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Conserved domains on  [gi|488386109|ref|WP_002455494|]
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MULTISPECIES: ABC transporter ATP-binding protein [Staphylococcus]

Protein Classification

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

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
 1-342 0e+00

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


:

Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 520.43  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   1 MESLLSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANKRRVNT 80
Cdd:COG3842    2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGM 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  81 VFQDYALFPHLNVYENIAFGLRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDE 160
Cdd:COG3842   82 VFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDE 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 161 SLSALDLKLRTEMQYELRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIYDEPVNRFVADFIGESNI 240
Cdd:COG3842  162 PLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGEANL 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 241 VDGTMVKD--FVVNIYGQDFEC-VDARIPSGKKIEVVIRPEDISLV-ESTQGLFTATVDSMLFRGVHYEICCIDEKGYEW 316
Cdd:COG3842  242 LPGTVLGDegGGVRTGGRTLEVpADAGLAAGGPVTVAIRPEDIRLSpEGPENGLPGTVEDVVFLGSHVRYRVRLGDGQEL 321

                        330       340       350
                 ....*....|....*....|....*....|
gi 488386109 317 VIQSTKKT----TIGSQVGLFFEPEAIHIM 342
Cdd:COG3842  322 VVRVPNRAalplEPGDRVGLSWDPEDVVVL 351
 
Name Accession Description Interval E-value
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
 1-342 0e+00

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 520.43  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   1 MESLLSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANKRRVNT 80
Cdd:COG3842    2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGM 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  81 VFQDYALFPHLNVYENIAFGLRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDE 160
Cdd:COG3842   82 VFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDE 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 161 SLSALDLKLRTEMQYELRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIYDEPVNRFVADFIGESNI 240
Cdd:COG3842  162 PLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGEANL 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 241 VDGTMVKD--FVVNIYGQDFEC-VDARIPSGKKIEVVIRPEDISLV-ESTQGLFTATVDSMLFRGVHYEICCIDEKGYEW 316
Cdd:COG3842  242 LPGTVLGDegGGVRTGGRTLEVpADAGLAAGGPVTVAIRPEDIRLSpEGPENGLPGTVEDVVFLGSHVRYRVRLGDGQEL 321

                        330       340       350
                 ....*....|....*....|....*....|
gi 488386109 317 VIQSTKKT----TIGSQVGLFFEPEAIHIM 342
Cdd:COG3842  322 VVRVPNRAalplEPGDRVGLSWDPEDVVVL 351
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
3-284 1.74e-149

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 426.67  E-value: 1.74e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   3 SLLSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANKRRVNTVF 82
Cdd:PRK09452  13 PLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTVF 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  83 QDYALFPHLNVYENIAFGLRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDESL 162
Cdd:PRK09452  93 QSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESL 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 163 SALDLKLRTEMQYELRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIYDEPVNRFVADFIGESNIVD 242
Cdd:PRK09452 173 SALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIGEINIFD 252

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 488386109 243 GTMV-----KDFVVNIYGQDFEC-VDARIPSGKKIEVVIRPEDISLVE 284
Cdd:PRK09452 253 ATVIerldeQRVRANVEGRECNIyVNFAVEPGQKLHVLLRPEDLRVEE 300
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
 5-236 1.42e-148

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: 418.56  E-value: 1.42e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   5 LSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANKRRVNTVFQD 84
Cdd:cd03300    1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  85 YALFPHLNVYENIAFGLRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDESLSA 164
Cdd:cd03300   81 YALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488386109 165 LDLKLRTEMQYELRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIYDEPVNRFVADFIG 236
Cdd:cd03300  161 LDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
potA TIGR01187
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ...
 35-336 1.78e-117

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: 343.32  E-value: 1.78e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   35 LLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANKRRVNTVFQDYALFPHLNVYENIAFGLRLKKFSKQEIDKE 114
Cdd:TIGR01187   1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  115 VKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDESLSALDLKLRTEMQYELRELQKRLGITFIFVTHD 194
Cdd:TIGR01187  81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  195 QEEALALSDYIFVMKDGEIQQFGTPTDIYDEPVNRFVADFIGESNIVDGTMVK---DFVVNIYGQDFEC---VDARIPSG 268
Cdd:TIGR01187 161 QEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVFEATVIErksEQVVLAGVEGRRCdiyTDVPVEKD 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  269 KKIEVVIRPEDISLVE----STQGLFTATVDSMLFRG----VHYEIccidEKGYEWVIQ-------STKKTTIGSQVGLF 333
Cdd:TIGR01187 241 QPLHVVLRPEKIVIEEedeaNSSNAIIGHVIDITYLGmtleVHVRL----ETGQKVLVSeffneddPHMSPSIGDRVGLT 316


                  ...
gi 488386109  334 FEP 336
Cdd:TIGR01187 317 WHP 319
tungstate_WtpC NF040840
tungstate ABC transporter ATP-binding protein WtpC;
20-341 1.37e-90

tungstate ABC transporter ATP-binding protein WtpC;


Pssm-ID: 468779 [Multi-domain]  Cd Length: 347  Bit Score: 275.42  E-value: 1.37e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  20 LNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANKRRVNTVFQDYALFPHLNVYENIAF 99
Cdd:NF040840  16 LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIAYVYQNYMLFPHKTVFENIAF 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 100 GLRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDESLSALDLKLRTEMQYELRE 179
Cdd:NF040840  96 GLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALDVQTRDELIREMKR 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 180 LQKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIYDEPVNRFVADFIGESNIVDGTMVKDFVVNIYGQDFE 259
Cdd:NF040840 176 WHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVGFENIIEGVAEKGGEGTILDTGNI 255

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 260 CVDARIPSGKKIEVVIRPEDISLveSTQGLFTATVDSmlFRGVHYEIccID---------EKGYEWVIQSTKKT------ 324
Cdd:NF040840 256 KIELPEEKKGKVRIGIRPEDITI--STEKVKTSARNE--FKGKVEEI--EDlgplvkltlDVGIILVAFITRSSfldlei 329

                        330
                 ....*....|....*..
gi 488386109 325 TIGSQVGLFFEPEAIHI 341
Cdd:NF040840 330 NEGKEVYASFKASAVHV 346
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 20-160 6.95e-50

