIGR02857 400 WVPQHPFLFAG-TIAENIRLARPDASDAE------IREALERAGLDEFVAalpqgldTPIGEggagLSGGQAQRLALARA 472

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2753759418 152 LANDPEVLLLDEPLSALDyklrKELQQELRNIQKRL--GITFVFVTHDQEEALAMsDWIFVM 211
Cdd:TIGR02857 473 FLRDAPLLLLDEPTAHLD----AETEAEVLEALRALaqGRTVLLVTHRLALAALA-DRIVVL 529
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
 6-229 1.94e-30

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 122.12  E-value: 1.94e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   6 PILEFSKVALSF-----------GDTEVLKEIDLVLESGKFYTLLGPSGSGKST----ILKLISGQlqadaGKIFFEGQV 70
Cdd:PRK15134  274 PLLDVEQLQVAFpirkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINSQ-----GEIWFDGQP 348

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  71 INDVPAEK-----RRVNTVFQ--NYSLFPNMNVFDNVAFGPRL--KKMSEKDIQDKVKEMLGLVKLSGFER-REISELSG 140
Cdd:PRK15134  349 LHNLNRRQllpvrHRIQVVFQdpNSSLNPRLNVLQIIEEGLRVhqPTLSAAQREQQVIAVMEEVGLDPETRhRYPAEFSG 428

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 141 GQQQRVAIARALANDPEVLLLDEPLSALDYKLRKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNG 220
Cdd:PRK15134  429 GQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQG 508


                  ....*....
gi 2753759418 221 TPEDIYDEP 229
Cdd:PRK15134  509 DCERVFAAP 517
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
 17-238 2.01e-30

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 116.87  E-value: 2.01e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  17 FGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISG--QLQADAG-----KIFFEGQVINDV-PAE-KRRVNTVFQN 87
Cdd:PRK14267   14 YGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRllELNEEARvegevRLFGRNIYSPDVdPIEvRREVGMVFQY 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  88 YSLFPNMNVFDNVAFGPRLKKM--SEKDIQDKVKEMLGLVKLSGFERREI----SELSGGQQQRVAIARALANDPEVLLL 161
Cdd:PRK14267   94 PNPFPHLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALWDEVKDRLndypSNLSGGQRQRLVIARALAMKPKILLM 173

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2753759418 162 DEPLSALDYKLRKELQQELRNIQKRLgiTFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDEPINHFVADFI 238
Cdd:PRK14267  174 DEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELTEKYV 248
type_I_sec_LssB TIGR03375
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ...
 8-225 2.01e-30

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: 123.05  E-value: 2.01e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   8 LEFSKVALSF--GDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDV-PAEKRR-VNT 83
Cdd:TIGR03375 464 IEFRNVSFAYpgQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIdPADLRRnIGY 543

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  84 VFQNYSLFpNMNVFDNVAFGPRLkkmsekdIQDKvkEMLGLVKLSGFER----------REISE----LSGGQQQRVAIA 149
Cdd:TIGR03375 544 VPQDPRLF-YGTLRDNIALGAPY-------ADDE--EILRAAELAGVTEfvrrhpdgldMQIGErgrsLSGGQRQAVALA 613

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 150 RALANDPEVLLLDEPLSALD----YKLRKELQQELRniqkrlGITFVFVTHDQeEALAMSDWIFVMHDGLIQQNGTPEDI 225
Cdd:TIGR03375 614 RALLRDPPILLLDEPTSAMDnrseERFKDRLKRWLA------GKTLVLVTHRT-SLLDLVDRIIVMDNGRIVADGPKDQV 686
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
 10-197 6.67e-30

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 120.17  E-value: 6.67e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  10 FSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVindvpaekrRVNTVFQNYS 89
Cdd:COG0488     1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGL---------RIGYLPQEPP 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  90 LFPNMNVFDNV--AFGPRLKKMSEKD------------------IQDKVKEMLG----------LVKLsGFER----REI 135
Cdd:COG0488    72 LDDDLTVLDTVldGDAELRALEAELEeleaklaepdedlerlaeLQEEFEALGGweaearaeeiLSGL-GFPEedldRPV 150

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2753759418 136 SELSGGQQQRVAIARALANDPEVLLLDEPLSALDYKLRKELQQELRNIQKrlgiTFVFVTHD 197
Cdd:COG0488   151 SELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPG----TVLVVSHD 208
cbiO PRK13645
energy-coupling factor transporter ATPase;
23-226 1.84e-29

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 115.49  E-value: 1.84e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  23 LKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAG-------KIFFEGQVINDVPAEKRRVNTVFQ--NYSLFPN 93
Cdd:PRK13645   27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGqtivgdyAIPANLKKIKEVKRLRKEIGLVFQfpEYQLFQE 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  94 mNVFDNVAFGPRLKKMSEKDIQDKVKEMLGLVKL-SGFERREISELSGGQQQRVAIARALANDPEVLLLDEPLSALDYKL 172
Cdd:PRK13645  107 -TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKG 185

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2753759418 173 RKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIY 226
Cdd:PRK13645  186 EEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIF 239
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
 22-225 2.99e-29

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: 118.70  E-value: 2.99e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  22 VLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEK--RRVNTVFQNYSLFPNmNVFDN 99
Cdd:COG4618   347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREElgRHIGYLPQDVELFDG-TIAEN 425

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 100 VAfgprlkKMSEKDIQDKVK--------EM-LGLVKlsGFERReISE----LSGGQQQRVAIARALANDPEVLLLDEPLS 166
Cdd:COG4618   426 IA------RFGDADPEKVVAaaklagvhEMiLRLPD--GYDTR-IGEggarLSGGQRQRIGLARALYGDPRLVVLDEPNS 496

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2753759418 167 ALDYKLRKELQQELRNIQKRlGITFVFVTHDQeEALAMSDWIFVMHDGLIQQNGTPEDI 225
Cdd:COG4618   497 NLDDEGEAALAAAIRALKAR-GATVVVITHRP-SLLAAVDKLLVLRDGRVQAFGPRDEV 553
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
 6-239 9.06e-29

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 113.27  E-value: 9.06e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   6 PILEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKL-------ISGQLQAdaGKIFFEGQVI---NDVP 75
Cdd:PRK14271   20 PAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTlnrmndkVSGYRYS--GDVLLGGRSIfnyRDVL 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  76 AEKRRVNTVFQNYSLFPnMNVFDNVAFGPRLKKM-SEKDIQDKVKEMLGLVKLSGFERREISE----LSGGQQQRVAIAR 150
Cdd:PRK14271   98 EFRRRVGMLFQRPNPFP-MSIMDNVLAGVRAHKLvPRKEFRGVAQARLTEVGLWDAVKDRLSDspfrLSGGQQQLLCLAR 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 151 ALANDPEVLLLDEPLSALDYKLRKELQQELRNIQKRLgiTFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDEPI 230
Cdd:PRK14271  177 TLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPK 254


                  ....*....
gi 2753759418 231 NHFVADFIG 239
Cdd:PRK14271  255 HAETARYVA 263
cbiO PRK13642
energy-coupling factor transporter ATPase;
7-226 9.08e-29

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 113.26  E-value: 9.08e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   7 ILEFSKVALSF---GDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVIN--DVPAEKRRV 81
Cdd:PRK13642    4 ILEVENLVFKYekeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTaeNVWNLRRKI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  82 NTVFQNY-SLFPNMNVFDNVAFGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLL 160
Cdd:PRK13642   84 GMVFQNPdNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIII 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2753759418 161 LDEPLSALDYKLRKELQQELRNIQKRLGITFVFVTHDQEEAlAMSDWIFVMHDGLIQQNGTPEDIY 226
Cdd:PRK13642  164 LDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEA-ASSDRILVMKAGEIIKEAAPSELF 228
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
 21-228 1.58e-28

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: 111.42  E-value: 1.58e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  21 EVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAE--KRRVNTVFQNYSLFpNMNVFD 98
Cdd:cd03252    16 VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAwlRRQVGVVLQENVLF-NRSIRD 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  99 NVAF---GPRLKKMSE----KDIQDKVKEM-LGLVKLSGfERReiSELSGGQQQRVAIARALANDPEVLLLDEPLSALDY 170
Cdd:cd03252    95 NIALadpGMSMERVIEaaklAGAHDFISELpEGYDTIVG-EQG--AGLSGGQRQRIAIARALIHNPRILIFDEATSALDY 171

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2753759418 171 KLRKELQQELRNIQKrlGITFVFVTHdQEEALAMSDWIFVMHDGLIQQNGTPEDIYDE 228
Cdd:cd03252   172 ESEHAIMRNMHDICA--GRTVIIIAH-RLSTVKNADRIIVMEKGRIVEQGSHDELLAE 226
nickel_nikD TIGR02770
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ...
 26-229 1.61e-28

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: 111.31  E-value: 1.61e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  26 IDLVLESGKFYTLLGPSGSGKST----ILKLISGQLQADAGKIFFEGQVINDVPAEKRRVNTVFQN--YSLFPNMNVFDN 99
Cdd:TIGR02770   5 LNLSLKRGEVLALVGESGSGKSLtclaILGLLPPGLTQTSGEILLDGRPLLPLSIRGRHIATIMQNprTAFNPLFTMGNH 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 100 VAFGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREIS---ELSGGQQQRVAIARALANDPEVLLLDEPLSALDYKLRKEL 176
Cdd:TIGR02770  85 AIETLRSLGKLSKQARALILEALEAVGLPDPEEVLKKypfQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVNQARV 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2753759418 177 QQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDEP 229
Cdd:TIGR02770 165 LKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNP 217
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
 22-228 2.74e-28

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


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 110.94  E-value: 2.74e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  22 VLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVIndVPAEkrrVNTVFQnyslfPNMNVFDNVA 101
Cdd:COG1134    41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVS--ALLE---LGAGFH-----PELTGRENIY 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 102 FGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDEPLSALDYKLRKELQQELR 181
Cdd:COG1134   111 LNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIR 190

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2753759418 182 NIQKRlGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDE 228
Cdd:COG1134   191 ELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIAA 236
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
 22-244 9.48e-28

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 111.48  E-value: 9.48e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  22 VLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAG-----------KIFFEGQVINDVPAE-------KRRVNT 83
Cdd:PRK13631   41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGtiqvgdiyigdKKNNHELITNPYSKKiknfkelRRRVSM 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  84 VFQ--NYSLFPNmNVFDNVAFGPRLKKMSEKDIQDKVK---EMLGLVklSGFERREISELSGGQQQRVAIARALANDPEV 158
Cdd:PRK13631  121 VFQfpEYQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKfylNKMGLD--DSYLERSPFGLSGGQKRRVAIAGILAIQPEI 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 159 LLLDEPLSALDYKLRKELQQELRNiQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDEPinhfvaDFI 238
Cdd:PRK13631  198 LIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQ------HII 270


                  ....*.
gi 2753759418 239 GETNIV 244
Cdd:PRK13631  271 NSTSIQ 276
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
 22-214 1.10e-27

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: 107.94  E-value: 1.10e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  22 VLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGqvindvpaekrRVNTVFQNYSLFpNMNVFDNVA 101
Cdd:cd03250    20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-----------SIAYVSQEPWIQ-NGTIRENIL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 102 FGprlkkmSEKDIQ--DKVKEMLGLVK----LSGFERREISE----LSGGQQQRVAIARALANDPEVLLLDEPLSALDYK 171
Cdd:cd03250    88 FG------KPFDEEryEKVIKACALEPdleiLPDGDLTEIGEkginLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAH 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2753759418 172 LRKELQQELrnIQKRL--GITFVFVTHdQEEALAMSDWIFVMHDG 214
Cdd:cd03250   162 VGRHIFENC--ILGLLlnNKTRILVTH-QLQLLPHADQIVVLDNG 203
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
 22-259 1.28e-27

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 110.56  E-value: 1.28e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  22 VLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKI--FFEGQVINDVPAEK--------------------- 78
Cdd:PRK13651   22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewIFKDEKNKKKTKEKekvleklviqktrfkkikkik 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  79 ---RRVNTVFQ--NYSLFPNmNVFDNVAFGPRLKKMSEKDIQDKVKEMLGLVKLS-GFERREISELSGGQQQRVAIARAL 152
Cdd:PRK13651  102 eirRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDeSYLQRSPFELSGGQKRRVALAGIL 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 153 ANDPEVLLLDEPLSALDYKLRKELQQELRNIQKRlGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDEpinh 232
Cdd:PRK13651  181 AMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTYDILSD---- 255

                         250       260
                  ....*....|....*....|....*..
gi 2753759418 233 fvADFIGETNIVPgimkyDYLVHFVGK 259
Cdd:PRK13651  256 --NKFLIENNMEP-----PKLLNFVNK 275
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
6-223 1.38e-27

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 114.44  E-value: 1.38e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   6 PILEFSKVALSF----GDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVI----NDVPAE 77
Cdd:PRK10535    3 ALLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVatldADALAQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  78 KRR--VNTVFQNYSLFPNMNVFDNVAFGPRLKKMSEKDIQDKVKEMLGLVKLSgfERREI--SELSGGQQQRVAIARALA 153
Cdd:PRK10535   83 LRRehFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLE--DRVEYqpSQLSGGQQQRVSIARALM 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 154 NDPEVLLLDEPLSALDYKLRKELQQELRNIQKRlGITFVFVTHDQEEAlAMSDWIFVMHDGLIQQNGTPE 223
Cdd:PRK10535  161 NGGQVILADEPTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHDPQVA-AQAERVIEIRDGEIVRNPPAQ 228
type_I_sec_PrtD TIGR01842
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ...
 18-225 1.55e-27

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: 113.60  E-value: 1.55e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  18 GDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEK--RRVNTVFQNYSLFPNmN 95
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETfgKHIGYLPQDVELFPG-T 407

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  96 VFDNVA-FGPRLKkmSEKDIQ----DKVKEM-LGLVKlsGFERrEISE----LSGGQQQRVAIARALANDPEVLLLDEPL 165
Cdd:TIGR01842 408 VAENIArFGENAD--PEKIIEaaklAGVHELiLRLPD--GYDT-VIGPggatLSGGQRQRIALARALYGDPKLVVLDEPN 482

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 166 SALDYKLRKELQQELRNIQKRlGITFVFVTHdQEEALAMSDWIFVMHDGLIQQNGTPEDI 225
Cdd:TIGR01842 483 SNLDEEGEQALANAIKALKAR-GITVVVITH-RPSLLGCVDKILVLQDGRIARFGERDEV 540
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
 17-229 1.98e-27

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 110.44  E-value: 1.98e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  17 FGDTEVLKEIDLV---LESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQ--VINDVPAEK---RRVNTVFQN- 87
Cdd:PRK11308   22 FKPERLVKALDGVsftLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQdlLKADPEAQKllrQKIQIVFQNp 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  88 Y-SLFPNMNVFDNVAfGPRL--KKMSEKDIQDKVKEMLGLVKL-SGFERREISELSGGQQQRVAIARALANDPEVLLLDE 163
Cdd:PRK11308  102 YgSLNPRKKVGQILE-EPLLinTSLSAAERREKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADE 180

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2753759418 164 PLSALDYKLRKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDEP 229
Cdd:PRK11308  181 PVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNP 246
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
 8-229 2.43e-27

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 113.66  E-value: 2.43e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   8 LEFSKVALSF---GDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAE--KRRVN 82
Cdd:TIGR00958 479 IEFQDVSFSYpnrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHylHRQVA 558

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  83 TVFQNYSLFpNMNVFDNVAFGprLKKMSEKDIQDKVKEMLGLVKLSGFER---REISE----LSGGQQQRVAIARALAND 155
Cdd:TIGR00958 559 LVGQEPVLF-SGSVRENIAYG--LTDTPDEEIMAAAKAANAHDFIMEFPNgydTEVGEkgsqLSGGQKQRIAIARALVRK 635

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2753759418 156 PEVLLLDEPLSALDyklrKELQQELRNIQKRLGITFVFVTHdQEEALAMSDWIFVMHDGLIQQNGTPEDIYDEP 229
Cdd:TIGR00958 636 PRVLILDEATSALD----AECEQLLQESRSRASRTVLLIAH-RLSTVERADQILVLKKGSVVEMGTHKQLMEDQ 704
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
7-226 4.50e-27

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 108.56  E-value: 4.50e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   7 ILEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVIN----DVPAEKRRVN 82
Cdd:PRK13638    1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDyskrGLLALRQQVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  83 TVFQNyslfPNMNVF-----DNVAFGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPE 157
Cdd:PRK13638   81 TVFQD----PEQQIFytdidSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQAR 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2753759418 158 VLLLDEPLSALDYKLRKELQQELRNIQKRlGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIY 226
Cdd:PRK13638  157 YLLLDEPTAGLDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
 6-214 4.66e-27