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: 164.36  E-value: 6.95e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   20 LNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANKRRVN--TVFQDYALFPHLNVYENI 97
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEigYVFQDPQLFPRLTVRENL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488386109   98 AFGLRLKKFSKQEIDKEVKEALKLVKLTGYEQRHID----EMSGGQKQRVAIARAIVNKPEILLLDE 160
Cdd:pfam00005  81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGerpgTLSGGQRQRVAIARALLTKPKLLLLDE 147
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
14-200 9.24e-28

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 107.70  E-value: 9.24e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  14 FDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGqiiyknqSIEKLPAnkRRVNTVFQDYAL---FPh 90
Cdd:NF040873   2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSG-------TVRRAGG--ARVAYVPQRSEVpdsLP- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  91 LNVYENIAFGL--------RLKKFSKQEIDkevkEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDESL 162
Cdd:NF040873  72 LTVRDLVAMGRwarrglwrRLTRDDRAAVD----DALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPT 147

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 488386109 163 SALDLKLRTEMQYELRELQKRlGITFIFVTHDQEEALA 200
Cdd:NF040873 148 TGLDAESRERIIALLAEEHAR-GATVVVVTHDLELVRR 184
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
11-222 4.03e-16

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 79.78  E-value: 4.03e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  11 TKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEklpAN----KRRVNTVFQDYA 86
Cdd:NF033858 273 TMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVD---AGdiatRRRVGYMSQAFS 349

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  87 LFPHLNVYENIAFGLRLKKFSKQEIDKEVKEALKLVKLTGYeqrhIDEMSG----GQKQRVAIARAIVNKPEILLLDESL 162
Cdd:NF033858 350 LYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADV----ADALPDslplGIRQRLSLAVAVIHKPELLILDEPT 425

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488386109 163 SALDLKLRTEMQYELRELQKRLGITfIFV-THDQEEAlALSDYIFVMKDGEIQQFGTPTDI 222
Cdd:NF033858 426 SGVDPVARDMFWRLLIELSREDGVT-IFIsTHFMNEA-ERCDRISLMHAGRVLASDTPAAL 484
GguA NF040905
sugar ABC transporter ATP-binding protein;
4-211 9.81e-14

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 72.13  E-value: 9.81e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   4 LLSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFeQPN---EGQIIYKNQSIE--KLPANKRR- 77
Cdd:NF040905   1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGV-YPHgsyEGEILFDGEVCRfkDIRDSEALg 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  78 VNTVFQDYALFPHLNVYENIAFGLRLKKF---SKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPE 154
Cdd:NF040905  80 IVIIHQELALIPYLSIAENIFLGNERAKRgviDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVK 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488386109 155 ILLLDESLSALD-------LKLrtemqyeLRELQKRlGITFIFVTHDQEEALALSDYIFVMKDG 211
Cdd:NF040905 160 LLILDEPTAALNeedsaalLDL-------LLELKAQ-GITSIIISHKLNEIRRVADSITVLRDG 215
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
10-222 1.61e-12

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 68.61  E-value: 1.61e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  10 VTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIeklpANKRRVNTVFQDYA--- 86
Cdd:NF033858   7 VSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDM----ADARHRRAVCPRIAymp 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  87 ------LFPHLNVYENIAFGLRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDE 160
Cdd:NF033858  83 qglgknLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDE 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488386109 161 SLSALD-LKLRtemQY-----ELRelQKRLGITFIFVTHDQEEAlALSDYIFVMKDGEIQQFGTPTDI 222
Cdd:NF033858 163 PTTGVDpLSRR---QFwelidRIR--AERPGMSVLVATAYMEEA-ERFDWLVAMDAGRVLATGTPAEL 224
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 29-212 1.04e-10

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 59.31  E-value: 1.04e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109    29 SGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANKRRVNTVFQDYALfphlnvyeniafglrlkkfsk 108
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKA--------------------- 59

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   109 qeidkevkealklvkltgyeqrhidEMSGGQKQRVAIARAIVNKPEILLLDESLSALD-----LKLRTEMQYELRELQKR 183
Cdd:smart00382  60 -------------------------SGSGELRLRLALALARKLKPDVLILDEITSLLDaeqeaLLLLLEELRLLLLLKSE 114

                          170       180       190
                   ....*....|....*....|....*....|....
gi 488386109   184 LGITFIFVTHDQE-----EALALSDYIFVMKDGE 212
Cdd:smart00382 115 KNLTVILTTNDEKdlgpaLLRRRFDRRIVLLLIL 148
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
8-213 2.95e-10

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 60.90  E-value: 2.95e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   8 KKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTiLKLIAGFEQPNEGQIIYKnqsIEKLPANKRRVNTVFQDY-- 85
Cdd:NF000106  17 RGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**R-GALPAHV*GPDAGRRPWR---F*TWCANRRALRRTIG*Hrp 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  86 ---ALFPHLNVYENIAFGLRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDESL 162
Cdd:NF000106  93 vr*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPT 172

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 488386109 163 SALDLKLRTEMQYELRELQkRLGITFIFVTHDQEEALALSDYIFVMKDGEI 213
Cdd:NF000106 173 TGLDPRTRNEVWDEVRSMV-RDGATVLLTTQYMEEAEQLAHELTVIDRGRV 222
 
Name Accession Description Interval E-value
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
 1-342 0e+00

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 520.43  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   1 MESLLSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANKRRVNT 80
Cdd:COG3842    2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGM 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  81 VFQDYALFPHLNVYENIAFGLRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDE 160
Cdd:COG3842   82 VFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDE 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 161 SLSALDLKLRTEMQYELRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIYDEPVNRFVADFIGESNI 240
Cdd:COG3842  162 PLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGEANL 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 241 VDGTMVKD--FVVNIYGQDFEC-VDARIPSGKKIEVVIRPEDISLV-ESTQGLFTATVDSMLFRGVHYEICCIDEKGYEW 316
Cdd:COG3842  242 LPGTVLGDegGGVRTGGRTLEVpADAGLAAGGPVTVAIRPEDIRLSpEGPENGLPGTVEDVVFLGSHVRYRVRLGDGQEL 321

                        330       340       350
                 ....*....|....*....|....*....|
gi 488386109 317 VIQSTKKT----TIGSQVGLFFEPEAIHIM 342
Cdd:COG3842  322 VVRVPNRAalplEPGDRVGLSWDPEDVVVL 351
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
 5-341 3.70e-150

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


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 427.18  E-value: 3.70e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   5 LSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANKRRVNTVFQD 84
Cdd:COG3839    4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIAMVFQS 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  85 YALFPHLNVYENIAFGLRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDESLSA 164
Cdd:COG3839   84 YALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSN 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 165 LDLKLRTEMQYELRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIYDEPVNRFVADFIGES--NIVD 242
Cdd:COG3839  164 LDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGFIGSPpmNLLP 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 243 GTMVKDFVVnIYGQDFEC-VDARIPSGKKIEVVIRPEDISLVESTQGLFTATVDSMLFRGVHYEICCiDEKGYEWVIQST 321
Cdd:COG3839  244 GTVEGGGVR-LGGVRLPLpAALAAAAGGEVTLGIRPEHLRLADEGDGGLEATVEVVEPLGSETLVHV-RLGGQELVARVP 321

                        330       340
                 ....*....|....*....|..
gi 488386109 322 KKTTI--GSQVGLFFEPEAIHI 341
Cdd:COG3839  322 GDTRLrpGDTVRLAFDPERLHL 343
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
3-284 1.74e-149

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 426.67  E-value: 1.74e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   3 SLLSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANKRRVNTVF 82
Cdd:PRK09452  13 PLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTVF 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  83 QDYALFPHLNVYENIAFGLRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDESL 162
Cdd:PRK09452  93 QSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESL 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 163 SALDLKLRTEMQYELRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIYDEPVNRFVADFIGESNIVD 242
Cdd:PRK09452 173 SALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIGEINIFD 252

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 488386109 243 GTMV-----KDFVVNIYGQDFEC-VDARIPSGKKIEVVIRPEDISLVE 284
Cdd:PRK09452 253 ATVIerldeQRVRANVEGRECNIyVNFAVEPGQKLHVLLRPEDLRVEE 300
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
 5-236 1.42e-148

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: 418.56  E-value: 1.42e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   5 LSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANKRRVNTVFQD 84
Cdd:cd03300    1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  85 YALFPHLNVYENIAFGLRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDESLSA 164
Cdd:cd03300   81 YALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488386109 165 LDLKLRTEMQYELRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIYDEPVNRFVADFIG 236
Cdd:cd03300  161 LDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
 5-344 5.84e-125

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


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 363.31  E-value: 5.84e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   5 LSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIE-KLPANKRRVNTVFQ 83
Cdd:COG1118    3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFtNLPPRERRVGFVFQ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  84 DYALFPHLNVYENIAFGLRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDESLS 163
Cdd:COG1118   83 HYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFG 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 164 ALDLKLRTEMQYELRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIYDEPVNRFVADFIGESNIVDG 243
Cdd:COG1118  163 ALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLGCVNVLRG 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 244 TmVKDFVVNIYGQDFEcVDARIPSGKKiEVVIRPEDISLVESTQG--LFTATVDSMLFRG--VHYEICCIDEKGYEWVIQ 319
Cdd:COG1118  243 R-VIGGQLEADGLTLP-VAEPLPDGPA-VAGVRPHDIEVSREPEGenTFPATVARVSELGpeVRVELKLEDGEGQPLEAE 319

                        330       340       350
                 ....*....|....*....|....*....|.
gi 488386109 320 STKKT------TIGSQVglFFEPEAIHIMVP 344
Cdd:COG1118  320 VTKEAwaelglAPGDPV--YLRPRPARVFLP 348
potA TIGR01187
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ...
 35-336 1.78e-117

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: 343.32  E-value: 1.78e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   35 LLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANKRRVNTVFQDYALFPHLNVYENIAFGLRLKKFSKQEIDKE 114
Cdd:TIGR01187   1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  115 VKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDESLSALDLKLRTEMQYELRELQKRLGITFIFVTHD 194
Cdd:TIGR01187  81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  195 QEEALALSDYIFVMKDGEIQQFGTPTDIYDEPVNRFVADFIGESNIVDGTMVK---DFVVNIYGQDFEC---VDARIPSG 268
Cdd:TIGR01187 161 QEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVFEATVIErksEQVVLAGVEGRRCdiyTDVPVEKD 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  269 KKIEVVIRPEDISLVE----STQGLFTATVDSMLFRG----VHYEIccidEKGYEWVIQ-------STKKTTIGSQVGLF 333
Cdd:TIGR01187 241 QPLHVVLRPEKIVIEEedeaNSSNAIIGHVIDITYLGmtleVHVRL----ETGQKVLVSeffneddPHMSPSIGDRVGLT 316


                  ...
gi 488386109  334 FEP 336
Cdd:TIGR01187 317 WHP 319
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
3-306 4.74e-114

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 335.54  E-value: 4.74e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   3 SLLSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANKRRVNTVF 82
Cdd:PRK11432   5 NFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMVF 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  83 QDYALFPHLNVYENIAFGLRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDESL 162
Cdd:PRK11432  85 QSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPL 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 163 SALDLKLRTEMQYELRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIYDEPVNRFVADFIGESNIVD 242
Cdd:PRK11432 165 SNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMGDANIFP 244

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488386109 243 GTMVKDFvVNIYGQDFECVDA---RIPSGkKIEVVIRPEDISLVESTQGLFTATVDSMLFRGVHYEI 306
Cdd:PRK11432 245 ATLSGDY-VDIYGYRLPRPAAfafNLPDG-ECTVGVRPEAITLSEQGEESQRCTIKHVAYMGPQYEV 309
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
 5-217 3.87e-113

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


Pssm-ID: 213226 [Multi-domain]  Cd Length: 213  Bit Score: 327.94  E-value: 3.87e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   5 LSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANKRRVNTVFQD 84
Cdd:cd03259    1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVFQD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  85 YALFPHLNVYENIAFGLRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDESLSA 164
Cdd:cd03259   81 YALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 488386109 165 LDLKLRTEMQYELRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFG 217
Cdd:cd03259  161 LDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
 5-217 1.24e-101