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: 107.13  E-value: 4.66e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   6 PILEFSKVALSF-----GDTE--VLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFF--EGQVINDVPA 76
Cdd:COG4778     3 TLLEVENLSKTFtlhlqGGKRlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVDLAQA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  77 EKRRV-----NT---VFQNYSLFPNMNVFDNVAFGPRLKKMSEKDIQDKVKEMLglvklsgfERREISE---------LS 139
Cdd:COG4778    83 SPREIlalrrRTigyVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELL--------ARLNLPErlwdlppatFS 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 140 GGQQQRVAIARALANDPEVLLLDEPLSALDYKLR---KELQQELrniqKRLGITFVFVTHDQE--EALAmsDWIFVMHDG 214
Cdd:COG4778   155 GGEQQRVNIARGFIADPPLLLLDEPTASLDAANRavvVELIEEA----KARGTAIIGIFHDEEvrEAVA--DRVVDVTPF 228
type_I_sec_HlyB TIGR01846
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ...
 21-225 1.95e-26

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


Pssm-ID: 273831 [Multi-domain]  Cd Length: 694  Bit Score: 110.99  E-value: 1.95e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  21 EVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQ--VINDVPAEKRRVNTVFQNYSLFpNMNVFD 98
Cdd:TIGR01846 471 EVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVdlAIADPAWLRRQMGVVLQENVLF-SRSIRD 549

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  99 NVAFGprlkkmsekDIQDKVKEMLGLVKLSGFE----------RREISE----LSGGQQQRVAIARALANDPEVLLLDEP 164
Cdd:TIGR01846 550 NIALC---------NPGAPFEHVIHAAKLAGAHdfiselpqgyNTEVGEkganLSGGQRQRIAIARALVGNPRILIFDEA 620

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2753759418 165 LSALDYKLRKELQQELRNIQKrlGITFVFVTHdQEEALAMSDWIFVMHDGLIQQNGTPEDI 225
Cdd:TIGR01846 621 TSALDYESEALIMRNMREICR--GRTVIIIAH-RLSTVRACDRIIVLEKGQIAESGRHEEL 678
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
 7-292 2.73e-26

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: 109.91  E-value: 2.73e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   7 ILEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADA--GKIFFEGQVI---NDVPAEKRRV 81
Cdd:TIGR02633   1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLkasNIRDTERAGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  82 NTVFQNYSLFPNMNVFDNVAFGPRL----KKMSEKDIQDKVKEMLGLVKLSGF-ERREISELSGGQQQRVAIARALANDP 156
Cdd:TIGR02633  81 VIIHQELTLVPELSVAENIFLGNEItlpgGRMAYNAMYLRAKNLLRELQLDADnVTRPVGDYGGGQQQLVEIAKALNKQA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 157 EVLLLDEPLSALDYKLRKELQQELRNIQKRlGITFVFVTHDQEEALAMSDWIFVMHDGliQQNGT-PEDIYDEPinhfva 235
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDG--QHVATkDMSTMSED------ 231

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2753759418 236 dfigetnivpgimkyDYLVHFVGKDFENVDAgMRPNERVEVVLRPEDLDLTDPANGK 292
Cdd:TIGR02633 232 ---------------DIITMMVGREITSLYP-HEPHEIGDVILEARNLTCWDVINPH 272
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
 22-220 2.90e-26

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: 104.92  E-value: 2.90e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  22 VLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVpaekrRVNTVFQnyslfPNMNVFDNVA 101
Cdd:cd03220    37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLL-----GLGGGFN-----PELTGRENIY 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 102 FGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDEPLSALDYKLRKELQQELR 181
Cdd:cd03220   107 LNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLR 186

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2753759418 182 NIQKRlGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNG 220
Cdd:cd03220   187 ELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
1-225 6.22e-26

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 105.07  E-value: 6.22e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   1 MVEKMPILEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEK-- 78
Cdd:PRK10253    1 MTESVARLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEva 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  79 RRVNTVFQNYSLFPNMNVFDNVAFG-----PRLKKMSEKDiQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALA 153
Cdd:PRK10253   81 RRIGLLAQNATTPGDITVQELVARGryphqPLFTRWRKED-EEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLA 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2753759418 154 NDPEVLLLDEPLSALDYKLRKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDI 225
Cdd:PRK10253  160 QETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
 5-225 6.88e-26

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 104.21  E-value: 6.88e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   5 MPILEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAE---KRRV 81
Cdd:PRK10895    1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHaraRRGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  82 NTVFQNYSLFPNMNVFDNVAFGPRLKK-MSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLL 160
Cdd:PRK10895   81 GYLPQEASIFRRLSVYDNLMAVLQIRDdLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFIL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2753759418 161 LDEPLSALDYKLRKELQQELRNIQKRlGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDI 225
Cdd:PRK10895  161 LDEPFAGVDPISVIDIKRIIEHLRDS-GLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
 8-221 1.73e-25

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: 107.98  E-value: 1.73e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   8 LEFSKValSFG---DTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAE--KRRVN 82
Cdd:COG5265   358 VRFENV--SFGydpERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQAslRAAIG 435

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  83 TVFQNYSLFpNMNVFDNVAFGpRLkKMSEKDIQDKVKemlgLVKLSGFERR-------EISE----LSGGQQQRVAIARA 151
Cdd:COG5265   436 IVPQDTVLF-NDTIAYNIAYG-RP-DASEEEVEAAAR----AAQIHDFIESlpdgydtRVGErglkLSGGEKQRVAIART 508

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2753759418 152 LANDPEVLLLDEPLSALDYKLRKELQQELRNIQKrlGITFVFVTH--------DQeealamsdwIFVMHDGLIQQNGT 221
Cdd:COG5265   509 LLKNPPILIFDEATSALDSRTERAIQAALREVAR--GRTTLVIAHrlstivdaDE---------ILVLEAGRIVERGT 575
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
5-216 1.74e-25

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


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 103.03  E-value: 1.74e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   5 MPILEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEK---RRV 81
Cdd:PRK11614    3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKimrEAV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  82 NTVFQNYSLFPNMNVFDNVAFGPRLkkMSEKDIQDKVKEMLGLV-KLsgFERR--EISELSGGQQQRVAIARALANDPEV 158
Cdd:PRK11614   83 AIVPEGRRVFSRMTVEENLAMGGFF--AERDQFQERIKWVYELFpRL--HERRiqRAGTMSGGEQQMLAIGRALMSQPRL 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 159 LLLDEPLSALDYKLrkeLQQELRNIQ--KRLGITFVFVTHDQEEALAMSDWIFVMHDGLI 216
Cdd:PRK11614  159 LLLDEPSLGLAPII---IQQIFDTIEqlREQGMTIFLVEQNANQALKLADRGYVLENGHV 215
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
 8-228 1.86e-25

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: 108.29  E-value: 1.86e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   8 LEFSKVALSFG-DTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVP--AEKRRVNTV 84
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDrhTLRQFINYL 553

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  85 FQNYSLFPNmNVFDNVAFGPRlkkmsEKDIQDKVKEMLGLVKLS--------GFERR---EISELSGGQQQRVAIARALA 153
Cdd:TIGR01193 554 PQEPYIFSG-SILENLLLGAK-----ENVSQDEIWAACEIAEIKddienmplGYQTElseEGSSISGGQKQRIALARALL 627

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2753759418 154 NDPEVLLLDEPLSALDYKLRKELQQELRNIQKRlgiTFVFVTHDQEEAlAMSDWIFVMHDGLIQQNGTPEDIYDE 228
Cdd:TIGR01193 628 TDSKVLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVA-KQSDKIIVLDHGKIIEQGSHDELLDR 698
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
8-225 6.63e-25

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 106.26  E-value: 6.63e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   8 LEFSKVALSF--GDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVIND--VPAEKRRVNT 83
Cdd:PRK11176  342 IEFRNVTFTYpgKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDytLASLRNQVAL 421

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  84 VFQNYSLFpNMNVFDNVAFgPRLKKMSEKDIQDKVK---EMLGLVKL-SGFERrEISE----LSGGQQQRVAIARALAND 155
Cdd:PRK11176  422 VSQNVHLF-NDTIANNIAY-ARTEQYSREQIEEAARmayAMDFINKMdNGLDT-VIGEngvlLSGGQRQRIAIARALLRD 498

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 156 PEVLLLDEPLSALDYKLRKELQQELRNIQKRLgiTFVFVTHdQEEALAMSDWIFVMHDGLIQQNGTPEDI 225
Cdd:PRK11176  499 SPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAH-RLSTIEKADEILVVEDGEIVERGTHAEL 565
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
 2-197 6.99e-25

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: 105.91  E-value: 6.99e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   2 VEKMPILEFSKVALSF-GDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIffegqVINDVPAEKRR 80
Cdd:TIGR02868 329 GLGKPTLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEV-----TLDGVPVSSLD 403

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  81 VNTVFQNYSLFP-NMNVFD-----NVAFGprlkkmsEKDIQD-KVKEMLGLVKLSGFERR-------EISE----LSGGQ 142
Cdd:TIGR02868 404 QDEVRRRVSVCAqDAHLFDttvreNLRLA-------RPDATDeELWAALERVGLADWLRAlpdgldtVLGEggarLSGGE 476

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2753759418 143 QQRVAIARALANDPEVLLLDEPLSALDYKLRKELQQELRNIQKrlGITFVFVTHD 197
Cdd:TIGR02868 477 RQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALS--GRTVVLITHH 529
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
 5-237 8.52e-25

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 101.73  E-value: 8.52e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   5 MPILEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVindvpaekrRVNTV 84
Cdd:PRK09544    2 TSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKL---------RIGYV 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  85 FQNYSLFPNM--NVFDNVAFGPRLKKmseKDIQDKVKEmlglVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLD 162
Cdd:PRK09544   73 PQKLYLDTTLplTVNRFLRLRPGTKK---EDILPALKR----VQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLD 145

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2753759418 163 EPLSALDYKLRKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMhDGLIQQNGTPEDIYDEPinHFVADF 237
Cdd:PRK09544  146 EPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCL-NHHICCSGTPEVVSLHP--EFISMF 217
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
 5-214 1.00e-24

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 105.40  E-value: 1.00e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   5 MPILEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADA--GKIFFEGQV-----INDvpAE 77
Cdd:PRK13549    3 EYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFEGEElqasnIRD--TE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  78 KRRVNTVFQNYSLFPNMNVFDNVAFGPRLKK---MSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALAN 154
Cdd:PRK13549   81 RAGIAIIHQELALVKELSVLENIFLGNEITPggiMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNK 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2753759418 155 DPEVLLLDEPLSALDyklRKELQQELRNIQ--KRLGITFVFVTHDQEEALAMSDWIFVMHDG 214
Cdd:PRK13549  161 QARLLILDEPTASLT---ESETAVLLDIIRdlKAHGIACIYISHKLNEVKAISDTICVIRDG 219
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
 7-181 1.03e-24

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: 100.62  E-value: 1.03e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   7 ILEFSKVALSF---GDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAE--KRRV 81
Cdd:cd03248    11 IVKFQNVTFAYptrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKylHSKV 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  82 NTVFQNYSLFPNmNVFDNVAFG-PRLKKMSEKDIQDKVKEMLGLVKLSGFERREISE----LSGGQQQRVAIARALANDP 156
Cdd:cd03248    91 SLVGQEPVLFAR-SLQDNIAYGlQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEkgsqLSGGQKQRVAIARALIRNP 169

                         170       180
                  ....*....|....*....|....*
gi 2753759418 157 EVLLLDEPLSALDYKLRKELQQELR 181
Cdd:cd03248   170 QVLILDEATSALDAESEQQVQQALY 194
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
 8-214 1.30e-24

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: 97.90  E-value: 1.30e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   8 LEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIffegqvindvpaekrrvntvfqn 87
Cdd:cd03221     1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV----------------------- 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  88 yslfpnmnvfdnvAFGPRLKkmsekdiqdkvkemLGLVklsgferreiSELSGGQQQRVAIARALANDPEVLLLDEPLSA 167
Cdd:cd03221    58 -------------TWGSTVK--------------IGYF----------EQLSGGEKMRLALAKLLLENPNLLLLDEPTNH 100

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2753759418 168 LDYKLRKELQQELRNIQKrlgiTFVFVTHDQE--EALAmsDWIFVMHDG 214
Cdd:cd03221   101 LDLESIEALEEALKEYPG----TVILVSHDRYflDQVA--TKIIELEDG 143
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
13-225 1.56e-24

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 101.40  E-value: 1.56e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  13 VALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVIN--DVPAEKRRVNTVFQNYSL 90
Cdd:PRK10575   17 VSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLEswSSKAFARKVAYLPQQLPA 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  91 FPNMNVFDNVAFG--P---RLKKMSEKDiQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDEPL 165
Cdd:PRK10575   97 AEGMTVRELVAIGryPwhgALGRFGAAD-REKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPT 175

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 166 SALDYKLRKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDI 225
Cdd:PRK10575  176 SALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
 6-214 1.69e-24

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 104.76  E-value: 1.69e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   6 PILEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIffegqvindvpaeKRRVNTVF 85
Cdd:COG0488   314 KVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV-------------KLGETVKI 380

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  86 ----QNYSLF-PNMNVFDNVA-FGPRLKKMSekdiqdkVKEMLGLVKLSGFE-RREISELSGGQQQRVAIARALANDPEV 158
Cdd:COG0488   381 gyfdQHQEELdPDKTVLDELRdGAPGGTEQE-------VRGYLGRFLFSGDDaFKPVGVLSGGEKARLALAKLLLSPPNV 453

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2753759418 159 LLLDEPLSALDYKLRKELQQELRNIQkrlGiTFVFVTHDQE--EALAmsDWIFVMHDG 214
Cdd:COG0488   454 LLLDEPTNHLDIETLEALEEALDDFP---G-TVLLVSHDRYflDRVA--TRILEFEDG 505
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
 22-214 2.40e-24

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


Pssm-ID: 213182 [Multi-domain]  Cd Length: 182  Bit Score: 98.27  E-value: 2.40e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  22 VLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEKRRVNTVF------QNYSLFPNMN 95
Cdd:cd03215    15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAyvpedrKREGLVLDLS 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  96 VFDNVAFGprlkkmsekdiqdkvkemlglvklsgferreiSELSGGQQQRVAIARALANDPEVLLLDEPLSALDYKLRKE 175
Cdd:cd03215    95 VAENIALS--------------------------------SLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAE 142

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2753759418 176 LQQELRNIQKRlGITFVFVTHDQEEALAMSDWIFVMHDG 214
Cdd:cd03215   143 IYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEG 180
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
 21-220 2.82e-24

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: 99.71  E-value: 2.82e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  21 EVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIffegQVINDVPAEKR-----RVNTVF-QNYSLFPNM 94
Cdd:cd03267    35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEV----RVAGLVPWKRRkkflrRIGVVFgQKTQLWWDL 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  95 NVFDNVAFGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDEPLSALDYKLRK 174
Cdd:cd03267   111 PVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQE 190

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2753759418 175 ELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNG 220
Cdd:cd03267   191 NIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
 22-216 5.81e-24

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


Pssm-ID: 213201 [Multi-domain]  Cd Length: 226  Bit Score: 98.50  E-value: 5.81e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  22 VLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADA---GKIFFEGQVINdvPAE-KRRVNTVFQNYSLFPNMNVF 97
Cdd:cd03234    22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRK--PDQfQKCVAYVRQDDILLPGLTVR 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  98 DNVAFGPRLK---KMSEKDIQDKVKEM-LGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDEPLSALDYKLR 173
Cdd:cd03234   100 ETLTYTAILRlprKSSDAIRKKRVEDVlLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTA 179

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2753759418 174 KELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLI 216
Cdd:cd03234   180 LNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEI 222
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
43-216 6.41e-24

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 102.79  E-value: 6.41e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  43 GSGKSTILKLISGQLQADAGKIFFEGQVIN-----D--------VPAEKRRvntvfqnYSLFPNMNVFDNVAFgPRLKKM 109
Cdd:COG1129   288 GAGRTELARALFGADPADSGEIRLDGKPVRirsprDairagiayVPEDRKG-------EGLVLDLSIRENITL-ASLDRL 359

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 110 S---------EKDIQDKVKEMLGlVKLSGFERrEISELSGGQQQRVAIARALANDPEVLLLDEPLSALD-------YKLR 173
Cdd:COG1129   360 SrgglldrrrERALAEEYIKRLR-IKTPSPEQ-PVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDvgakaeiYRLI 437

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2753759418 174 KELQQElrniqkrlGITFVFVTHDQEEALAMSDWIFVMHDGLI 216
Cdd:COG1129   438 RELAAE--------GKAVIVISSELPELLGLSDRILVMREGRI 472
CP_lyasePhnK TIGR02323
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ...
 6-229 7.14e-24

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: 99.13  E-value: 7.14e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   6 PILEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVP------AEKR 79
Cdd:TIGR02323   2 PLLQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELElyqlseAERR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  80 RV-----NTVFQNYSLFPNMNVFDNVAFGPRLKKMSEK---DIQDKVKEMLGLVKLsgfERREISEL----SGGQQQRVA 147
Cdd:TIGR02323  82 RLmrtewGFVHQNPRDGLRMRVSAGANIGERLMAIGARhygNIRATAQDWLEEVEI---DPTRIDDLprafSGGMQQRLQ 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 148 IARALANDPEVLLLDEPLSALDYKLRKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYD 227
Cdd:TIGR02323 159 IARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLD 238


                  ..
gi 2753759418 228 EP 229
Cdd:TIGR02323 239 DP 240
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
 8-220 8.73e-24