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: 298.78  E-value: 1.24e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   5 LSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANKRRVNTVFQD 84
Cdd:cd03301    1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVFQN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  85 YALFPHLNVYENIAFGLRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDESLSA 164
Cdd:cd03301   81 YALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 488386109 165 LDLKLRTEMQYELRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFG 217
Cdd:cd03301  161 LDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
 7-237 4.28e-101

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: 298.48  E-value: 4.28e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   7 FKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANKRRVNTVFQDYA 86
Cdd:cd03296    5 VRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFVFQHYA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  87 LFPHLNVYENIAFGLRLKK----FSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDESL 162
Cdd:cd03296   85 LFRHMTVFDNVAFGLRVKPrserPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPF 164

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488386109 163 SALDLKLRTEMQYELRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIYDEPVNRFVADFIGE 237
Cdd:cd03296  165 GALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFLGE 239
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
5-296 1.30e-95

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


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 288.67  E-value: 1.30e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   5 LSFKKVTKKFD-DTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKL-PANkRRVNTVF 82
Cdd:PRK11650   4 LKLQAVRKSYDgKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELePAD-RDIAMVF 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  83 QDYALFPHLNVYENIAFGLRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDESL 162
Cdd:PRK11650  83 QNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPL 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 163 SALDLKLRTEMQYELRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIYDEPVNRFVADFIGES--NI 240
Cdd:PRK11650 163 SNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASFIGSPamNL 242

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 488386109 241 VDGTMVKDFVVNIYGQDFE---CVDARIPSGKKIEVVIRPEDISLVESTQGLfTATVDS 296
Cdd:PRK11650 243 LDGRVSADGAAFELAGGIAlplGGGYRQYAGRKLTLGIRPEHIALSSAEGGV-PLTVDT 300
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
9-282 2.77e-92

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 280.05  E-value: 2.77e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   9 KVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANKRRVNTVFQDYALF 88
Cdd:PRK10851   7 NIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVFQHYALF 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  89 PHLNVYENIAFGL----RLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDESLSA 164
Cdd:PRK10851  87 RHMTVFDNIAFGLtvlpRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGA 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 165 LDLKLRTEMQYELRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIYDEPVNRFVADFIGESNIVDGT 244
Cdd:PRK10851 167 LDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMGEVNRLQGT 246

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 488386109 245 mvkdfvvnIYGQDFECVDARIPSG------KKIEVVIRPEDISL 282
Cdd:PRK10851 247 --------IRGGQFHVGAHRWPLGytpayqGPVDLFLRPWEVDI 282
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
 1-211 1.32e-91

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


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 275.04  E-value: 1.32e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   1 MESLLSFKKVTKKF----DDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKlPANKR 76
Cdd:COG1116    4 AAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG-PGPDR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  77 RVntVFQDYALFPHLNVYENIAFGLRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEIL 156
Cdd:COG1116   83 GV--VFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVL 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 488386109 157 LLDESLSALDLKLRTEMQYELRELQKRLGITFIFVTHDQEEALALSDYIFVMKDG 211
Cdd:COG1116  161 LMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSAR 215
tungstate_WtpC NF040840
tungstate ABC transporter ATP-binding protein WtpC;
20-341 1.37e-90

tungstate ABC transporter ATP-binding protein WtpC;


Pssm-ID: 468779 [Multi-domain]  Cd Length: 347  Bit Score: 275.42  E-value: 1.37e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  20 LNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANKRRVNTVFQDYALFPHLNVYENIAF 99
Cdd:NF040840  16 LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIAYVYQNYMLFPHKTVFENIAF 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 100 GLRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDESLSALDLKLRTEMQYELRE 179
Cdd:NF040840  96 GLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALDVQTRDELIREMKR 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 180 LQKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIYDEPVNRFVADFIGESNIVDGTMVKDFVVNIYGQDFE 259
Cdd:NF040840 176 WHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVGFENIIEGVAEKGGEGTILDTGNI 255

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 260 CVDARIPSGKKIEVVIRPEDISLveSTQGLFTATVDSmlFRGVHYEIccID---------EKGYEWVIQSTKKT------ 324
Cdd:NF040840 256 KIELPEEKKGKVRIGIRPEDITI--STEKVKTSARNE--FKGKVEEI--EDlgplvkltlDVGIILVAFITRSSfldlei 329

                        330
                 ....*....|....*..
gi 488386109 325 TIGSQVGLFFEPEAIHI 341
Cdd:NF040840 330 NEGKEVYASFKASAVHV 346
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
4-284 1.26e-88

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 271.71  E-value: 1.26e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   4 LLSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANKRRVNTVFQ 83
Cdd:PRK11607  19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMFQ 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  84 DYALFPHLNVYENIAFGLRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDESLS 163
Cdd:PRK11607  99 SYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMG 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 164 ALDLKLRTEMQYELRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIYDEPVNRFVADFIGESNIVDG 243
Cdd:PRK11607 179 ALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNVFEG 258

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 488386109 244 TMVK---DFVVnIYGQDFEC-----VDARIPSGKKIEVVIRPEDISLVE 284
Cdd:PRK11607 259 VLKErqeDGLV-IDSPGLVHplkvdADASVVDNVPVHVALRPEKIMLCE 306
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
1-236 2.40e-88

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 270.75  E-value: 2.40e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   1 MESLlSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANKRRVNT 80
Cdd:PRK11000   1 MASV-TLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGM 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  81 VFQDYALFPHLNVYENIAFGLRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDE 160
Cdd:PRK11000  80 VFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDE 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488386109 161 SLSALDLKLRTEMQYELRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIYDEPVNRFVADFIG 236
Cdd:PRK11000 160 PLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIG 235
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
 5-208 4.36e-88

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: 264.72  E-value: 4.36e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   5 LSFKKVTKKFDD----TTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKlPANKRRVnt 80
Cdd:cd03293    1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG-PGPDRGY-- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  81 VFQDYALFPHLNVYENIAFGLRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDE 160
Cdd:cd03293   78 VFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDE 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 488386109 161 SLSALDLKLRTEMQYELRELQKRLGITFIFVTHDQEEALALSDYIFVM 208
Cdd:cd03293  158 PFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
 20-240 2.32e-84

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


Pssm-ID: 213266 [Multi-domain]  Cd Length: 235  Bit Score: 255.72  E-value: 2.32e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  20 LNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANKRRVNTVFQDYALFPHLNVYENIAF 99
Cdd:cd03299   15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVPQNYALFPHMTVYKNIAY 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 100 GLRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDESLSALDLKLRTEMQYELRE 179
Cdd:cd03299   95 GLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKK 174

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488386109 180 LQKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIYDEPVNRFVADFIGESNI 240
Cdd:cd03299  175 IRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLGFNNI 235
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
 5-238 6.57e-80

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: 244.52  E-value: 6.57e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   5 LSFKKVTKKF-DDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANK--RRVNTV 81
Cdd:cd03295    1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElrRKIGYV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  82 FQDYALFPHLNVYENIAFGLRLKKFSKQEIDKEVKEALKLVKL--TGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLD 159
Cdd:cd03295   81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488386109 160 ESLSALDLKLRTEMQYELRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIYDEPVNRFVADFIGES 238
Cdd:cd03295  161 EPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVGAD 239
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
 10-235 7.03e-78

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: 240.24  E-value: 7.03e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  10 VTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPAN------KRRVNTVFQ 83
Cdd:cd03294   30 ILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKelrelrRKKISMVFQ 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  84 DYALFPHLNVYENIAFGLRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDESLS 163
Cdd:cd03294  110 SFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFS 189

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488386109 164 ALDLKLRTEMQYELRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIYDEPVNRFVADFI 235
Cdd:cd03294  190 ALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFF 261
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
1-213 3.18e-76

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 234.55  E-value: 3.18e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   1 MESLLSFKKVTKKFDD----TTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANKR 76
Cdd:COG1136    1 MSPLLELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSEREL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  77 ---RVNT---VFQDYALFPHLNVYENIAFGLRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIV 150
Cdd:COG1136   81 arlRRRHigfVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488386109 151 NKPEILLLDESLSALDLKLRTE-MQyELRELQKRLGITFIFVTHDqEEALALSDYIFVMKDGEI 213
Cdd:COG1136  161 NRPKLILADEPTGNLDSKTGEEvLE-LLRELNRELGTTIVMVTHD-PELAARADRVIRLRDGRI 222
ProV COG4175
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ...
 20-235 3.86e-75

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


Pssm-ID: 443334 [Multi-domain]  Cd Length: 389  Bit Score: 237.31  E-value: 3.86e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  20 LNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANK------RRVNTVFQDYALFPHLNV 93
Cdd:COG4175   43 VNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITKLSKKElrelrrKKMSMVFQHFALLPHRTV 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  94 YENIAFGLRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDESLSALDLKLRTEM 173
Cdd:COG4175  123 LENVAFGLEIQGVPKAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPLIRREM 202

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488386109 174 QYELRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIYDEPVNRFVADFI 235
Cdd:COG4175  203 QDELLELQAKLKKTIVFITHDLDEALRLGDRIAIMKDGRIVQIGTPEEILTNPANDYVADFV 264
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
 5-212 1.84e-74

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: 228.23  E-value: 1.84e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   5 LSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKL----PANKRRVNT 80
Cdd:cd03229    1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLedelPPLRRRIGM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  81 VFQDYALFPHLNVYENIAFGLrlkkfskqeidkevkealklvkltgyeqrhidemSGGQKQRVAIARAIVNKPEILLLDE 160
Cdd:cd03229   81 VFQDFALFPHLTVLENIALGL----------------------------------SGGQQQRVALARALAMDPDVLLLDE 126

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 488386109 161 SLSALDLKLRTEMQYELRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGE 212
Cdd:cd03229  127 PTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
 1-235 2.85e-74

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: 229.87  E-value: 2.85e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   1 MESLLSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANK----- 75
Cdd:COG1127    2 SEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKElyelr 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  76 RRVNTVFQDYALFPHLNVYENIAFGLR-LKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPE 154
Cdd:COG1127   82 RRIGMLFQGGALFDSLTVFENVAFPLReHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPE 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 155 ILLLDESLSALDLKLRTEMQYELRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIYDEPvNRFVADF 234
Cdd:COG1127  162 ILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASD-DPWVRQF 240


                 .
gi 488386109 235 I 235
Cdd:COG1127  241 L 241
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
 2-226 2.99e-72

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: 233.64  E-value: 2.99e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   2 ESLLSFKKVTKKF-----DDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANK- 75
Cdd:COG1123  258 EPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSl 337

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  76 ----RRVNTVFQD--YALFPHLNVYENIAFGLRL-KKFSKQEIDKEVKEALKLVKL-TGYEQRHIDEMSGGQKQRVAIAR 147
Cdd:COG1123  338 relrRRVQMVFQDpySSLNPRMTVGDIIAEPLRLhGLLSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIAR 417

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488386109 148 AIVNKPEILLLDESLSALDLKLRTEMQYELRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIYDEP 226
Cdd:COG1123  418 ALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANP 496
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
5-237 4.35e-71

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 221.55  E-value: 4.35e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   5 LSFKKVTKKFDDTTIlnNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANKRRVNTVFQD 84
Cdd:COG3840    2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSMLFQE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  85 YALFPHLNVYENIAFGLRLK-KFSKQEIDKeVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDESLS 163
Cdd:COG3840   80 NNLFPHLTVAQNIGLGLRPGlKLTAEQRAQ-VEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFS 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488386109 164 ALDLKLRTEMQYELRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIYDEPVNRFVADFIGE 237
Cdd:COG3840  159 ALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYLGI 232
proV TIGR01186
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ...
 12-248 1.32e-70

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: 224.73  E-value: 1.32e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   12 KKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQI------IYKNQSIEKLPANKRRVNTVFQDY 85
Cdd:TIGR01186   1 KKTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIfidgenIMKQSPVELREVRRKKIGMVFQQF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   86 ALFPHLNVYENIAFGLRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDESLSAL 165
Cdd:TIGR01186  81 ALFPHMTILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSAL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  166 DLKLRTEMQYELRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIYDEPVNRFVADFIGESNIVDGTM 245
Cdd:TIGR01186 161 DPLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGKVDLSQVFD 240