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: 97.00  E-value: 8.73e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   8 LEFSKVALSFGDTE--VLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEKRRVNTVF 85
Cdd:cd03247     1 LSINNVSFSYPEQEqqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  86 -QNYSLFpNMNVFDNVafGPRlkkmsekdiqdkvkemlglvklsgferreiseLSGGQQQRVAIARALANDPEVLLLDEP 164
Cdd:cd03247    81 nQRPYLF-DTTLRNNL--GRR--------------------------------FSGGERQRLALARILLQDAPIVLLDEP 125

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2753759418 165 LSALDYKLRKELqqeLRNIQKRL-GITFVFVTHdQEEALAMSDWIFVMHDGLIQQNG 220
Cdd:cd03247   126 TVGLDPITERQL---LSLIFEVLkDKTLIWITH-HLTGIEHMDKILFLENGKIIMQG 178
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
 19-214 1.43e-23

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: 97.40  E-value: 1.43e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  19 DTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEKRRVNTVFQ-----NYSLFPN 93
Cdd:cd03290    13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSvayaaQKPWLLN 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  94 MNVFDNVAFGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISE----LSGGQQQRVAIARALANDPEVLLLDEPLSALD 169
Cdd:cd03290    93 ATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGErginLSGGQRQRICVARALYQNTNIVFLDDPFSALD 172

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2753759418 170 YKLRKELQQE--LRNIQ--KRlgiTFVFVTHdQEEALAMSDWIFVMHDG 214
Cdd:cd03290   173 IHLSDHLMQEgiLKFLQddKR---TLVLVTH-KLQYLPHADWIIAMKDG 217
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
 30-229 2.37e-23

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 101.86  E-value: 2.37e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  30 LESGKFYTLLGPSGSGKST----ILKLISGQlqadAGKIFFEGQVINDVPAEK-----RRVNTVFQN--YSLFPNMNVFD 98
Cdd:PRK10261  347 LWPGETLSLVGESGSGKSTtgraLLRLVESQ----GGEIIFNGQRIDTLSPGKlqalrRDIQFIFQDpyASLDPRQTVGD 422

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  99 NVAFGPRLKKMSE-KDIQDKVKEMLGLVKL-SGFERREISELSGGQQQRVAIARALANDPEVLLLDEPLSALDYKLRKEL 176
Cdd:PRK10261  423 SIMEPLRVHGLLPgKAAAARVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQI 502

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2753759418 177 QQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDEP 229
Cdd:PRK10261  503 INLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENP 555
SufC COG0396
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ...
 16-223 2.68e-23

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


Pssm-ID: 440165 [Multi-domain]  Cd Length: 245  Bit Score: 97.45  E-value: 2.68e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  16 SFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISG--QLQADAGKIFFEGQVINDVPAEKR---RVNTVFQNYSL 90
Cdd:COG0396     9 SVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGhpKYEVTSGSILLDGEDILELSPDERaraGIFLAFQYPVE 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  91 FPNMNVFD--NVAFGP-RLKKMSEKDIQDKVKEMLGLVKLS-GFERREISE-LSGGQQQRVAIARALANDPEVLLLDEPL 165
Cdd:COG0396    89 IPGVSVSNflRTALNArRGEELSAREFLKLLKEKMKELGLDeDFLDRYVNEgFSGGEKKRNEILQMLLLEPKLAILDETD 168

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2753759418 166 SALD---YKLRKELQQELRNiQKRlgiTFVFVTHdQEEALAM--SDWIFVMHDGLIQQNGTPE 223
Cdd:COG0396   169 SGLDidaLRIVAEGVNKLRS-PDR---GILIITH-YQRILDYikPDFVHVLVDGRIVKSGGKE 226
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
19-229 3.19e-23

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


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 101.33  E-value: 3.19e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  19 DTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAE--KRRVNTVFQNYSLFPNmNV 96
Cdd:PRK10789  327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDswRSRLAVVSQTPFLFSD-TV 405

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  97 FDNVAFG-PrlkKMSEKDIQDKVK------EMLGLVKlsGFErREISE----LSGGQQQRVAIARALANDPEVLLLDEPL 165
Cdd:PRK10789  406 ANNIALGrP---DATQQEIEHVARlasvhdDILRLPQ--GYD-TEVGErgvmLSGGQKQRISIARALLLNAEILILDDAL 479

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2753759418 166 SALDYKLRKELQQELRniQKRLGITFVFVTHdQEEALAMSDWIFVMHDGLIQQNGTPEDIYDEP 229
Cdd:PRK10789  480 SAVDGRTEHQILHNLR--QWGEGRTVIISAH-RLSALTEASEILVMQHGHIAQRGNHDQLAQQS 540
ycf16 CHL00131
sulfate ABC transporter protein; Validated
 1-223 4.22e-23

sulfate ABC transporter protein; Validated


Pssm-ID: 214372 [Multi-domain]  Cd Length: 252  Bit Score: 97.02  E-value: 4.22e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   1 MVEKMPILEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQ--LQADAGKIFFEGQVINDVPAEK 78
Cdd:CHL00131    1 MNKNKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEPEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  79 RR---VNTVFQNYSLFPNMNVFD--NVAFGPRLKKMSEKDIQ-----DKVKEMLGLVKLS-GFERREISE-LSGGQQQRV 146
Cdd:CHL00131   81 RAhlgIFLAFQYPIEIPGVSNADflRLAYNSKRKFQGLPELDpleflEIINEKLKLVGMDpSFLSRNVNEgFSGGEKKRN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 147 AIARALANDPEVLLLDEPLSALDYKLRKELQQELrNIQKRLGITFVFVTHDQEeaL---AMSDWIFVMHDGLIQQNGTPE 223
Cdd:CHL00131  161 EILQMALLDSELAILDETDSGLDIDALKIIAEGI-NKLMTSENSIILITHYQR--LldyIKPDYVHVMQNGKIIKTGDAE 237
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
 5-229 8.49e-23

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 96.15  E-value: 8.49e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   5 MPILEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVP------AEK 78
Cdd:PRK11701    4 QPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDlyalseAER 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  79 RRV-----NTVFQNYSLFPNMNVFDNVAFGPRLKKMSEK---DIQDKVKEMLGLVKLsgfERREISEL----SGGQQQRV 146
Cdd:PRK11701   84 RRLlrtewGFVHQHPRDGLRMQVSAGGNIGERLMAVGARhygDIRATAGDWLERVEI---DAARIDDLpttfSGGMQQRL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 147 AIARALANDPEVLLLDEPLSALDYKLRKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIY 226
Cdd:PRK11701  161 QIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQVL 240


                  ...
gi 2753759418 227 DEP 229
Cdd:PRK11701  241 DDP 243
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
 8-221 1.01e-22

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 99.90  E-value: 1.01e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   8 LEFSKVALSFGDTE--VLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEKRR--VNT 83
Cdd:PRK11160  339 LTLNNVSFTYPDQPqpVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRqaISV 418

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  84 VFQNYSLFpNMNVFDNVAFGprlkkmSEKDIQDKVKEML---GLVKL-SGFERRE--ISE----LSGGQQQRVAIARALA 153
Cdd:PRK11160  419 VSQRVHLF-SATLRDNLLLA------APNASDEALIEVLqqvGLEKLlEDDKGLNawLGEggrqLSGGEQRRLGIARALL 491

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2753759418 154 NDPEVLLLDEPLSALDyklRKELQQELRNIQKR-LGITFVFVTHdQEEALAMSDWIFVMHDGLIQQNGT 221
Cdd:PRK11160  492 HDAPLLLLDEPTEGLD---AETERQILELLAEHaQNKTVLMITH-RLTGLEQFDRICVMDNGQIIEQGT 556
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
21-241 1.83e-22

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 95.63  E-value: 1.83e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  21 EVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVIN--DVPAEKRRVNTVFQN--YSLFPNMNV 96
Cdd:PRK15112   27 EAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDYSYRSQRIRMIFQDpsTSLNPRQRI 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  97 FDNVAFGPRLKkmSEKDIQDKVKEMLGLVKLSGFERREIS----ELSGGQQQRVAIARALANDPEVLLLDEPLSALDYKL 172
Cdd:PRK15112  107 SQILDFPLRLN--TDLEPEQREKQIIETLRQVGLLPDHASyyphMLAPGQKQRLGLARALILRPKVIIADEALASLDMSM 184

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2753759418 173 RKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDEPIN----HFVADFIGET 241
Cdd:PRK15112  185 RSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPLHeltkRLIAGHFGEA 257
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
 13-229 1.93e-22

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 98.76  E-value: 1.93e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  13 VALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLqADAGKIFFEGQVINDVPAE--KRRVNTVFQNYSL 90
Cdd:PRK11174  356 EILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPEswRKHLSWVGQNPQL 434

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  91 FPNmNVFDNVAFGPrlKKMSEKDIQD-----KVKEMLGLVKLsGFERrEISE----LSGGQQQRVAIARALANDPEVLLL 161
Cdd:PRK11174  435 PHG-TLRDNVLLGN--PDASDEQLQQalenaWVSEFLPLLPQ-GLDT-PIGDqaagLSVGQAQRLALARALLQPCQLLLL 509

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2753759418 162 DEPLSALDYKLRKELQQELRNIQKRLgiTFVFVTHdQEEALAMSDWIFVMHDGLIQQNGTPEDIYDEP 229
Cdd:PRK11174  510 DEPTASLDAHSEQLVMQALNAASRRQ--TTLMVTH-QLEDLAQWDQIWVMQDGQIVQQGDYAELSQAG 574
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
 10-214 2.16e-22

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: 93.38  E-value: 2.16e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  10 FSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQL--QADAGKIFFEGQvinDVPAE--KRRVNTVF 85
Cdd:cd03213    12 TVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRtgLGVSGEVLINGR---PLDKRsfRKIIGYVP 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  86 QNYSLFPNMNVFDNVAFGPRLKKmsekdiqdkvkemlglvklsgferreiseLSGGQQQRVAIARALANDPEVLLLDEPL 165
Cdd:cd03213    89 QDDILHPTLTVRETLMFAAKLRG-----------------------------LSGGERKRVSIALELVSNPSLLFLDEPT 139

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2753759418 166 SALDYKLRKELQQELRNIQKrLGITFVFVTHD-QEEALAMSDWIFVMHDG 214
Cdd:cd03213   140 SGLDSSSALQVMSLLRRLAD-TGRTIICSIHQpSSEIFELFDKLLLLSQG 188
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
 26-228 3.00e-22

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: 98.34  E-value: 3.00e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  26 IDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFE-GQVINDV----PAEKRRVNT----VFQNYSLFPNMNV 96
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEWVDMtkpgPDGRGRAKRyigiLHQEYDLYPHRTV 382

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  97 FDNvafgprLKKMSEKDIQDKVKEMLGLV--KLSGFER---REI-----SELSGGQQQRVAIARALANDPEVLLLDEPLS 166
Cdd:TIGR03269 383 LDN------LTEAIGLELPDELARMKAVItlKMVGFDEekaEEIldkypDELSEGERHRVALAQVLIKEPRIVILDEPTG 456

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2753759418 167 ALDYKLRKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDE 228
Cdd:TIGR03269 457 TMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIVEE 518
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
 8-268 3.55e-22

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: 97.95  E-value: 3.55e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   8 LEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISG--QLQADAGKIFFE-------GQVinDVPAE- 77
Cdd:TIGR03269   1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIIYHvalcekcGYV--ERPSKv 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  78 -----------------------------KRRVNTVFQ-NYSLFPNMNVFDNVafgprLKKMSE-----KDIQDKVKEML 122
Cdd:TIGR03269  79 gepcpvcggtlepeevdfwnlsdklrrriRKRIAIMLQrTFALYGDDTVLDNV-----LEALEEigyegKEAVGRAVDLI 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 123 GLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDEPLSALDYKLRKELQQELRNIQKRLGITFVFVTHDQEEAL 202
Cdd:TIGR03269 154 EMVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIE 233

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2753759418 203 AMSDWIFVMHDGLIQQNGTPediyDEPINHF---VADFIGETNIVPG--IMKydylVHFVGKDFENVDAGM 268
Cdd:TIGR03269 234 DLSDKAIWLENGEIKEEGTP----DEVVAVFmegVSEVEKECEVEVGepIIK----VRNVSKRYISVDRGV 296
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
 12-214 4.10e-22

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


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 93.48  E-value: 4.10e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  12 KVALSFGDTE------VLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFegqvinDVPAEKrrvntvf 85
Cdd:COG2401    29 IVLEAFGVELrvveryVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCV------DVPDNQ------- 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  86 qnysLFPNMNVFDNVAfgprlkkmSEKDIQDKVkEMLGLVKLSG--FERREISELSGGQQQRVAIARALANDPEVLLLDE 163
Cdd:COG2401    96 ----FGREASLIDAIG--------RKGDFKDAV-ELLNAVGLSDavLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDE 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2753759418 164 PLSALDYKLRKELQQELRNIQKRLGITFVFVTHDQE--EALAmSDWIFVMHDG 214
Cdd:COG2401   163 FCSHLDRQTAKRVARNLQKLARRAGITLVVATHHYDviDDLQ-PDLLIFVGYG 214
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
 5-197 9.37e-22

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 96.94  E-value: 9.37e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   5 MPILEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVI-----NDVPaekR 79
Cdd:PRK11147    1 MSLISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIvarlqQDPP---R 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  80 RVNTvfqnyslfpnmNVFDNVAFG---------------------------PRLKKMSEK-DIQD------KVKEMLGLV 125
Cdd:PRK11147   78 NVEG-----------TVYDFVAEGieeqaeylkryhdishlvetdpseknlNELAKLQEQlDHHNlwqlenRINEVLAQL 146

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2753759418 126 KLSGfeRREISELSGGQQQRVAIARALANDPEVLLLDEPLSALDYKLRKELQQELRNIQKrlgiTFVFVTHD 197
Cdd:PRK11147  147 GLDP--DAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQG----SIIFISHD 212
BtuD COG4138
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ...
 38-230 1.50e-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: 1.50e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  38 LLGPSGSGKSTILKLISGQLQAdAGKIFFEGQVINDVPA-EKRRVNTVF-QNYSLFPNMNVFDNVAFGPRLKKMSEKDIQ 115
Cdd:COG4138    27 LIGPNGAGKSTLLARMAGLLPG-QGEILLNGRPLSDWSAaELARHRAYLsQQQSPPFAMPVFQYLALHQPAGASSEAVEQ 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 116 --DKVKEMLGLV-KLSgferREISELSGGQQQRVAIARAL-----ANDPE--VLLLDEPLSALD-------YKLRKELQQ 178
Cdd:COG4138   106 llAQLAEALGLEdKLS----RPLTQLSGGEWQRVRLAAVLlqvwpTINPEgqLLLLDEPMNSLDvaqqaalDRLLRELCQ 181

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2753759418 179 elrniqkrLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDEPI 230
Cdd:COG4138   182 --------QGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMTPEN 225
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
8-196 2.74e-21

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 90.63  E-value: 2.74e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   8 LEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEKRRvntvfqn 87
Cdd:PRK13538    2 LEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQ------- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  88 ySLF---------PNMNVFDNVAFGPRLKKMSEkdiQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEV 158
Cdd:PRK13538   75 -DLLylghqpgikTELTALENLRFYQRLHGPGD---DEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPL 150

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2753759418 159 LLLDEPLSALDYKLRKELQQELRNIQKRLGITfVFVTH 196
Cdd:PRK13538  151 WILDEPFTAIDKQGVARLEALLAQHAEQGGMV-ILTTH 187
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
5-214 7.28e-21

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 93.82  E-value: 7.28e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   5 MPILEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVI---NDVPAEKRRV 81
Cdd:PRK11288    2 SPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfaSTTAALAAGV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  82 NTVFQNYSLFPNMNVFDNVAFG--P-RLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEV 158
Cdd:PRK11288   82 AIIYQELHLVPEMTVAENLYLGqlPhKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARV 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2753759418 159 LLLDEPLSALD-------YKLRKELQQELRNIqkrlgitfVFVTHDQEEALAMSDWIFVMHDG 214
Cdd:PRK11288  162 IAFDEPTSSLSareieqlFRVIRELRAEGRVI--------LYVSHRMEEIFALCDAITVFKDG 216
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
 8-196 1.03e-20

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: 88.95  E-value: 1.03e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   8 LEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEKRRvNTVFQN 87
Cdd:TIGR01189   1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHE-NILYLG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  88 YS--LFPNMNVFDNVAFGPRLKKMSEKDIQDkvkeMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDEPL 165
Cdd:TIGR01189  80 HLpgLKPELSALENLHFWAAIHGGAQRTIED----ALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPT 155

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2753759418 166 SALDYKLRKELQQELRNIQKRLGITfVFVTH 196
Cdd:TIGR01189 156 TALDKAGVALLAGLLRAHLARGGIV-LLTTH 185
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
 1-245 2.26e-20

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 90.94  E-value: 2.26e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   1 MVEKMPILEFSKVALSF----GDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQAD---AGKIFFEGQVI-- 71
Cdd:PRK09473    6 QQQADALLDVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREIln 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  72 ------NDVPAEKrrVNTVFQN--YSLFPNMNVFDNVAFGPRL-KKMSEKDIQDKVKEMLGLVKLSGfERREIS----EL 138
Cdd:PRK09473   86 lpekelNKLRAEQ--ISMIFQDpmTSLNPYMRVGEQLMEVLMLhKGMSKAEAFEESVRMLDAVKMPE-ARKRMKmyphEF 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 139 SGGQQQRVAIARALANDPEVLLLDEPLSALDYKLRKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQ 218
Cdd:PRK09473  163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTME 242

                         250       260
                  ....*....|....*....|....*..
gi 2753759418 219 NGTPEDIYDEPINHFVadfIGETNIVP 245
Cdd:PRK09473  243 YGNARDVFYQPSHPYS---IGLLNAVP 266
hmuV PRK13547
heme ABC transporter ATP-binding protein;
22-225 2.79e-20

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 89.50  E-value: 2.79e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  22 VLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADA--------GKIFFEGQVINDVPAEK---RRVNTVFQNYSL 90
Cdd:PRK13547   16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGaprgarvtGDVTLNGEPLAAIDAPRlarLRAVLPQAAQPA 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  91 FPnMNVFDNVAFG--PRLKKMSEKDIQDK--VKEMLGLVKLSGFERREISELSGGQQQRVAIARALAN---------DPE 157
Cdd:PRK13547   96 FA-FSAREIVLLGryPHARRAGALTHRDGeiAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQlwpphdaaqPPR 174

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2753759418 158 VLLLDEPLSALDYKLRKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDI 225
Cdd:PRK13547  175 YLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADV 242
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
 8-223 4.30e-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: 87.20  E-value: 4.30e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   8 LEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISG--QLQADAGKIFFEGQVINDVPAEKRRVNTVF 85
Cdd:cd03217     1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEILFKGEDITDLPPEERARLGIF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  86 qnyslfpnmnvfdnVAFgprlkkmsekdiQDKVkEMLGlVKLSGFeRREISE-LSGGQQQRVAIARALANDPEVLLLDEP 164
Cdd:cd03217    81 --------------LAF------------QYPP-EIPG-VKNADF-LRYVNEgFSGGEKKRNEILQLLLLEPDLAILDEP 131

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2753759418 165 LSALD---YKLRKELQQELRNiqkrLGITFVFVTHDQEEALAM-SDWIFVMHDGLIQQNGTPE 223
Cdd:cd03217   132 DSGLDidaLRLVAEVINKLRE----EGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDKE 190
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
6-230 4.34e-20

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 91.77  E-value: 4.34e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   6 PILEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVP---AEKRRVN 82
Cdd:PRK09700    4 PYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDhklAAQLGIG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  83 TVFQNYSLFPNMNVFDNVAFGPRLKK-------MSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALAND 155
Cdd:PRK09700   84 IIYQELSVIDELTVLENLYIGRHLTKkvcgvniIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLD 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2753759418 156 PEVLLLDEPLSALDYKLRKELQQELRNIQKRlGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDEPI 230
Cdd:PRK09700  164 AKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDI 237
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
 23-216 1.30e-19

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 90.06  E-value: 1.30e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  23 LKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVP------------AEKRRVN------TV 84
Cdd:PRK10762  268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSpqdglangivyiSEDRKRDglvlgmSV 347

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  85 FQNYSLfPNMNVFDNVAFgpRLKKMSEKDIQDKVKEMLGlVKLSGFERReISELSGGQQQRVAIARALANDPEVLLLDEP 164
Cdd:PRK10762  348 KENMSL-TALRYFSRAGG--SLKHADEQQAVSDFIRLFN-IKTPSMEQA-IGLLSGGNQQKVAIARGLMTRPKVLILDEP 422

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2753759418 165 LSALDYKLRKELQQeLRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLI 216
Cdd:PRK10762  423 TRGVDVGAKKEIYQ-LINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 21-244 1.41e-19

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


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 88.22  E-value: 1.41e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  21 EVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIffegQVINDVPAEKRRVN-----TVF-QNYSLFPNM 94
Cdd:COG4586    36 EAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEV----RVLGYVPFKRRKEFarrigVVFgQRSQLWWDL 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  95 NVFDNVAFgprLKKM---SEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDEPLSALDYK 171
Cdd:COG4586   112 PAIDSFRL---LKAIyriPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVV 188

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2753759418 172 LRKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIqqngtpedIYDEPINHFVADFIGETNIV 244
Cdd:COG4586   189 SKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRI--------IYDGSLEELKERFGPYKTIV 253
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
 8-196 1.50e-19

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: 86.01  E-value: 1.50e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   8 LEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDV-PAEKRRVNTVFQ 86
Cdd:cd03231     1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQrDSIARGLLYLGH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  87 NYSLFPNMNVFDNVAFGPRLKKmsekdiQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDEPLS 166
Cdd:cd03231    81 APGIKTTLSVLENLRFWHADHS------DEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTT 154

                         170       180       190
                  ....*....|....*....|....*....|
gi 2753759418 167 ALDYKLRKELQQELRNIQKRLGITfVFVTH 196
Cdd:cd03231   155 ALDKAGVARFAEAMAGHCARGGMV-VLTTH 183
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
 5-229 2.25e-19

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 87.87  E-value: 2.25e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   5 MPILEFSKVALSFGDTEV-LKEIDLV---LESGKFYTLLGPSGSGKS----TILKLIS--GQLQADagKIFFEGQVINDV 74
Cdd:PRK11022    1 MALLNVDKLSVHFGDESApFRAVDRIsysVKQGEVVGIVGESGSGKSvsslAIMGLIDypGRVMAE--KLEFNGQDLQRI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  75 PAEKRR------VNTVFQN--YSLFPNMNVFDNVAFGPRLKKM-SEKDIQDKVKEMLGLVKLSGFERR---EISELSGGQ 142
Cdd:PRK11022   79 SEKERRnlvgaeVAMIFQDpmTSLNPCYTVGFQIMEAIKVHQGgNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGM 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 143 QQRVAIARALANDPEVLLLDEPLSALDYKLRKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTP 222
Cdd:PRK11022  159 SQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKA 238


                  ....*..
gi 2753759418 223 EDIYDEP 229
Cdd:PRK11022  239 HDIFRAP 245
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
9-228 2.38e-19

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 89.64  E-value: 2.38e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   9 EFSKVALSF-GDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEKRRVN--TVF 85
Cdd:PRK13657  336 EFDDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNiaVVF 415

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  86 QNYSLFpNMNVFDNVafgpRLKKMSEKDiqDKVKEMLGLVKLSGF-ERRE------ISE----LSGGQQQRVAIARALAN 154
Cdd:PRK13657  416 QDAGLF-NRSIEDNI----RVGRPDATD--EEMRAAAERAQAHDFiERKPdgydtvVGErgrqLSGGERQRLAIARALLK 488

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2753759418 155 DPEVLLLDEPLSALDYKLRKELQQELRNIQK-RlgITFVfVTHdQEEALAMSDWIFVMHDGLIQQNGTpediYDE 228
Cdd:PRK13657  489 DPPILILDEATSALDVETEAKVKAALDELMKgR--TTFI-IAH-RLSTVRNADRILVFDNGRVVESGS----FDE 555
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
 18-169 2.49e-19

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 85.31  E-value: 2.49e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  18 GDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQvindvPAEKRRVNTVF-----QNySLFP 92
Cdd:PRK13539   13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGG-----DIDDPDVAEAChylghRN-AMKP 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2753759418  93 NMNVFDNVAFGPRLKKMSEKDIQdkvkEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDEPLSALD 169
Cdd:PRK13539   87 ALTVAENLEFWAAFLGGEELDIA----AALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALD 159
PTZ00243 PTZ00243
ABC transporter; Provisional
 21-230 2.66e-19

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 90.22  E-value: 2.66e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   21 EVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEgQVINDVPAEKRRVNTVFQNYSLFpnmnvFDnv 100
Cdd:PTZ00243   674 VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE-RSIAYVPQQAWIMNATVRGNILF-----FD-- 745

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  101 afgprlkKMSEKDIQDKVK----EMlGLVKLSGFERREISE----LSGGQQQRVAIARALANDPEVLLLDEPLSALDYKL 172
Cdd:PTZ00243   746 -------EEDAARLADAVRvsqlEA-DLAQLGGGLETEIGEkgvnLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHV 817

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2753759418  173 RKELQQELrnIQKRL-GITFVFVTHdQEEALAMSDWIFVMHDGLIQQNGTPEDIYDEPI 230
Cdd:PTZ00243   818 GERVVEEC--FLGALaGKTRVLATH-QVHVVPRADYVVALGDGRVEFSGSSADFMRTSL 873
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
 21-232 3.37e-19

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 88.95  E-value: 3.37e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  21 EVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVIND-------------VPaEKRRVNTVFQN 87
Cdd:PRK15439  277 EGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINAlstaqrlarglvyLP-EDRQSSGLYLD 355

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  88 YSLFPNMN--VFDNVAFGPRLKKmsEKDIQDKVKEMLGlVKLSGfERREISELSGGQQQRVAIARALANDPEVLLLDEPL 165
Cdd:PRK15439  356 APLAWNVCalTHNRRGFWIKPAR--ENAVLERYRRALN-IKFNH-AEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPT 431

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2753759418 166 SALDYKLRKELQQELRNIQKRlGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDEPINH 232
Cdd:PRK15439  432 RGVDVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEISGALTGAAINVDTIMR 497
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
 26-222 4.04e-19

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: 89.69  E-value: 4.04e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   26 IDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVI-NDVPAEKRRVNTVFQNYSLFPNMNVFDNVAFGP 104
Cdd:TIGR01257  949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIeTNLDAVRQSLGMCPQHNILFHHLTVAEHILFYA 1028

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  105 RLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDEPLSALDYKLRKELQQELrnIQ 184
Cdd:TIGR01257 1029 QLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL--LK 1106

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 2753759418  185 KRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTP 222
Cdd:TIGR01257 1107 YRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
 18-227 7.16e-19

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: 88.85  E-value: 7.16e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   18 GDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINdVPAEkrrvnTVFQNYSLFpnmnvf 97
Cdd:TIGR00957  649 DLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAY-VPQQ-----AWIQNDSLR------ 716

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   98 DNVAFGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISE----LSGGQQQRVAIARALANDPEVLLLDEPLSALDYKLR 173
Cdd:TIGR00957  717 ENILFGKALNEKYYQQVLEACALLPDLEILPSGDRTEIGEkgvnLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVG 796

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2753759418  174 KELQQELRNIQKRL-GITFVFVTHDQeEALAMSDWIFVMHDGLIQQNGTPEDIYD 227
Cdd:TIGR00957  797 KHIFEHVIGPEGVLkNKTRILVTHGI-SYLPQVDVIIVMSGGKISEMGSYQELLQ 850
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
 13-214 8.00e-19

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 87.86  E-value: 8.00e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  13 VALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVIN---DVPAEKRRVNTVFQNYS 89
Cdd:PRK10982    4 ISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfksSKEALENGISMVHQELN 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  90 LFPNMNVFDNVAFGPRLKK---MSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDEPLS 166
Cdd:PRK10982   84 LVLQRSVMDNMWLGRYPTKgmfVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTS 163

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2753759418 167 ALDYKLRKELQQELRNIQKRlGITFVFVTHDQEEALAMSDWIFVMHDG 214
Cdd:PRK10982  164 SLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDG 210
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
 20-229 8.14e-19

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 87.99  E-value: 8.14e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  20 TEVLKEIDLVLESGKFYTLLGPSGSGKS-TILKLISgQLQADAGKIFFEG--------QVIN---DVPAEKRRVN----- 82
Cdd:PRK10261   29 IAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMR-LLEQAGGLVQCDKmllrrrsrQVIElseQSAAQMRHVRgadma 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  83 TVFQN--YSLFPNMNVFDNVAFGPRLKK-MSEKDIQDKVKEMLGLVKLSGFE---RREISELSGGQQQRVAIARALANDP 156
Cdd:PRK10261  108 MIFQEpmTSLNPVFTVGEQIAESIRLHQgASREEAMVEAKRMLDQVRIPEAQtilSRYPHQLSGGMRQRVMIAMALSCRP 187

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2753759418 157 EVLLLDEPLSALDYKLRKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDEP 229
Cdd:PRK10261  188 AVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAP 260
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 29-212 9.16e-19

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: 87.92  E-value: 9.16e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  29 VLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIffegqvinDVPAEKRRV-----NTVFQNYslfpnmnvFDNVAFG 103
Cdd:COG1245    95 VPKKGKVTGILGPNGIGKSTALKILSGELKPNLGDY--------DEEPSWDEVlkrfrGTELQDY--------FKKLANG 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 104 --------------PR---------LKKMSEKDIQDKVKEMLGLVKLSGferREISELSGGQQQRVAIARALANDPEVLL 160
Cdd:COG1245   159 eikvahkpqyvdliPKvfkgtvrelLEKVDERGKLDELAEKLGLENILD---RDISELSGGELQRVAIAAALLRDADFYF 235

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2753759418 161 LDEPLSALDYKLRKELQQELRNIQKRlGITFVFVTHDqeeaLA----MSDWIFVMH 212
Cdd:COG1245   236 FDEPSSYLDIYQRLNVARLIRELAEE-GKYVLVVEHD----LAildyLADYVHILY 286
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
 8-196 1.18e-18

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 87.56  E-value: 1.18e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   8 LEFSKVALSFGDTEVL-KEIDLVLESGKFYTLLGPSGSGKSTILKLISGqlqadagkI--FFEGQVIndVPAEKRrvnTV 84
Cdd:COG4178   363 LALEDLTLRTPDGRPLlEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG--------LwpYGSGRIA--RPAGAR---VL 429

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  85 F---QNYslFPNMNVFDNVAFgPRlkkmSEKDIQD-KVKEMLGLVKLSGF------ERREISELSGGQQQRVAIARALAN 154
Cdd:COG4178   430 FlpqRPY--LPLGTLREALLY-PA----TAEAFSDaELREALEAVGLGHLaerldeEADWDQVLSLGEQQRLAFARLLLH 502

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2753759418 155 DPEVLLLDEPLSALDYKLRKELQQELRniQKRLGITFVFVTH 196
Cdd:COG4178   503 KPDWLFLDEATSALDEENEAALYQLLR--EELPGTTVISVGH 542
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
23-226 1.84e-18

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 84.55  E-value: 1.84e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  23 LKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVpAEKRRVNTVFQNYSL---FPNMnVFDN 99
Cdd:PRK15056   23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQA-LQKNLVAYVPQSEEVdwsFPVL-VEDV 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 100 VAFGPR-----LKKMSEKDiQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDEPLSALDYKLRK 174
Cdd:PRK15056  101 VMMGRYghmgwLRRAKKRD-RQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEA 179

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2753759418 175 ELQQELRNIQKRlGITFVFVTHDQEEALAMSDWIfVMHDGLIQQNGTPEDIY 226
Cdd:PRK15056  180 RIISLLRELRDE-GKTMLVSTHNLGSVTEFCDYT-VMVKGTVLASGPTETTF 229
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
 6-214 3.21e-18

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 85.83  E-value: 3.21e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   6 PILEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVIN-DVPAEKRR--VN 82
Cdd:PRK10762    3 ALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfNGPKSSQEagIG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  83 TVFQNYSLFPNMNVFDNV--------AFGPRL-KKMSEKdiQDKVKEMLGLVKLSgfeRREISELSGGQQQRVAIARALA 153
Cdd:PRK10762   83 IIHQELNLIPQLTIAENIflgrefvnRFGRIDwKKMYAE--ADKLLARLNLRFSS---DKLVGELSIGEQQMVEIAKVLS 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2753759418 154 NDPEVLLLDEPLSALD-------YKLRKELQQELRNIqkrlgitfVFVTHDQEEALAMSDWIFVMHDG 214
Cdd:PRK10762  158 FESKVIIMDEPTDALTdteteslFRVIRELKSQGRGI--------VYISHRLKEIFEICDDVTVFRDG 217
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
 21-246 3.63e-18

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


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 86.25  E-value: 3.63e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  21 EVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQAD---AGKIFFEGQVInDVPAEKRRVNTVFQNYSLFPNMNVF 97
Cdd:TIGR00955  39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPI-DAKEMRAISAYVQQDDLFIPTLTVR 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  98 DNVAFGPRLK---KMSEKDIQDKVKE---MLGLVK----LSGFERReISELSGGQQQRVAIARALANDPEVLLLDEPLSA 167
Cdd:TIGR00955 118 EHLMFQAHLRmprRVTKKEKRERVDEvlqALGLRKcantRIGVPGR-VKGLSGGERKRLAFASELLTDPPLLFCDEPTSG 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 168 LDYKLRKELQQELRNIQKRlGITFVFVTHD-QEEALAMSDWIFVMHDGLIQQNGTPE---DIYDE-----PINHFVADF- 237
Cdd:TIGR00955 197 LDSFMAYSVVQVLKGLAQK-GKTIICTIHQpSSELFELFDKIILMAEGRVAYLGSPDqavPFFSDlghpcPENYNPADFy 275


                  ....*....
gi 2753759418 238 IGETNIVPG 246
Cdd:TIGR00955 276 VQVLAVIPG 284
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
29-208 5.14e-18