                  ...
gi 488386109  246 VKD 248
Cdd:TIGR01186 241 AER 243
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
 5-223 2.07e-70

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: 219.90  E-value: 2.07e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   5 LSFKKVTKKF-DDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANK--RRVNTV 81
Cdd:COG1122    1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElrRKVGLV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  82 FQ--DYALFpHLNVYENIAFGLRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLD 159
Cdd:COG1122   81 FQnpDDQLF-APTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLD 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488386109 160 ESLSALDLKLRTEMQYELRELQKRlGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIY 223
Cdd:COG1122  160 EPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVF 222
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
 5-213 3.57e-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: 218.90  E-value: 3.57e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   5 LSFKKVTKKFDD----TTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANKR---- 76
Cdd:cd03255    1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  77 --RVNTVFQDYALFPHLNVYENIAFGLRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPE 154
Cdd:cd03255   81 rrHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 488386109 155 ILLLDESLSALDLKLRTEMQYELRELQKRLGITFIFVTHDQEEAlALSDYIFVMKDGEI 213
Cdd:cd03255  161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
 12-217 9.87e-70

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: 217.55  E-value: 9.87e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  12 KKFDDTTilnnMNLDIE-SGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYK-------NQSIEkLPANKRRVNTVFQ 83
Cdd:cd03297    8 KRLPDFT----LKIDFDlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNgtvlfdsRKKIN-LPPQQRKIGLVFQ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  84 DYALFPHLNVYENIAFGLRLKKFSKQEIdkEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDESLS 163
Cdd:cd03297   83 QYALFPHLNVRENLAFGLKRKRNREDRI--SVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFS 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488386109 164 ALDLKLRTEMQYELRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFG 217
Cdd:cd03297  161 ALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
TauB COG4525
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
3-208 2.69e-68

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


Pssm-ID: 443596 [Multi-domain]  Cd Length: 262  Bit Score: 215.50  E-value: 2.69e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   3 SLLSFKKVTKKFD----DTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKlPANKRRV 78
Cdd:COG4525    2 SMLTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG-PGADRGV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  79 ntVFQDYALFPHLNVYENIAFGLRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLL 158
Cdd:COG4525   81 --VFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLM 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 488386109 159 DESLSALDLKLRTEMQYELRELQKRLGITFIFVTHDQEEALALSDYIFVM 208
Cdd:COG4525  159 DEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVM 208
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
 5-234 7.68e-68

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: 213.52  E-value: 7.68e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   5 LSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKL-PANK----RRVN 79
Cdd:cd03261    1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLsEAELyrlrRRMG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  80 TVFQDYALFPHLNVYENIAFGLRLK-KFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLL 158
Cdd:cd03261   81 MLFQSGALFDSLTVFENVAFPLREHtRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488386109 159 DESLSALDLKLRTEMQYELRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIYDEPvNRFVADF 234
Cdd:cd03261  161 DEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASD-DPLVRQF 235
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
5-214 1.42e-66

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 209.52  E-value: 1.42e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   5 LSFKKVTKKF-DDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANK-----RRV 78
Cdd:COG2884    2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipylrRRI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  79 NTVFQDYALFPHLNVYENIAFGLRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLL 158
Cdd:COG2884   82 GVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLA 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 488386109 159 DESLSALDLKLRTE-MQYeLRELQkRLGITFIFVTHDQEEALALSDYIFVMKDGEIQ 214
Cdd:COG2884  162 DEPTGNLDPETSWEiMEL-LEEIN-RRGTTVLIATHDLELVDRMPKRVLELEDGRLV 216
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
5-222 8.25e-65

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 205.68  E-value: 8.25e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   5 LSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPAN-KRRVNTVFQ 83
Cdd:COG1131    1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEvRRRIGYVPQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  84 DYALFPHLNVYENIAFGLRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDESLS 163
Cdd:COG1131   81 EPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 488386109 164 ALDLKLRTEMQYELRELQKRlGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDI 222
Cdd:COG1131  161 GLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
 6-212 1.02e-63

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: 201.93  E-value: 1.02e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   6 SFKKVTKKFDDTT--ILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANK--RRVNTV 81
Cdd:cd03225    1 ELKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKElrRKVGLV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  82 FQ--DYALFpHLNVYENIAFGLRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLD 159
Cdd:cd03225   81 FQnpDDQFF-GPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLD 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 488386109 160 ESLSALDLKLRTEMQYELRELQKRlGITFIFVTHDQEEALALSDYIFVMKDGE 212
Cdd:cd03225  160 EPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
 4-222 3.06e-63

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: 202.20  E-value: 3.06e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   4 LLSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANK--RRVNTV 81
Cdd:COG1120    1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRElaRRIAYV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  82 FQDYALFPHLNVYENIAFGL-----RLKKFSKQEIDKeVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEIL 156
Cdd:COG1120   81 PQEPPAPFGLTVRELVALGRyphlgLFGRPSAEDREA-VEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLL 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 157 LLDESLSALDLKlrteMQYE----LRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDI 222
Cdd:COG1120  160 LLDEPTSHLDLA----HQLEvlelLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
 4-236 3.84e-63

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


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 201.38  E-value: 3.84e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   4 LLSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPAN----KRRVN 79
Cdd:COG1126    1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDinklRRKVG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  80 TVFQDYALFPHLNVYENIAFGLR-LKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLL 158
Cdd:COG1126   81 MVFQQFNLFPHLTVLENVTLAPIkVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 159 DESLSALDlklrTEMQYE----LRELQKRlGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIYDEPVNRFVADF 234
Cdd:COG1126  161 DEPTSALD----PELVGEvldvMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTRAF 235


                 ..
gi 488386109 235 IG 236
Cdd:COG1126  236 LS 237
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
 35-282 2.27e-62