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 85.63  E-value: 5.14e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  29 VLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIffegqvinDVPAEKRRV-----NTVFQNYslfpnmnvFDNVAFG 103
Cdd:PRK13409   95 IPKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDY--------EEEPSWDEVlkrfrGTELQNY--------FKKLYNG 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 104 --------------PR---------LKKMSEKDIQDKVKEMLGLVKLSGferREISELSGGQQQRVAIARALANDPEVLL 160
Cdd:PRK13409  159 eikvvhkpqyvdliPKvfkgkvrelLKKVDERGKLDEVVERLGLENILD---RDISELSGGELQRVAIAAALLRDADFYF 235

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2753759418 161 LDEPLSALDYKLRKELQQELRNIQKrlGITFVFVTHDqeeaLAMSDWI 208
Cdd:PRK13409  236 FDEPTSYLDIRQRLNVARLIRELAE--GKYVLVVEHD----LAVLDYL 277
PLN03130 PLN03130
ABC transporter C family member; Provisional
 16-225 8.50e-18

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 85.56  E-value: 8.50e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   16 SFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFfegqVINDVPAEKRRVNTVFqnyslfpNMN 95
Cdd:PLN03130   626 SKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASV----VIRGTVAYVPQVSWIF-------NAT 694

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   96 VFDNVAFGPRLkkmsEKDIQDKVKEMLGLVK----LSGFERREISE----LSGGQQQRVAIARALANDPEVLLLDEPLSA 167
Cdd:PLN03130   695 VRDNILFGSPF----DPERYERAIDVTALQHdldlLPGGDLTEIGErgvnISGGQKQRVSMARAVYSNSDVYIFDDPLSA 770

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2753759418  168 LDYKLRKE-----LQQELRniqkrlGITFVFVThDQEEALAMSDWIFVMHDGLIQQNGTPEDI 225
Cdd:PLN03130   771 LDAHVGRQvfdkcIKDELR------GKTRVLVT-NQLHFLSQVDRIILVHEGMIKEEGTYEEL 826
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
 6-216 8.90e-18

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 84.69  E-value: 8.90e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   6 PILEFSKV-ALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEKRRVNTV 84
Cdd:COG3845   256 VVLEVENLsVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLGV 335

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  85 F------QNYSLFPNMNVFDNVAFG----PRLKK---MSEKDIQDKVKEMLGL--VKLSGFERReISELSGGQQQRVAIA 149
Cdd:COG3845   336 AyipedrLGRGLVPDMSVAENLILGryrrPPFSRggfLDRKAIRAFAEELIEEfdVRTPGPDTP-ARSLSGGNQQKVILA 414

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2753759418 150 RALANDPEVLLLDEPLSALD----YKLRKELqQELRNiqKRLGItfVFVTHDQEEALAMSDWIFVMHDGLI 216
Cdd:COG3845   415 RELSRDPKLLIAAQPTRGLDvgaiEFIHQRL-LELRD--AGAAV--LLISEDLDEILALSDRIAVMYEGRI 480
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
7-225 1.10e-17

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 84.79  E-value: 1.10e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   7 ILEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISG--QLQadagkiffEGQVI---NDVpAEKRRV 81
Cdd:NF033858    1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGarKIQ--------QGRVEvlgGDM-ADARHR 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  82 NTVFQ-----------NysLFPNMNVFDNVAFGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIAR 150
Cdd:NF033858   72 RAVCPriaympqglgkN--LYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCC 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2753759418 151 ALANDPEVLLLDEPLSALDYKLRK---ELQQELRniQKRLGITFVFVTHDQEEAlAMSDWIFVMHDGLIQQNGTPEDI 225
Cdd:NF033858  150 ALIHDPDLLILDEPTTGVDPLSRRqfwELIDRIR--AERPGMSVLVATAYMEEA-ERFDWLVAMDAGRVLATGTPAEL 224
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
 29-243 1.39e-17

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: 81.64  E-value: 1.39e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  29 VLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKI-----------FFEGQVIND----VPAEKRRVNTVFQNYSLFPN 93
Cdd:cd03236    22 VPREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppdwdeildEFRGSELQNyftkLLEGDVKVIVKPQYVDLIPK 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  94 mnVFDNVAfGPRLKKMSEKDIQDKVKEMLGLVKLSgfeRREISELSGGQQQRVAIARALANDPEVLLLDEPLSALDYKLR 173
Cdd:cd03236   102 --AVKGKV-GELLKKKDERGKLDELVDQLELRHVL---DRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQR 175

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2753759418 174 KELQQELRNIQKRlGITFVFVTHDQEEALAMSDWIFVMHD-----GLIqqngTPEDIYDEPINHFVADFIGETNI 243
Cdd:cd03236   176 LNAARLIRELAED-DNYVLVVEHDLAVLDYLSDYIHCLYGepgayGVV----TLPKSVREGINEFLDGYLPTENM 245
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
 38-229 2.10e-17

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 80.75  E-value: 2.10e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  38 LLGPSGSGKSTILKLISGQLQAdAGKIFFEGQVINDVPAEK---RRVNTVFQNYSLFpNMNVFDNVA-FGPrlKKMSEKD 113
Cdd:PRK03695   27 LVGPNGAGKSTLLARMAGLLPG-SGSIQFAGQPLEAWSAAElarHRAYLSQQQTPPF-AMPVFQYLTlHQP--DKTRTEA 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 114 IQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARAL-----ANDPE--VLLLDEPLSALD-------YKLRKELQQe 179
Cdd:PRK03695  103 VASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqvwpDINPAgqLLLLDEPMNSLDvaqqaalDRLLSELCQ- 181

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2753759418 180 lrniqkrLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDEP 229
Cdd:PRK03695  182 -------QGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPE 224
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
15-221 2.13e-17

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


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 83.61  E-value: 2.13e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  15 LSF---GDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVP--AEKRRVNTVFQNYS 89
Cdd:PRK10790  346 VSFayrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLShsVLRQGVAMVQQDPV 425

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  90 LFPNmNVFDNVAFGprlkkmseKDI-QDKVKEMLGLVKLSGFERR-------EISE----LSGGQQQRVAIARALANDPE 157
Cdd:PRK10790  426 VLAD-TFLANVTLG--------RDIsEEQVWQALETVQLAELARSlpdglytPLGEqgnnLSVGQKQLLALARVLVQTPQ 496

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2753759418 158 VLLLDEPLSALDYKLRKELQQELRNIQKRlgITFVFVTHdQEEALAMSDWIFVMHDGLIQQNGT 221
Cdd:PRK10790  497 ILILDEATANIDSGTEQAIQQALAAVREH--TTLVVIAH-RLSTIVEADTILVLHRGQAVEQGT 557
PRK10522 PRK10522
multidrug transporter membrane component/ATP-binding component; Provisional
 8-218 2.90e-17

multidrug transporter membrane component/ATP-binding component; Provisional


Pssm-ID: 236707 [Multi-domain]  Cd Length: 547  Bit Score: 83.10  E-value: 2.90e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   8 LEFSKVALSFGDTEV-LKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVI--NDVPAEKRRVNTV 84
Cdd:PRK10522  323 LELRNVTFAYQDNGFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVtaEQPEDYRKLFSAV 402

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  85 FQNYSLFPNMnvfdnvaFGPRlKKMSEKDIQDKVKEMLGL---VKLSGFERREISeLSGGQQQRVAIARALANDPEVLLL 161
Cdd:PRK10522  403 FTDFHLFDQL-------LGPE-GKPANPALVEKWLERLKMahkLELEDGRISNLK-LSKGQKKRLALLLALAEERDILLL 473

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2753759418 162 DEPLSALDYKLRKELQQELRNIQKRLGITFVFVTHDqEEALAMSDWIFVMHDGLIQQ 218
Cdd:PRK10522  474 DEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQLSE 529
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
 7-207 5.73e-17

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127 [Multi-domain]  Cd Length: 200  Bit Score: 78.45  E-value: 5.73e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   7 ILEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVIN-DVPAEKRRVNTVF 85
Cdd:PRK13540    1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKkDLCTYQKQLCFVG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  86 QNYSLFPNMNVFDNVAFgprlkKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDEPL 165
Cdd:PRK13540   81 HRSGINPYLTLRENCLY-----DIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPL 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2753759418 166 SALDYKLRKELQQELRNIQKRLGItfVFVTHDQEEALAMSDW 207
Cdd:PRK13540  156 VALDELSLLTIITKIQEHRAKGGA--VLLTSHQDLPLNKADY 195
PLN03211 PLN03211
ABC transporter G-25; Provisional
 11-214 8.97e-17

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 81.85  E-value: 8.97e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  11 SKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAgkifFEGQV-INDVPAEK---RRVNTVFQ 86
Cdd:PLN03211   72 SDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNN----FTGTIlANNRKPTKqilKRTGFVTQ 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  87 NYSLFPNMNVFDNVAFGP--RLKKMSEKDIQDKVKEM----LGLVKLSG--FERREISELSGGQQQRVAIARALANDPEV 158
Cdd:PLN03211  148 DDILYPHLTVRETLVFCSllRLPKSLTKQEKILVAESviseLGLTKCENtiIGNSFIRGISGGERKRVSIAHEMLINPSL 227

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2753759418 159 LLLDEPLSALDYKLRKELQQELRNIQKRlGITFVFVTHD-QEEALAMSDWIFVMHDG 214
Cdd:PLN03211  228 LILDEPTSGLDATAAYRLVLTLGSLAQK-GKTIVTSMHQpSSRVYQMFDSVLVLSEG 283
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
 8-224 2.05e-16

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 80.71  E-value: 2.05e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   8 LEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFegqvindvpAEKRRVNTVFQ- 86
Cdd:PRK15064  320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKW---------SENANIGYYAQd 390

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  87 NYSLFPN-MNVFDNVAfgprlKKMSEKDIQDKVKEMLGLVKLSGFE-RREISELSGGQQQRVAIARALANDPEVLLLDEP 164
Cdd:PRK15064  391 HAYDFENdLTLFDWMS-----QWRQEGDDEQAVRGTLGRLLFSQDDiKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEP 465

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2753759418 165 LSALDYKLRKELQQELRNIQKrlgiTFVFVTHDQE--EALAmSDWIFVMHDGLIQQNGTPED 224
Cdd:PRK15064  466 TNHMDMESIESLNMALEKYEG----TLIFVSHDREfvSSLA-TRIIEITPDGVVDFSGTYEE 522
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
 21-222 2.40e-16

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: 77.07  E-value: 2.40e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  21 EVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEK--RRVNTVFQNYSLFP-----N 93
Cdd:cd03369    22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDlrSSLTIIPQDPTLFSgtirsN 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  94 MNVFDnvafgprlkKMSEKDIQDKVKemlglVKLSGferreiSELSGGQQQRVAIARALANDPEVLLLDEPLSALDYKLR 173
Cdd:cd03369   102 LDPFD---------EYSDEEIYGALR-----VSEGG------LNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATD 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2753759418 174 KELQQELRNIQKrlGITFVFVTHdQEEALAMSDWIFVMHDGLIQQNGTP 222
Cdd:cd03369   162 ALIQKTIREEFT--NSTILTIAH-RLRTIIDYDKILVMDAGEVKEYDHP 207
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
 5-221 3.59e-16

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 79.75  E-value: 3.59e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   5 MPILEFSKVALSF--GDTE--VLKEIDLVLESGKFYTLLGPSGSGKS----TILKLI-SGQLQADAGKIFFEGQVINDVP 75
Cdd:PRK15134    3 QPLLAIENLSVAFrqQQTVrtVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLpSPPVVYPSGDIRFHGESLLHAS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  76 AEKRR------VNTVFQN--YSLFPNMNVfdnvafgprlkkmsEKdiqdKVKEMLGLVK-----------LSGFERREIS 136
Cdd:PRK15134   83 EQTLRgvrgnkIAMIFQEpmVSLNPLHTL--------------EK----QLYEVLSLHRgmrreaargeiLNCLDRVGIR 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 137 -----------ELSGGQQQRVAIARALANDPEVLLLDEPLSALDYKLRKELQQELRNIQKRLGITFVFVTHDQEEALAMS 205
Cdd:PRK15134  145 qaakrltdyphQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLA 224

                         250
                  ....*....|....*..
gi 2753759418 206 DWIFVMHDG-LIQQNGT 221
Cdd:PRK15134  225 DRVAVMQNGrCVEQNRA 241
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
 43-225 9.08e-16

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 78.43  E-value: 9.08e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  43 GSGKSTILKLISGQLQ-ADAGKIFFEGQVIND-------------VPAEKRRvntvfqnYSLFPNMNVFDNV-------- 100
Cdd:PRK13549  298 GAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIrnpqqaiaqgiamVPEDRKR-------DGIVPVMGVGKNItlaaldrf 370

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 101 AFGPRLKKMSE-KDIQDKVKEMLglVKLSGFERReISELSGGQQQRVAIARALANDPEVLLLDEPLSALD-------YKL 172
Cdd:PRK13549  371 TGGSRIDDAAElKTILESIQRLK--VKTASPELA-IARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDvgakyeiYKL 447

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2753759418 173 RKELQQElrniqkrlGITFVFVTHDQEEALAMSDWIFVMHDG-----LIQQNGTPEDI 225
Cdd:PRK13549  448 INQLVQQ--------GVAIIVISSELPEVLGLSDRVLVMHEGklkgdLINHNLTQEQV 497
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
 6-224 1.35e-15

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 78.29  E-value: 1.35e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   6 PILEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKI---------FFEGQVINDVPA 76
Cdd:PRK10636  311 PLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIglakgiklgYFAQHQLEFLRA 390

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  77 EKRRVNtvfqnyslfpnmnvfdnvafgpRLKKMSEKDIQDKVKEMLGLVKLSGFERREISE-LSGGQQQRVAIARALAND 155
Cdd:PRK10636  391 DESPLQ----------------------HLARLAPQELEQKLRDYLGGFGFQGDKVTEETRrFSGGEKARLVLALIVWQR 448

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 156 PEVLLLDEPLSALDYKLRKELQQELRNIQKRLgitfVFVTHDQEEALAMSDWIFVMHDGLIQQ-NGTPED 224
Cdd:PRK10636  449 PNLLLLDEPTNHLDLDMRQALTEALIDFEGAL----VVVSHDRHLLRSTTDDLYLVHDGKVEPfDGDLED 514
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
 8-196 1.71e-15

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: 73.34  E-value: 1.71e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   8 LEFSKVALS--FGDTeVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIffegqvinDVPAEkrrvntvf 85
Cdd:cd03223     1 IELENLSLAtpDGRV-LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI--------GMPEG-------- 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  86 qnyslfpnmnvfDNVAFGPRlkkmsekdiqdkvKEMLGLVKLsgferREI------SELSGGQQQRVAIARALANDPEVL 159
Cdd:cd03223    64 ------------EDLLFLPQ-------------RPYLPLGTL-----REQliypwdDVLSGGEQQRLAFARLLLHKPKFV 113

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2753759418 160 LLDEPLSALDyklrKELQQELRNIQKRLGITFVFVTH 196
Cdd:cd03223   114 FLDEATSALD----EESEDRLYQLLKELGITVISVGH 146
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
19-218 2.84e-15

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 77.13  E-value: 2.84e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  19 DTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVI---NDVPAEKRRVNTVFQNY---SLFP 92
Cdd:PRK09700  275 DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIsprSPLDAVKKGMAYITESRrdnGFFP 354

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  93 NMNVFDNVAFGPRLKK------------MSEKDIQDKVKEMLGLvKLSGFERrEISELSGGQQQRVAIARALANDPEVLL 160
Cdd:PRK09700  355 NFSIAQNMAISRSLKDggykgamglfheVDEQRTAENQRELLAL-KCHSVNQ-NITELSGGNQQKVLISKWLCCCPEVII 432

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2753759418 161 LDEPLSALDYKLRKELQQELRNIQKRlGITFVFVTHDQEEALAMSDWIFVMHDGLIQQ 218
Cdd:PRK09700  433 FDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
PLN03232 PLN03232
ABC transporter C family member; Provisional
 23-226 5.26e-15

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 76.94  E-value: 5.26e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   23 LKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQL-QADAGKIFFEGQVindvpAEKRRVNTVFqnyslfpNMNVFDNVA 101
Cdd:PLN03232   633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELsHAETSSVVIRGSV-----AYVPQVSWIF-------NATVRENIL 700

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  102 FGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISE----LSGGQQQRVAIARALANDPEVLLLDEPLSALDYKLRKE-- 175
Cdd:PLN03232   701 FGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGErgvnISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQvf 780

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2753759418  176 ---LQQELRniqkrlGITFVFVThDQEEALAMSDWIFVMHDGLIQQNGTPEDIY 226
Cdd:PLN03232   781 dscMKDELK------GKTRVLVT-NQLHFLPLMDRIILVSEGMIKEEGTFAELS 827
SapD COG4170
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
5-229 5.27e-15

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


Pssm-ID: 443330 [Multi-domain]  Cd Length: 331  Bit Score: 75.33  E-value: 5.27e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   5 MPILEFSKVALSF----GDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISG------QLQADagKIFFEGQVINDV 74
Cdd:COG4170     1 MPLLDIRNLTIEIdtpqGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGitkdnwHVTAD--RFRWNGIDLLKL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  75 PAEKRR------VNTVFQN--YSLFPNMNVFDN---VAFGPRLKKMSEKDIQDKVKEMLGLVKLSGF-ERREI-----SE 137
Cdd:COG4170    79 SPRERRkiigreIAMIFQEpsSCLDPSAKIGDQlieAIPSWTFKGKWWQRFKWRKKRAIELLHRVGIkDHKDImnsypHE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 138 LSGGQQQRVAIARALANDPEVLLLDEPLSALDYKLRKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQ 217
Cdd:COG4170   159 LTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTV 238

                         250
                  ....*....|..
gi 2753759418 218 QNGTPEDIYDEP 229
Cdd:COG4170   239 ESGPTEQILKSP 250
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
 15-214 5.60e-15

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: 76.87  E-value: 5.60e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   15 LSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEG------QVINDVPAEKRRvNTVFQ-N 87
Cdd:TIGR01271  434 FSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGrisfspQTSWIMPGTIKD-NIIFGlS 512

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   88 YSLFPNMNVFDNVAFGPRLKKMSEKdiqDKVKEMLGLVKlsgferreiseLSGGQQQRVAIARALANDPEVLLLDEPLSA 167
Cdd:TIGR01271  513 YDEYRYTSVIKACQLEEDIALFPEK---DKTVLGEGGIT-----------LSGGQRARISLARAVYKDADLYLLDSPFTH 578

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 2753759418  168 LDYKLRKELQQelRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDG 214
Cdd:TIGR01271  579 LDVVTEKEIFE--SCLCKLMSNKTRILVTSKLEHLKKADKILLLHEG 623
PRK13543 PRK13543
heme ABC exporter ATP-binding protein CcmA;
6-169 1.38e-14

heme ABC exporter ATP-binding protein CcmA;


Pssm-ID: 184129 [Multi-domain]  Cd Length: 214  Bit Score: 72.19  E-value: 1.38e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   6 PILEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQviNDVPAEKRRvntvF 85
Cdd:PRK13543   10 PLLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGK--TATRGDRSR----F 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  86 QNY-----SLFPNMNVFDNVAF-----GPRLKKMSekdiqdkvKEMLGLVKLSGFERREISELSGGQQQRVAIARALAND 155
Cdd:PRK13543   84 MAYlghlpGLKADLSTLENLHFlcglhGRRAKQMP--------GSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSP 155

                         170
                  ....*....|....
gi 2753759418 156 PEVLLLDEPLSALD 169
Cdd:PRK13543  156 APLWLLDEPYANLD 169
GguA NF040905
sugar ABC transporter ATP-binding protein;
7-214 2.42e-14

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 74.06  E-value: 2.42e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   7 ILEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQAD--AGKIFFEGQV-----INDvpAEKR 79
Cdd:NF040905    1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGsyEGEILFDGEVcrfkdIRD--SEAL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  80 RVNTVFQNYSLFPNMNVFDNVAFG-PRLKK--MSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDP 156
Cdd:NF040905   79 GIVIIHQELALIPYLSIAENIFLGnERAKRgvIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDV 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2753759418 157 EVLLLDEPLSALD-------YKLRKELQQElrniqkrlGITFVFVTHDQEEALAMSDWIFVMHDG 214
Cdd:NF040905  159 KLLILDEPTAALNeedsaalLDLLLELKAQ--------GITSIIISHKLNEIRRVADSITVLRDG 215
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
 20-214 2.50e-14

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


Pssm-ID: 213258 [Multi-domain]  Cd Length: 282  Bit Score: 72.58  E-value: 2.50e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  20 TEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGqvindvpaekrRVNTVFQNYSLFPNmNVFDN 99
Cdd:cd03291    50 APVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-----------RISFSSQFSWIMPG-TIKEN 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 100 VAFGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISE----LSGGQQQRVAIARALANDPEVLLLDEPLSALDYKLRKE 175
Cdd:cd03291   118 IIFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKE 197

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2753759418 176 LQQ----ELRNIQKRLGITfvfvthDQEEALAMSDWIFVMHDG 214
Cdd:cd03291   198 IFEscvcKLMANKTRILVT------SKMEHLKKADKILILHEG 234
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
 18-197 3.79e-14

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


Pssm-ID: 274744 [Multi-domain]  Cd Length: 552  Bit Score: 73.82  E-value: 3.79e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  18 GDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGqLQADagkifFEGQVindVPAEKRRVNTVFQNYSLFPNMNVF 97
Cdd:TIGR03719  16 PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG-VDKD-----FNGEA---RPQPGIKVGYLPQEPQLDPTKTVR 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  98 DNVAFGPRLKK------------MSEKDI--------QDKVKEMLGLVKLSGFERR---------------EISELSGGQ 142
Cdd:TIGR03719  87 ENVEEGVAEIKdaldrfneisakYAEPDAdfdklaaeQAELQEIIDAADAWDLDSQleiamdalrcppwdaDVTKLSGGE 166

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2753759418 143 QQRVAIARALANDPEVLLLDEPLSALDYKLRKELQQELRNIQKrlgiTFVFVTHD 197
Cdd:TIGR03719 167 RRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPG----TVVAVTHD 217
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
 4-225 3.90e-14

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 74.30  E-value: 3.90e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418    4 KMPILEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISG--QLQADAgKIFFEGQVINDVPAEK--- 78
Cdd:PTZ00265  1165 KIEIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRfyDLKNDH-HIVFKNEHTNDMTNEQdyq 1243

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   79 ---------RRVN--------------TVFQN-------------YSLFPNMNVFDNVAFGPRLKKMS---------EKD 113
Cdd:PTZ00265  1244 gdeeqnvgmKNVNefsltkeggsgedsTVFKNsgkilldgvdicdYNLKDLRNLFSIVSQEPMLFNMSiyenikfgkEDA 1323

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  114 IQDKVKEMLGLVKLSGFERREISE-----------LSGGQQQRVAIARALANDPEVLLLDEPLSALDYKLRKELQQELRN 182
Cdd:PTZ00265  1324 TREDVKRACKFAAIDEFIESLPNKydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVD 1403

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 2753759418  183 IQKRLGITFVFVTHdQEEALAMSDWIFVMHD-----GLIQQNGTPEDI 225
Cdd:PTZ00265  1404 IKDKADKTIITIAH-RIASIKRSDKIVVFNNpdrtgSFVQAHGTHEEL 1450
PLN03073 PLN03073
ABC transporter F family; Provisional
 6-214 5.84e-14

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 73.36  E-value: 5.84e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   6 PILEFSKVALSF-GDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEKRRVNTV 84
Cdd:PLN03073  507 PIISFSDASFGYpGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAVFSQHHVDGLD 586

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  85 FQNYSLFPNMNVFDNVAfgprlkkmsekdiQDKVKEMLGLVKLSG-FERREISELSGGQQQRVAIARALANDPEVLLLDE 163
Cdd:PLN03073  587 LSSNPLLYMMRCFPGVP-------------EQKLRAHLGSFGVTGnLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDE 653

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2753759418 164 PLSALDYKLRKELQQELRNIQKrlGItfVFVTHDQEEALAMSDWIFVMHDG 214
Cdd:PLN03073  654 PSNHLDLDAVEALIQGLVLFQG--GV--LMVSHDEHLISGSVDELWVVSEG 700
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
23-216 7.34e-14

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 72.64  E-value: 7.34e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  23 LKE-IDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVIN-DVPA-----------EKRRVNTVFQNYS 89
Cdd:PRK11288  268 LREpISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDiRSPRdairagimlcpEDRKAEGIIPVHS 347

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  90 LFPNMNVF---DNVAFGPRLKKMSEKDIQDKVKEMLGLVKLSGfeRREISELSGGQQQRVAIARALANDPEVLLLDEPLS 166
Cdd:PRK11288  348 VADNINISarrHHLRAGCLINNRWEAENADRFIRSLNIKTPSR--EQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTR 425

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2753759418 167 ALDYKLRKELQQELRNIQKRlGITFVFVTHDQEEALAMSDWIFVMHDGLI 216
Cdd:PRK11288  426 GIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRI 474
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
 7-197 7.65e-14

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


Pssm-ID: 274744 [Multi-domain]  Cd Length: 552  Bit Score: 72.66  E-value: 7.65e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   7 ILEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFegqvindvpAEKRRVNTVFQ 86
Cdd:TIGR03719 322 VIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI---------GETVKLAYVDQ 392

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  87 NY-SLFPNMNVFDNVAFGPRLKKMSEKDIQDKVkeMLGLVKLSGFER-REISELSGGQQQRVAIARALANDPEVLLLDEP 164
Cdd:TIGR03719 393 SRdALDPNKTVWEEISGGLDIIKLGKREIPSRA--YVGRFNFKGSDQqKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEP 470

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2753759418 165 LSALDYKLRKELQQELRNIQkrlGITFVfVTHD 197
Cdd:TIGR03719 471 TNDLDVETLRALEEALLNFA---GCAVV-ISHD 499
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
 8-222 8.24e-14

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: 69.83  E-value: 8.24e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   8 LEFSKVALSFGDTE--VLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEK--RRVNT 83
Cdd:cd03244     3 IEFKNVSLRYRPNLppVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDlrSRISI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  84 VFQNYSLFP-----NMNVFD--------NVafgprLKKMSEKDIQDKVKEMLGL-VKLSGferreiSELSGGQQQRVAIA 149
Cdd:cd03244    83 IPQDPVLFSgtirsNLDPFGeysdeelwQA-----LERVGLKEFVESLPGGLDTvVEEGG------ENLSVGQRQLLCLA 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2753759418 150 RALANDPEVLLLDEPLSALDYKLRKELQQELRNiqKRLGITFVFVTHdQEEALAMSDWIFVMHDGLIQQNGTP 222
Cdd:cd03244   152 RALLRKSKILVLDEATASVDPETDALIQKTIRE--AFKDCTVLTIAH-RLDTIIDSDRILVLDKGRVVEFDSP 221
PvdE COG4615
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...
 26-197 1.08e-13

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: 72.14  E-value: 1.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  26 IDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEKRRVN--TVFQNYSLFPNM----NVFDN 99
Cdd:COG4615   351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLfsAVFSDFHLFDRLlgldGEADP 430

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 100 VAFGPRLKKMsekDIQDKVKemlglvklsgFERREIS--ELSGGQQQRVAIARALANDPEVLLLDEplSALD-------- 169
Cdd:COG4615   431 ARARELLERL---ELDHKVS----------VEDGRFSttDLSQGQRKRLALLVALLEDRPILVFDE--WAADqdpefrrv 495

                         170       180
                  ....*....|....*....|....*....
gi 2753759418 170 -YklrKELQQELrniqKRLGITFVFVTHD 197
Cdd:COG4615   496 fY---TELLPEL----KARGKTVIAISHD 517
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
39-225 1.42e-13

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 72.46  E-value: 1.42e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  39 LGPSGSGKSTILKLISGQLQADAGKIFFEGQVI--NDVpAEKRRVNTVFQNYSLFPNMNVFDNVAFGPRLKKMSEKDIQD 116
Cdd:NF033858  298 LGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVdaGDI-ATRRRVGYMSQAFSLYGELTVRQNLELHARLFHLPAAEIAA 376

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 117 KVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDEPLSALDYKLRKELQQELRNIQKRLGITfVFV-T 195
Cdd:NF033858  377 RVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELSREDGVT-IFIsT 455

                         170       180       190
                  ....*....|....*....|....*....|
gi 2753759418 196 HDQEEAlAMSDWIFVMHDGLIQQNGTPEDI 225
Cdd:NF033858  456 HFMNEA-ERCDRISLMHAGRVLASDTPAAL 484
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
 33-221 1.63e-13

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


Pssm-ID: 130324 [Multi-domain]  Cd Length: 2272  Bit Score: 72.35  E-value: 1.63e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   33 GKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVIndvpaeKRRVNTVFQNYSLFPNMNVFDNVAFG-------PR 105
Cdd:TIGR01257 1965 GECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI------LTNISDVHQNMGYCPQFDAIDDLLTGrehlylyAR 2038

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  106 LKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDEPLSALDYKLRKELQQELRNIqK 185
Cdd:TIGR01257 2039 LRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSI-I 2117

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 2753759418  186 RLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGT 221
Cdd:TIGR01257 2118 REGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGT 2153
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
 8-225 2.19e-13

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 71.98  E-value: 2.19e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418    8 LEFSKVALSFG---DTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFF-EGQVINDVPAE--KRRV 81
Cdd:PTZ00265   383 IQFKNVRFHYDtrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKwwRSKI 462

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   82 NTVFQNYSLFPNmNVFDNVAFG----PRLKKMSEK------------------------DIQDKVKEML--GLVKL---- 127
Cdd:PTZ00265   463 GVVSQDPLLFSN-SIKNNIKYSlyslKDLEALSNYynedgndsqenknkrnscrakcagDLNDMSNTTDsnELIEMrkny 541

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  128 SGFERREI----------------------------SELSGGQQQRVAIARALANDPEVLLLDEPLSALDYKLRKELQQE 179
Cdd:PTZ00265   542 QTIKDSEVvdvskkvlihdfvsalpdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKT 621

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 2753759418  180 LRNIQKRLGITFVFVTHdQEEALAMSDWIFVMHDgliQQNGTPEDI 225
Cdd:PTZ00265   622 INNLKGNENRITIIIAH-RLSTIRYANTIFVLSN---RERGSTVDV 663
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
 24-219 4.09e-13

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: 70.62  E-value: 4.09e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  24 KEIDLV---LESGKFYTLLGPSGSGKSTILKLISGQLQ-ADAGKIFFEGQVIND-------------VPAEKRR-----V 81
Cdd:TIGR02633 274 KRVDDVsfsLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGKPVDIrnpaqairagiamVPEDRKRhgivpI 353

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  82 NTVFQNYSLfpnmNVFDNVAFGPRLKKMSEKDIQDKVKEMLGLVKLSGFerREISELSGGQQQRVAIARALANDPEVLLL 161
Cdd:TIGR02633 354 LGVGKNITL----SVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPF--LPIGRLSGGNQQKAVLAKMLLTNPRVLIL 427

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2753759418 162 DEPLSALD-------YKLRKELQQElrniqkrlGITFVFVTHDQEEALAMSDWIFVMHDGLIQQN 219
Cdd:TIGR02633 428 DEPTRGVDvgakyeiYKLINQLAQE--------GVAIIVVSSELAEVLGLSDRVLVIGEGKLKGD 484
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
 19-229 4.16e-13

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 68.57  E-value: 4.16e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  19 DTEVLKEIDLVLESGKFYTLLGPSGSGKS----TILKLISGQLQADAGKIFFEGQVINDVPAEKRRVNTVFQN-YSLFpn 93
Cdd:PRK10418   15 AQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVAPCALRGRKIATIMQNpRSAF-- 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  94 mNVFDNVAFGPR--LKKMSEKDIQDKVKEMLGLVKLSGFER---REISELSGGQQQRVAIARALANDPEVLLLDEPLSAL 168
Cdd:PRK10418   93 -NPLHTMHTHARetCLALGKPADDATLTAALEAVGLENAARvlkLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDL 171

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2753759418 169 DYKLRKELQQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDIYDEP 229
Cdd:PRK10418  172 DVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAP 232
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 32-204 5.09e-13

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: 66.24  E-value: 5.09e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   32 SGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFegqvindvpaekrrVNTvfqnyslfpnmnvfdnvafgprlkkmse 111
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY--------------IDG---------------------------- 38

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  112 kdiqDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDEPLSALDYKLRKELQQELR-----NIQKR 186
Cdd:smart00382  39 ----EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrlllLLKSE 114

                          170
                   ....*....|....*...
gi 2753759418  187 LGITFVFVTHDQEEALAM 204
Cdd:smart00382 115 KNLTVILTTNDEKDLGPA 132
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 6-208 1.19e-12

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: 69.04  E-value: 1.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   6 PILEFSKVALSFGDTEvlkeidLVLESGKFY-----TLLGPSGSGKSTILKLISGQLQADAGKIFFE------GQVIN-D 73
Cdd:COG1245   340 TLVEYPDLTKSYGGFS------LEVEGGEIRegevlGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDlkisykPQYISpD 413

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  74 VPAekrrvnTVFQNyslfpnmnvfdnvafgprLKKMSEKDIQDK-----VKEMLGLVKLsgFERrEISELSGGQQQRVAI 148
Cdd:COG1245   414 YDG------TVEEF------------------LRSANTDDFGSSyykteIIKPLGLEKL--LDK-NVKDLSGGELQRVAI 466

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 149 ARALANDPEVLLLDEPLSALDYKLRKELQQELRNIQKRLGITFVFVTHDqeeaLAMSDWI 208
Cdd:COG1245   467 AACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHD----IYLIDYI 522
3a01203 TIGR00954
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...
 22-196 1.27e-12

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: 69.01  E-value: 1.27e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  22 VLKEIDLVLESGKFYTLLGPSGSGKSTILKLI-------SGQLQADA-GKIFFegqvindVPAEKRRVNTVFQNYSLFPn 93
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILgelwpvyGGRLTKPAkGKLFY-------VPQRPYMTLGTLRDQIIYP- 538