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: 203.41  E-value: 2.27e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  35 LLGPSGCGKTTILKLIAGFEQPNEGQIIYKN---QSIEK---LPANKRRVNTVFQDYALFPHLNVYENIAFGLRLKKFSK 108
Cdd:COG4148   30 LFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlQDSARgifLPPHRRRIGYVFQEARLFPHLSVRGNLLYGRKRAPRAE 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 109 QEIDKEvkEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDESLSALDLKLRTEMQYELRELQKRLGITF 188
Cdd:COG4148  110 RRISFD--EVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYLERLRDELDIPI 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 189 IFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIYDEPVNRFVADFIGESNIVDGTmVKDF-------VVNIYGQDFECV 261
Cdd:COG4148  188 LYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAGGEEAGSVLEAT-VAAHdpdygltRLALGGGRLWVP 266

                        250       260
                 ....*....|....*....|.
gi 488386109 262 DARIPSGKKIEVVIRPEDISL 282
Cdd:COG4148  267 RLDLPPGTRVRVRIRARDVSL 287
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
 4-217 2.03e-61

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: 196.57  E-value: 2.03e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   4 LLSFKKVTKKFDD----TTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANKRR-- 77
Cdd:cd03257    1 LLEVKNLSVSFPTgggsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKir 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  78 ---VNTVFQDY--ALFPHLNVYENIAFGLRLKKFSKQEIDKEVKEALKLVKLTGYEQ---RHIDEMSGGQKQRVAIARAI 149
Cdd:cd03257   81 rkeIQMVFQDPmsSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEvlnRYPHELSGGQRQRVAIARAL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488386109 150 VNKPEILLLDESLSALDLKLRTEMQYELRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFG 217
Cdd:cd03257  161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
 4-222 1.17e-60

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


Pssm-ID: 440741 [Multi-domain]  Cd Length: 248  Bit Score: 195.41  E-value: 1.17e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   4 LLSFKKVTKKF----DDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEK--LPANKRR 77
Cdd:COG1124    1 MLEVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRrrRKAFRRR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  78 VNTVFQDY--ALFPHLNVYENIAFGLRLKKFskQEIDKEVKEALKLVKLT-GYEQRHIDEMSGGQKQRVAIARAIVNKPE 154
Cdd:COG1124   81 VQMVFQDPyaSLHPRHTVDRILAEPLRIHGL--PDREERIAELLEQVGLPpSFLDRYPHQLSGGQRQRVAIARALILEPE 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488386109 155 ILLLDESLSALDLKLRTEMQYELRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDI 222
Cdd:COG1124  159 LLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADL 226
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
 4-226 1.94e-60

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: 194.34  E-value: 1.94e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   4 LLSFKKVTKKFDDT----TILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANK---- 75
Cdd:cd03258    1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElrka 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  76 -RRVNTVFQDYALFPHLNVYENIAFGLRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPE 154
Cdd:cd03258   81 rRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488386109 155 ILLLDESLSALDLKLRTEMQYELRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIYDEP 226
Cdd:cd03258  161 VLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANP 232
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
5-238 3.62e-60

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 196.84  E-value: 3.62e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   5 LSFKKVTKKFD----DTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANK----- 75
Cdd:COG1135    2 IELENLSKTFPtkggPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElraar 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  76 RRVNTVFQDYALFPHLNVYENIAFGLRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEI 155
Cdd:COG1135   82 RKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 156 LLLDESLSALD-------LKLrtemqyeLRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIYDEPVN 228
Cdd:COG1135  162 LLCDEATSALDpettrsiLDL-------LKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQS 234

                        250
                 ....*....|
gi 488386109 229 RFVADFIGES 238
Cdd:COG1135  235 ELTRRFLPTV 244
PhnC COG3638
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ...
 3-237 2.72e-58

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


Pssm-ID: 442855 [Multi-domain]  Cd Length: 249  Bit Score: 189.11  E-value: 2.72e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   3 SLLSFKKVTKKF-DDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANK-----R 76
Cdd:COG3638    1 PMLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAlrrlrR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  77 RVNTVFQDYALFPHLNVYENIAFG-------LR--LKKFSKQEIDKeVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIAR 147
Cdd:COG3638   81 RIGMIFQQFNLVPRLSVLTNVLAGrlgrtstWRslLGLFPPEDRER-ALEALERVGLADKAYQRADQLSGGQQQRVAIAR 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 148 AIVNKPEILLLDESLSALDLKL-RTEMQYeLRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEIqqfgtptdIYDEP 226
Cdd:COG3638  160 ALVQEPKLILADEPVASLDPKTaRQVMDL-LRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRV--------VFDGP 230

                        250
                 ....*....|.
gi 488386109 227 VNRFVADFIGE 237
Cdd:COG3638  231 PAELTDAVLRE 241
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
 5-222 6.84e-58

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: 187.39  E-value: 6.84e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   5 LSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGF-----EQPNEGQIIYKNQSIEKLPAN----K 75
Cdd:cd03260    1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLDVDvlelR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  76 RRVNTVFQDYALFPhLNVYENIAFGLRL-KKFSKQEIDKEVKEALKLVKLTGYEQR--HIDEMSGGQKQRVAIARAIVNK 152
Cdd:cd03260   81 RRVGMVFQKPNPFP-GSIYDNVAYGLRLhGIKLKEELDERVEEALRKAALWDEVKDrlHALGLSGGQQQRLCLARALANE 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 153 PEILLLDESLSALDLKLRTEMQYELRELQKRlgITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDI 222
Cdd:cd03260  160 PEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
 1-226 9.34e-58

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: 195.51  E-value: 9.34e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   1 MESLLSFKKVTKKF--DDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPN---EGQIIYKNQSIEKLPANK 75
Cdd:COG1123    1 MTPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  76 R--RVNTVFQD--YALFPhLNVYENIAFGLRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVN 151
Cdd:COG1123   81 RgrRIGMVFQDpmTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALAL 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488386109 152 KPEILLLDESLSALDLKLRTEMQYELRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIYDEP 226
Cdd:COG1123  160 DPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAP 234
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
5-213 1.55e-57

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 185.79  E-value: 1.55e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   5 LSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANK--RRVNTVF 82
Cdd:COG4619    1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwrRQVAYVP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  83 QDYALFPHlNVYENIAFGLRLKKfsKQEIDKEVKEALKLVKLT-GYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDES 161
Cdd:COG4619   81 QEPALWGG-TVRDNLPFPFQLRE--RKFDRERALELLERLGLPpDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEP 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 488386109 162 LSALDLKLRTEMQYELRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEI 213
Cdd:COG4619  158 TSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
 5-200 1.02e-56