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  94 MNVFDnvafgprlkkMSEKDIQDKV-KEMLGLVKLSGFERREIS---------ELSGGQQQRVAIARALANDPEVLLLDE 163
Cdd:TIGR00954 539 DSSED----------MKRRGLSDKDlEQILDNVQLTHILEREGGwsavqdwmdVLSGGEKQRIAMARLFYHKPQFAILDE 608

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2753759418 164 PLSALDYklrkELQQELRNIQKRLGITFVFVTH 196
Cdd:TIGR00954 609 CTSAVSV----DVEGYMYRLCREFGITLFSVSH 637
PRK15093 PRK15093
peptide ABC transporter ATP-binding protein SapD;
5-229 1.90e-12

peptide ABC transporter ATP-binding protein SapD;


Pssm-ID: 185049 [Multi-domain]  Cd Length: 330  Bit Score: 67.52  E-value: 1.90e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   5 MPILEFSKVALSF----GDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGqLQADAGKIFFEGQVINDV------ 74
Cdd:PRK15093    1 MPLLDIRNLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICG-VTKDNWRVTADRMRFDDIdllrls 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  75 PAEKRR-----VNTVFQ--NYSLFPNMNVFDNVA---------------FGPRLKKMSE----KDIQDKVKEMlglvkls 128
Cdd:PRK15093   80 PRERRKlvghnVSMIFQepQSCLDPSERVGRQLMqnipgwtykgrwwqrFGWRKRRAIEllhrVGIKDHKDAM------- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 129 gfeRREISELSGGQQQRVAIARALANDPEVLLLDEPLSALDYKLRKELQQELRNIQKRLGITFVFVTHDQEealAMSDW- 207
Cdd:PRK15093  153 ---RSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQ---MLSQWa 226

                         250       260
                  ....*....|....*....|....
gi 2753759418 208 --IFVMHDGLIQQNGTPEDIYDEP 229
Cdd:PRK15093  227 dkINVLYCGQTVETAPSKELVTTP 250
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
 23-216 3.58e-12

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 67.45  E-value: 3.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  23 LKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPA------------EKRRVNTVFQNY-- 88
Cdd:PRK10982  264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNAneainhgfalvtEERRSTGIYAYLdi 343

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  89 ---SLFPNMNVFDNvAFGPRLKKMSEKDIQDKVKEMLglVKLSGfERREISELSGGQQQRVAIARALANDPEVLLLDEPL 165
Cdd:PRK10982  344 gfnSLISNIRNYKN-KVGLLDNSRMKSDTQWVIDSMR--VKTPG-HRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPT 419

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2753759418 166 SALDYKLRKELQQELRNI-QKRLGItfVFVTHDQEEALAMSDWIFVMHDGLI 216
Cdd:PRK10982  420 RGIDVGAKFEIYQLIAELaKKDKGI--IIISSEMPELLGITDRILVMSNGLV 469
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
6-208 6.60e-12

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 66.76  E-value: 6.60e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   6 PILEFSKVALSFGDtevlkeIDLVLESGKFY-----TLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVindvpAEKRr 80
Cdd:PRK13409  339 TLVEYPDLTKKLGD------FSLEVEGGEIYegeviGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKI-----SYKP- 406

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  81 vntvfQNYSLFPNMNVFDNVAFGPrlKKMSEKDIQDKVKEMLGLVKLsgFERrEISELSGGQQQRVAIARALANDPEVLL 160
Cdd:PRK13409  407 -----QYIKPDYDGTVEDLLRSIT--DDLGSSYYKSEIIKPLQLERL--LDK-NVKDLSGGELQRVAIAACLSRDADLYL 476

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2753759418 161 LDEPLSALDYKLRKELQQELRNIQKRLGITFVFVTHDqeeaLAMSDWI 208
Cdd:PRK13409  477 LDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHD----IYMIDYI 520
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
 23-173 7.91e-12

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


Pssm-ID: 213204 [Multi-domain]  Cd Length: 246  Bit Score: 64.74  E-value: 7.91e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  23 LKEIDLVLESGKFY-----TLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEKRRVNTVFQNYSLfpnMNVF 97
Cdd:cd03237    10 LGEFTLEVEGGSISeseviGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIKADYEGTVRDLL---SSIT 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2753759418  98 DNVAFGPRLKKmsekdiqdkvkEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDEPLSALDYKLR 173
Cdd:cd03237    87 KDFYTHPYFKT-----------EIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQR 151
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
 5-225 9.72e-12

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 66.19  E-value: 9.72e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   5 MPILEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTI-------LKLISGQLQADAGKIF---FEgQVINDV 74
Cdd:PRK10938    1 MSSLQISQGTFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALaralageLPLLSGERQSQFSHITrlsFE-QLQKLV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  75 PAEKRRVNTvfqnyslfpNMNVFDNVAFGprlkKMSEKDIQDKVK---------EMLGLVKLsgFERReISELSGGQQQR 145
Cdd:PRK10938   80 SDEWQRNNT---------DMLSPGEDDTG----RTTAEIIQDEVKdparceqlaQQFGITAL--LDRR-FKYLSTGETRK 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 146 VAIARALANDPEVLLLDEPLSALDYKLRKELQQELRNIQKRlGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDI 225
Cdd:PRK10938  144 TLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEI 222
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
 6-201 1.26e-11

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 65.81  E-value: 1.26e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   6 PILEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISG-QLQADAGK-IFF-----EGQVINDVpaeK 78
Cdd:PRK10938  259 PRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdHPQGYSNDlTLFgrrrgSGETIWDI---K 335

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  79 R-------------RVNTVFQNYSL---FPNMNVFDNVAFGPRLKKMSEKDIqdkvkemLGLVKL---SGFERreiseLS 139
Cdd:PRK10938  336 KhigyvssslhldyRVSTSVRNVILsgfFDSIGIYQAVSDRQQKLAQQWLDI-------LGIDKRtadAPFHS-----LS 403

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2753759418 140 GGQQQRVAIARALANDPEVLLLDEPLSALD---YKL-RKELQQELRNIQKRLgitfVFVTHDQEEA 201
Cdd:PRK10938  404 WGQQRLALIVRALVKHPTLLILDEPLQGLDplnRQLvRRFVDVLISEGETQL----LFVSHHAEDA 465
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
 20-214 1.68e-11

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: 63.05  E-value: 1.68e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  20 TEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADA---GKIFFEGqVINDVPAEKRRVNTVF--QNYSLFPNM 94
Cdd:cd03233    20 IPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNG-IPYKEFAEKYPGEIIYvsEEDVHFPTL 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  95 NVFDNVAFGPRLKkmsekdiqdkvkemlGLVKLSGFerreiselSGGQQQRVAIARALANDPEVLLLDEPLSALDYKLRK 174
Cdd:cd03233    99 TVRETLDFALRCK---------------GNEFVRGI--------SGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTAL 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2753759418 175 ELQQELRNIQKRLGIT-FVFVTHDQEEALAMSDWIFVMHDG 214
Cdd:cd03233   156 EILKCIRTMADVLKTTtFVSLYQASDEIYDLFDKVLVLYEG 196
PRK13541 PRK13541
cytochrome c biogenesis protein CcmA; Provisional
 40-176 3.06e-11

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184128 [Multi-domain]  Cd Length: 195  Bit Score: 62.20  E-value: 3.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  40 GPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPaeKRRVNTVFQNYSLFPNMNVFDNVAFGPRLKKMSEkdiqdKVK 119
Cdd:PRK13541   33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIA--KPYCTYIGHNLGLKLEMTVFENLKFWSEIYNSAE-----TLY 105

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2753759418 120 EMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDEPLSALDYKLRKEL 176
Cdd:PRK13541  106 AAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLL 162
ABCG_PDR_domain2 cd03232
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...
 18-169 4.99e-11

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


Pssm-ID: 213199 [Multi-domain]  Cd Length: 192  Bit Score: 61.49  E-value: 4.99e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  18 GDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGqlQADAGKIffEGQV-INDVPAEK---RRVNTVFQNYSLFPN 93
Cdd:cd03232    18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAG--RKTAGVI--TGEIlINGRPLDKnfqRSTGYVEQQDVHSPN 93

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2753759418  94 MnvfdnvafgprlkkmsekdiqdKVKEMLglvKLSGFERreisELSGGQQQRVAIARALANDPEVLLLDEPLSALD 169
Cdd:cd03232    94 L----------------------TVREAL---RFSALLR----GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLD 140
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
 38-209 5.90e-11

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 63.82  E-value: 5.90e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  38 LLGPSGSGKSTILKLISGQLQADAGKIffegqvindvpaekrRVNT-----VFQNY--SLFPNMNVFDNVAFGprlKKms 110
Cdd:PRK11147  350 LIGPNGCGKTTLLKLMLGQLQADSGRI---------------HCGTklevaYFDQHraELDPEKTVMDNLAEG---KQ-- 409

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 111 EKDIQDKVKEMLGLvkLSGF------ERREISELSGGQQQRVAIARALANDPEVLLLDEPLSALDYKLRKELQQELRNIQ 184
Cdd:PRK11147  410 EVMVNGRPRHVLGY--LQDFlfhpkrAMTPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQ 487

                         170       180
                  ....*....|....*....|....*..
gi 2753759418 185 KrlgiTFVFVTHDQE--EALAMSDWIF 209
Cdd:PRK11147  488 G----TVLLVSHDRQfvDNTVTECWIF 510
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
 18-197 1.73e-10

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 62.44  E-value: 1.73e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  18 GDTEVLKEIDLvlesgKFYT-----LLGPSGSGKSTILKLISGqLQADagkifFEGQVindVPAEKRRVNTVFQNYSLFP 92
Cdd:PRK11819   18 PKKQILKDISL-----SFFPgakigVLGLNGAGKSTLLRIMAG-VDKE-----FEGEA---RPAPGIKVGYLPQEPQLDP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  93 NMNVFDNV--AFGPRLK----------KMSEKDI--------QDKVKEMLGLVKLSGFERR---------------EISE 137
Cdd:PRK11819   84 EKTVRENVeeGVAEVKAaldrfneiyaAYAEPDAdfdalaaeQGELQEIIDAADAWDLDSQleiamdalrcppwdaKVTK 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 138 LSGGQQQRVAIARALANDPEVLLLDEPLSALDYKLRKELQQELRNIQkrlGiTFVFVTHD 197
Cdd:PRK11819  164 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYP---G-TVVAVTHD 219
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
 22-232 2.96e-10

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


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 62.05  E-value: 2.96e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   22 VLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQ----ADAGKIFFEGQVINDVPAEKR-RVNTVFQNYSLFPNMNV 96
Cdd:TIGR00956   76 ILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDgfhiGVEGVITYDGITPEEIKKHYRgDVVYNAETDVHFPHLTV 155

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   97 FDNVAFGPRLKK-------MSEKD----IQDKVKEMLGL--VKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDE 163
Cdd:TIGR00956  156 GETLDFAARCKTpqnrpdgVSREEyakhIADVYMATYGLshTRNTKVGNDFVRGVSGGERKRVSIAEASLGGAKIQCWDN 235

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2753759418  164 PLSALDYKLRKELQQELRNIQKRLGITfVFVTHDQ--EEALAMSDWIFVMHDGliQQngtpedIYDEPINH 232
Cdd:TIGR00956  236 ATRGLDSATALEFIRALKTSANILDTT-PLVAIYQcsQDAYELFDKVIVLYEG--YQ------IYFGPADK 297
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
98-225 3.55e-10

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 60.90  E-value: 3.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  98 DNVAFGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDEPLSALDYKLRKELQ 177
Cdd:NF000106  105 ENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVW 184

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2753759418 178 QELRNIQkRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDI 225
Cdd:NF000106  185 DEVRSMV-RDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
sufC PRK09580
cysteine desulfurase ATPase component; Reviewed
 7-220 4.83e-10

cysteine desulfurase ATPase component; Reviewed


Pssm-ID: 181965 [Multi-domain]  Cd Length: 248  Bit Score: 59.42  E-value: 4.83e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   7 ILEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISG--QLQADAGKIFFEGQVINDVPAEKRRVNTV 84
Cdd:PRK09580    1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGTVEFKGKDLLELSPEDRAGEGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  85 FQNYS-----------LFPNMNVfDNVAFGPRLKKMSEKDIQDKVKEMLGLVKL-SGFERREISE-LSGGQQQRVAIARA 151
Cdd:PRK09580   81 FMAFQypveipgvsnqFFLQTAL-NAVRSYRGQEPLDRFDFQDLMEEKIALLKMpEDLLTRSVNVgFSGGEKKRNDILQM 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2753759418 152 LANDPEVLLLDEPLSALD---YKLRKELQQELRNiQKRlgiTFVFVTHDQE-EALAMSDWIFVMHDGLIQQNG 220
Cdd:PRK09580  160 AVLEPELCILDESDSGLDidaLKIVADGVNSLRD-GKR---SFIIVTHYQRiLDYIKPDYVHVLYQGRIVKSG 228
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
 32-197 7.12e-10

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 60.29  E-value: 7.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  32 SGKF-----YTLLGPSGSGKSTILKLISGQLQADAGKIFFEgqvindvPAEkrRVNTVFQNYSLFPNMNVFDNVAFGPR- 105
Cdd:PRK15064   21 SVKFgggnrYGLIGANGCGKSTFMKILGGDLEPSAGNVSLD-------PNE--RLGKLRQDQFAFEEFTVLDTVIMGHTe 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 106 -------------LKKMSEKD------IQDKVKEM-------------LGLvklsGFERRE----ISELSGGQQQRVAIA 149
Cdd:PRK15064   92 lwevkqerdriyaLPEMSEEDgmkvadLEVKFAEMdgytaearagellLGV----GIPEEQhyglMSEVAPGWKLRVLLA 167

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2753759418 150 RALANDPEVLLLDEPLSALDYKLRKELQQELRNIQKrlgiTFVFVTHD 197
Cdd:PRK15064  168 QALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNS----TMIIISHD 211
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
 85-225 3.39e-09

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: 58.49  E-value: 3.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  85 FQNYSLFPNMNVFDNVAFGPRLKKMSEKDIQDkVKEMLGLVKLSGFE----RREISELSGGQQQRVAIARALAND-PEVL 159
Cdd:TIGR00630 433 VSELSIREAHEFFNQLTLTPEEKKIAEEVLKE-IRERLGFLIDVGLDylslSRAAGTLSGGEAQRIRLATQIGSGlTGVL 511

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2753759418 160 -LLDEPLSALDYKLRKELQQELRNIQKrLGITFVFVTHDqEEALAMSDWIFVM------HDGLIQQNGTPEDI 225
Cdd:TIGR00630 512 yVLDEPSIGLHQRDNRRLINTLKRLRD-LGNTLIVVEHD-EDTIRAADYVIDIgpgageHGGEVVASGTPEEI 582
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
 7-169 1.10e-08

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 56.67  E-value: 1.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   7 ILEFSKVALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIffegqVINDvpaekrrvnTVFQ 86
Cdd:PRK11819  324 VIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTI-----KIGE---------TVKL 389

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  87 NY------SLFPNMNVFDNVAFGprlkkmsekdiQDKVK----EMLGLVKLSGF------ERREISELSGGQQQRVAIAR 150
Cdd:PRK11819  390 AYvdqsrdALDPNKTVWEEISGG-----------LDIIKvgnrEIPSRAYVGRFnfkggdQQKKVGVLSGGERNRLHLAK 458

                         170
                  ....*....|....*....
gi 2753759418 151 ALANDPEVLLLDEPLSALD 169
Cdd:PRK11819  459 TLKQGGNVLLLDEPTNDLD 477
TOBE_2 pfam08402
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the ...
 276-345 2.14e-08

TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the C-terminal strand of each domain is supplied by the partner. Probably involved in the recognition of small ligands such as molybdenum and sulphate. Found in ABC transporters immediately after the ATPase domain. In this family a strong RPE motif is found at the presumed N-terminus of the domain.


Pssm-ID: 462465 [Multi-domain]  Cd Length: 73  Bit Score: 50.70  E-value: 2.14e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2753759418 276 VVLRPEDLDLTDPANGkLVVTIQDQLFRGDYYEITAVDDDMNTWQVQATNPA----TVGARVGLTFDPEDIHIM 345
Cdd:pfam08402   1 LAIRPEKIRLAAAANG-LSGTVTDVEYLGDHTRYHVELAGGEELVVRVPNAHarppAPGDRVGLGWDPEDAHVL 73
PRK13546 PRK13546
teichoic acids export ABC transporter ATP-binding subunit TagH;
23-233 2.43e-08

teichoic acids export ABC transporter ATP-binding subunit TagH;


Pssm-ID: 184131 [Multi-domain]  Cd Length: 264  Bit Score: 54.44  E-value: 2.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  23 LKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQvindvpaekrrVNTVFQNYSLFPNMNVFDNVAF 102
Cdd:PRK13546   40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE-----------VSVIAISAGLSGQLTGIENIEF 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 103 GPRLKKMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDEPLSALDYKLRkelQQELRN 182
Cdd:PRK13546  109 KMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFA---QKCLDK 185

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2753759418 183 IQ--KRLGITFVFVTHDQEEALAMSDWIFVMHDGLIQQNGTPEDI---YDEPINHF 233
Cdd:PRK13546  186 IYefKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVlpkYEAFLNDF 241
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
 40-214 6.17e-08

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: 52.61  E-value: 6.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  40 GPSGSGKSTILKLI----------SGQLQADAGKIFFEGQVINDVPAEKRRVNTVfqNYSLFPNMNVFDNVAFGPrlkkm 109
Cdd:cd03240    29 GQNGAGKTTIIEALkyaltgelppNSKGGAHDPKLIREGEVRAQVKLAFENANGK--KYTITRSLAILENVIFCH----- 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 110 sEKDIQDKVKEMLGLvklsgferreiseLSGGQQQ------RVAIARALANDPEVLLLDEPLSALD-YKLRKELQQELRN 182
Cdd:cd03240   102 -QGESNWPLLDMRGR-------------CSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDeENIEESLAEIIEE 167

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2753759418 183 IQKRLGITFVFVTHDQEEALAMSDWIFVMHDG 214
Cdd:cd03240   168 RKSQKNFQLIVITHDEELVDAADHIYRVEKDG 199
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
 15-208 9.70e-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: 51.55  E-value: 9.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  15 LSFGDTEV--LKEIDLVLESGKFYTLLGPSGSGKSTILKlisgqlqadagKIFFEgqvindvpAEKRRVNTVFQNYSlfp 92
Cdd:cd03238     1 LTVSGANVhnLQNLDVSIPLNVLVVVTGVSGSGKSTLVN-----------EGLYA--------SGKARLISFLPKFS--- 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  93 nmnvFDNVAFGPRLKKMsekdiqdkVKEMLGLVKLSgferREISELSGGQQQRVAIARALANDPE--VLLLDEPLSALDY 170
Cdd:cd03238    59 ----RNKLIFIDQLQFL--------IDVGLGYLTLG----QKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQ 122

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2753759418 171 KLRKELQQELRNIqKRLGITFVFVTHDqEEALAMSDWI 208
Cdd:cd03238   123 QDINQLLEVIKGL-IDLGNTVILIEHN-LDVLSSADWI 158
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
 23-208 1.70e-07

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: 51.49  E-value: 1.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  23 LKEIDLVLESGKFYTLLGPSGSGKSTilklisgqLQADAgkIFFEGQvindvpaekRRVNTVFQNYS--LFPNMNVFD-- 98
Cdd:cd03270    11 LKNVDVDIPRNKLVVITGVSGSGKSS--------LAFDT--IYAEGQ---------RRYVESLSAYArqFLGQMDKPDvd 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  99 --------------NVAFGPRLKKMSEKDIQDK---------VKEMLGLVKLSGFE----RREISELSGGQQQRVAIARA 151
Cdd:cd03270    72 sieglspaiaidqkTTSRNPRSTVGTVTEIYDYlrllfarvgIRERLGFLVDVGLGyltlSRSAPTLSGGEAQRIRLATQ 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2753759418 152 LANDPEVLL--LDEPLSAL----DYKLRKELqQELRNiqkrLGITFVFVTHDqEEALAMSDWI 208
Cdd:cd03270   152 IGSGLTGVLyvLDEPSIGLhprdNDRLIETL-KRLRD----LGNTVLVVEHD-EDTIRAADHV 208
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
 13-169 4.25e-07

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


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 52.03  E-value: 4.25e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   13 VALSFGDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLqaDAGKIFFEGQVINDVPAEK---RRVNTVFQNYS 89
Cdd:TIGR00956  769 VKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERV--TTGVITGGDRLVNGRPLDSsfqRSIGYVQQQDL 846

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   90 LFPNMNVFDNVAFGPRLKK-----MSEK-DIQDKVKEMLG-------LVKLSGferreiSELSGGQQQRVAIARALANDP 156
Cdd:TIGR00956  847 HLPTSTVRESLRFSAYLRQpksvsKSEKmEYVEEVIKLLEmesyadaVVGVPG------EGLNVEQRKRLTIGVELVAKP 920

                          170
                   ....*....|....
gi 2753759418  157 EVLL-LDEPLSALD 169
Cdd:TIGR00956  921 KLLLfLDEPTSGLD 934
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
 38-199 6.11e-07

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 51.32  E-value: 6.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  38 LLGPSGSGKSTILKLISGQLQADAGKIFFEGQV----IN------DVPA---------EKRRVNTVFQNYSLFPNMNVFD 98
Cdd:PRK10636   32 LVGKNGCGKSTLLALLKNEISADGGSYTFPGNWqlawVNqetpalPQPAleyvidgdrEYRQLEAQLHDANERNDGHAIA 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  99 NVAfgPRLKKMSEKDIQDKVKEML-GLvklsGFER----REISELSGGQQQRVAIARALANDPEVLLLDEPLSALDYKLR 173
Cdd:PRK10636  112 TIH--GKLDAIDAWTIRSRAASLLhGL----GFSNeqleRPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAV 185

                         170       180
                  ....*....|....*....|....*.
gi 2753759418 174 KELQQELRNIQKrlgiTFVFVTHDQE 199
Cdd:PRK10636  186 IWLEKWLKSYQG----TLILISHDRD 207
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
 17-212 6.94e-07

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


Pssm-ID: 213189 [Multi-domain]  Cd Length: 177  Bit Score: 49.11  E-value: 6.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  17 FGDTEVLKEIDlVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQvindvpaekrrvntvfqnyslfpnmnv 96
Cdd:cd03222    10 YGVFFLLVELG-VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGI--------------------------- 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  97 fdNVAFGPRlkkmsekdiqdKVKemlglvklsgferreiseLSGGQQQRVAIARALANDPEVLLLDEPLSALDYKLRKEL 176
Cdd:cd03222    62 --TPVYKPQ-----------YID------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNA 110

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2753759418 177 QQELRNIQKRLGITFVFVTHDQEEALAMSDWIFVMH 212
Cdd:cd03222   111 ARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFE 146
PLN03140 PLN03140
ABC transporter G family member; Provisional
 7-182 1.52e-06

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 50.23  E-value: 1.52e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418    7 ILEFSKVALSFGDT--------------------EVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQlqADAGKIff 66
Cdd:PLN03140   860 VLPFTPLAMSFDDVnyfvdmpaemkeqgvtedrlQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGR--KTGGYI-- 935

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   67 EGQV-INDVPAEK----RRVNTVFQNYSLFPNMNVFDNVAFGPRLKKMSEKDIQDK---VKEMLGLVKLSGFERR----- 133
Cdd:PLN03140   936 EGDIrISGFPKKQetfaRISGYCEQNDIHSPQVTVRESLIYSAFLRLPKEVSKEEKmmfVDEVMELVELDNLKDAivglp 1015

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 2753759418  134 EISELSGGQQQRVAIARALANDPEVLLLDEPLSALDYKLRKELQQELRN 182
Cdd:PLN03140  1016 GVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRN 1064
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
 22-225 1.57e-06

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


Pssm-ID: 188098 [Multi-domain]  Cd Length: 1522  Bit Score: 50.33  E-value: 1.57e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   22 VLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEKRR--VNTVFQNYSLFPNMNVFDN 99
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRfkITIIPQDPVLFSGSLRMNL 1380

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  100 VAFGprlkKMSEKDIQdkvkEMLGLVKLSGFER-------REISE----LSGGQQQRVAIARALANDPEVLLLDEPLSAL 168
Cdd:TIGR00957 1381 DPFS----QYSDEEVW----WALELAHLKTFVSalpdkldHECAEggenLSVGQRQLVCLARALLRKTKILVLDEATAAV 1452

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2753759418  169 DYKLRKELQQELRNiqKRLGITFVFVTHDQEEALAMSDwIFVMHDGLIQQNGTPEDI 225
Cdd:TIGR00957 1453 DLETDNLIQSTIRT--QFEDCTVLTIAHRLNTIMDYTR-VIVLDKGEVAEFGAPSNL 1506
GguA NF040905
sugar ABC transporter ATP-binding protein;
104-216 1.82e-06

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 49.79  E-value: 1.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 104 PRLKKMSEKDIQDKVKEMlglVKLSGFERR----------EISELSGGQQQRVAIARALANDPEVLLLDEPLSALD---- 169
Cdd:NF040905  364 ANLGKVSRRGVIDENEEI---KVAEEYRKKmniktpsvfqKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDvgak 440

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2753759418 170 ---YKLRKELQQElrniqkrlGITFVFVTHDQEEALAMSDWIFVMHDGLI 216
Cdd:NF040905  441 yeiYTIINELAAE--------GKGVIVISSELPELLGMCDRIYVMNEGRI 482
PLN03073 PLN03073
ABC transporter F family; Provisional
 123-199 7.07e-06

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 47.93  E-value: 7.07e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2753759418 123 GLVKLSGFERREISELSGGQQQRVAIARALANDPEVLLLDEPLSALDYKLRKELQQELRNIQKrlgiTFVFVTHDQE 199
Cdd:PLN03073  330 GLSFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPK----TFIVVSHARE 402
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
 18-218 7.07e-06

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


Pssm-ID: 213256 [Multi-domain]  Cd Length: 275  Bit Score: 47.16  E-value: 7.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  18 GDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADaGKIFFEGQVINDVPAEKRRvntvfQNYSLFPNmNVF 97
Cdd:cd03289    15 GGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWR-----KAFGVIPQ-KVF 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  98 dnVAFGPRLK------KMSEKDIQdKVKEMLGLvklsgferREISE----------------LSGGQQQRVAIARALAND 155
Cdd:cd03289    88 --IFSGTFRKnldpygKWSDEEIW-KVAEEVGL--------KSVIEqfpgqldfvlvdggcvLSHGHKQLMCLARSVLSK 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2753759418 156 PEVLLLDEPLSALDYKLRKELQQELRniQKRLGITFVFVTHdQEEALAMSDWIFVMHDGLIQQ 218
Cdd:cd03289   157 AKILLLDEPSAHLDPITYQVIRKTLK--QAFADCTVILSEH-RIEAMLECQRFLVIEENKVRQ 216
ABCC_SUR2 cd03288
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...
 22-225 4.54e-05

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: 44.51  E-value: 4.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  22 VLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAE--KRRVNTVFQNYSLFPNMNVFDn 99
Cdd:cd03288    36 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHtlRSRLSIILQDPILFSGSIRFN- 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 100 vaFGPRlKKMSEKDIQD--KVKEMLGLVK-LSGFERREISE----LSGGQQQRVAIARALANDPEVLLLDEPLSALDYKL 172
Cdd:cd03288   115 --LDPE-CKCTDDRLWEalEIAQLKNMVKsLPGGLDAVVTEggenFSVGQRQLFCLARAFVRKSSILIMDEATASIDMAT 191

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2753759418 173 RKELQQELRN-IQKRLGITFVFVTHDQEEAlamsDWIFVMHDGLIQQNGTPEDI 225
Cdd:cd03288   192 ENILQKVVMTaFADRTVVTIAHRVSTILDA----DLVLVLSRGILVECDTPENL 241
PLN03232 PLN03232
ABC transporter C family member; Provisional
 8-225 4.89e-05

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 45.74  E-value: 4.89e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418    8 LEFSKVALSF--GDTEVLKEIDLVLESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVP-AEKRRVNTV 84
Cdd:PLN03232  1235 IKFEDVHLRYrpGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGlTDLRRVLSI 1314

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418   85 F-QNYSLFP-----NMNVFDNVAFGPRLKKMSEKDIQDKVKEMLGLVKLSGFERREisELSGGQQQRVAIARALANDPEV 158
Cdd:PLN03232  1315 IpQSPVLFSgtvrfNIDPFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGE--NFSVGQRQLLSLARALLRRSKI 1392

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2753759418  159 LLLDEPLSALDYKLRKELQQELRNIQKrlGITFVFVTHdQEEALAMSDWIFVMHDGLIQQNGTPEDI 225
Cdd:PLN03232  1393 LVLDEATASVDVRTDSLIQRTIREEFK--SCTMLVIAH-RLNTIIDCDKILVLSSGQVLEYDSPQEL 1456
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
 135-211 3.88e-04

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: 40.81  E-value: 3.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 135 ISELSGGQQQRVAIARALAN---DPEVL-LLDEPLSALDYKLRKELqqeLRNIQKRL--GITFVFVTHDqEEALAMSDWI 208
Cdd:cd03227    75 RLQLSGGEKELSALALILALaslKPRPLyILDEIDRGLDPRDGQAL---AEAILEHLvkGAQVIVITHL-PELAELADKL 150


                  ...
gi 2753759418 209 FVM 211
Cdd:cd03227   151 IHI 153
ABC_sbcCD cd03279
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ...
 30-199 1.05e-03

ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.


Pssm-ID: 213246 [Multi-domain]  Cd Length: 213  Bit Score: 39.94  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  30 LESGKFYTLLGPSGSGKSTILKLISGQLQADAGKIFFEGQVINDVPAEKRRVNTVF------QNYSLF--PNMNV--FDN 99
Cdd:cd03279    25 LDNNGLFLICGPTGAGKSTILDAITYALYGKTPRYGRQENLRSVFAPGEDTAEVSFtfqlggKKYRVErsRGLDYdqFTR 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 100 VAFGPrlkkmsekdiQDKVKEMLglvklsgfeRREISELSGGQQQRVAIARALA---------NDP-EVLLLDEPLSALD 169
Cdd:cd03279   105 IVLLP----------QGEFDRFL---------ARPVSTLSGGETFLASLSLALAlsevlqnrgGARlEALFIDEGFGTLD 165

                         170       180       190
                  ....*....|....*....|....*....|
gi 2753759418 170 YKLRKELQQELRNIQkRLGITFVFVTHDQE 199
Cdd:cd03279   166 PEALEAVATALELIR-TENRMVGVISHVEE 194
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
 122-224 1.52e-03

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 40.97  E-value: 1.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  122 LGLVKLSgfERREISELSGGQQQRVAIARALANDPE--VLLLDEPLSALDYKLRKELQQELRNIQKRlGITFVFVTHDqE 199
Cdd:PRK00635   463 LGLPYLT--PERALATLSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQ-GNTVLLVEHD-E 538

                           90       100       110
                   ....*....|....*....|....*....|.
gi 2753759418  200 EALAMSDWIF------VMHDGLIQQNGTPED 224
Cdd:PRK00635   539 QMISLADRIIdigpgaGIFGGEVLFNGSPRE 569
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
 104-226 2.92e-03

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 39.81  E-value: 2.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  104 PRLKKMsEKDIQDKVKEMLGLVKLSgferREISELSGGQQQRVAIARAL---ANDPEVLLLDEPLSALDYKLRKELQQEL 180
Cdd:PRK00635  1671 PFLKKI-QKPLQALIDNGLGYLPLG----QNLSSLSLSEKIAIKIAKFLylpPKHPTLFLLDEIATSLDNQQKSALLVQL 1745

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2753759418  181 RNIQKrLGITFVFVTHDQeEALAMSDWIFVM------HDGLIQQNGTPEDIY 226
Cdd:PRK00635  1746 RTLVS-LGHSVIYIDHDP-ALLKQADYLIEMgpgsgkTGGKILFSGPPKDIS 1795
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
15-197 7.13e-03

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 440188 [Multi-domain]  Cd Length: 204  Bit Score: 37.30  E-value: 7.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  15 LSFGDTEvlkEIDLvleSGKFYTLLGPSGSGKSTILKLI----------SGQLQADA-----------------GKIF-- 65
Cdd:COG0419    11 RSYRDTE---TIDF---DDGLNLIVGPNGAGKSTILEAIryalygkarsRSKLRSDLinvgseeasvelefehgGKRYri 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418  66 --FEGQVINDVPAEKRRVNTVFQNysLFpNMNVFDNVAFgpRLK--------KMSEKDIQDKVKEMLgLVKLSGFErrEI 135
Cdd:COG0419    85 erRQGEFAEFLEAKPSERKEALKR--LL-GLEIYEELKE--RLKeleealesALEELAELQKLKQEI-LAQLSGLD--PI 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2753759418 136 SELSGGQQQRVAIARALAndpevLLLDepLSALDYKLRKELQQELRNIQkrlgitfvFVTHD 197
Cdd:COG0419   157 ETLSGGERLRLALADLLS-----LILD--FGSLDEERLERLLDALEELA--------IITHV 203
COG1106 COG1106
ATPase/GTPase, AAA15 family [General function prediction only];
108-199 8.88e-03

ATPase/GTPase, AAA15 family [General function prediction only];


Pssm-ID: 440723 [Multi-domain]  Cd Length: 330  Bit Score: 37.72  E-value: 8.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753759418 108 KMSEKDIQDKVKEMLGLVKLSGFERREISELSGGQQQRVAIARALAN---DPEVLLLDEPLSALDYKLRKELQQELRNIQ 184
Cdd:COG1106   173 EVEEEEIEDLVERKLIFKHKGGNVPLPLSEESDGTKRLLALAGALLDalaKGGVLLIDEIEASLHPSLLRKLLKLFLDLA 252

                          90
                  ....*....|....*
gi 2753759418 185 KRLGITFVFVTHDQE 199
Cdd:COG1106   253 NKNNAQLIFTTHSTE 267
 
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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