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


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 183.84  E-value: 1.02e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   5 LSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPN---EGQIIYKNQSIEKLPANKRRVNTV 81
Cdd:COG4136    2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAEQRRIGIL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  82 FQDYALFPHLNVYENIAFGLRlKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDES 161
Cdd:COG4136   82 FQDDLLFPHLSVGENLAFALP-PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEP 160

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 488386109 162 LSALDLKLRTEMQYELRELQKRLGITFIFVTHDQEEALA 200
Cdd:COG4136  161 FSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAPA 199
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
 5-213 1.55e-56

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: 183.50  E-value: 1.55e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   5 LSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPAN----KRRVNT 80
Cdd:cd03262    1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinelRQKVGM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  81 VFQDYALFPHLNVYENIAFGLR-LKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLD 159
Cdd:cd03262   81 VFQQFNLFPHLTVLENITLAPIkVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488386109 160 ESLSALDLKLRTEMQYELRELQKRlGITFIFVTHDQEEALALSDYIFVMKDGEI 213
Cdd:cd03262  161 EPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
 20-229 2.64e-55

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: 181.12  E-value: 2.64e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   20 LNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKlPANKRRVntVFQDYALFPHLNVYENIAF 99
Cdd:TIGR01184   1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITE-PGPDRMV--VFQNYSLLPWLTVRENIAL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  100 GLR--LKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDESLSALDLKLRTEMQYEL 177
Cdd:TIGR01184  78 AVDrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEEL 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 488386109  178 RELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDI-YDEPVNR 229
Cdd:TIGR01184 158 MQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVpFPRPRDR 210
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
 1-227 6.06e-54

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 177.97  E-value: 6.06e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   1 MESLLSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKlpaNKRRVNT 80
Cdd:COG1121    3 MMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR---ARRRIGY 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  81 VFQDYAL---FPhLNVYENIAFGLR-----LKKFSKQEIDKeVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNK 152
Cdd:COG1121   80 VPQRAEVdwdFP-ITVRDVVLMGRYgrrglFRRPSRADREA-VDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQD 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488386109 153 PEILLLDESLSALDLKLRTEMqYE-LRELQKRlGITFIFVTHDQEEALALSDYIFVMKDGEIqQFGTPTDIYDEPV 227
Cdd:COG1121  158 PDLLLLDEPFAGVDAATEEAL-YElLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRGLV-AHGPPEEVLTPEN 230
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
 4-257 1.20e-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: 1.20e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   4 LLSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLP-ANKRRVNTVF 82
Cdd:COG4555    1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPrEARRQIGVLP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  83 QDYALFPHLNVYENIAFGLRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDESL 162
Cdd:COG4555   81 DERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 163 SALDLKLRTEMQYELRELqKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIYDEpvnrfvadfIGESNIvd 242
Cdd:COG4555  161 NGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREE---------IGEENL-- 228

                        250
                 ....*....|....*
gi 488386109 243 gtmvKDFVVNIYGQD 257
Cdd:COG4555  229 ----EDAFVALIGSE 239
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
 5-213 1.86e-53

ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213197 [Multi-domain]  Cd Length: 173  Bit Score: 174.12  E-value: 1.86e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   5 LSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPAN-KRRVNTVFQ 83
Cdd:cd03230    1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEvKRRIGYLPE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  84 DYALFPHLNVYENIafglrlkkfskqeidkevkealklvkltgyeqrhidEMSGGQKQRVAIARAIVNKPEILLLDESLS 163
Cdd:cd03230   81 EPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTS 124

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 488386109 164 ALDLKLRTEMQYELRELQKRlGITFIFVTHDQEEALALSDYIFVMKDGEI 213
Cdd:cd03230  125 GLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
4-235 2.22e-53

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 176.44  E-value: 2.22e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   4 LLSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANKRRV----N 79
Cdd:PRK09493   1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIrqeaG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  80 TVFQDYALFPHLNVYENIAFG-LRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLL 158
Cdd:PRK09493  81 MVFQQFYLFPHLTALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLF 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488386109 159 DESLSALDLKLRTEMQYELRELQKRlGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIYDEPVNRFVADFI 235
Cdd:PRK09493 161 DEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFL 236
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
4-202 2.62e-53

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 176.81  E-value: 2.62e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   4 LLSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKlPANKRRVntVFQ 83
Cdd:PRK11248   1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG-PGAERGV--VFQ 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  84 DYALFPHLNVYENIAFGLRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDESLS 163
Cdd:PRK11248  78 NEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFG 157

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 488386109 164 ALDLKLRTEMQYELRELQKRLGITFIFVTHDQEEALALS 202
Cdd:PRK11248 158 ALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMA 196
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
 8-217 3.79e-53

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: 173.78  E-value: 3.79e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   8 KKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANKRRvntvfqdyal 87
Cdd:cd03214    3 ENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELA---------- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  88 fphlnvyENIAFglrlkkfskqeidkeVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDESLSALDL 167
Cdd:cd03214   73 -------RKIAY---------------VPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDI 130

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488386109 168 KlrteMQYE----LRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFG 217
Cdd:cd03214  131 A----HQIEllelLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
 5-229 7.74e-53

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: 175.06  E-value: 7.74e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   5 LSFKKVTKKF-DDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANK-----RRV 78
Cdd:cd03256    1 IEVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrqlrRQI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  79 NTVFQDYALFPHLNVYENIAFG-------LR--LKKFSKQEIdKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAI 149
Cdd:cd03256   81 GMIFQQFNLIERLSVLENVLSGrlgrrstWRslFGLFPKEEK-QRALAALERVGLLDKAYQRADQLSGGQQQRVAIARAL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 150 VNKPEILLLDESLSALDLKLRTE-MQYeLRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIYDEPVN 228
Cdd:cd03256  160 MQQPKLILADEPVASLDPASSRQvMDL-LKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTDEVLD 238


                 .
gi 488386109 229 R 229
Cdd:cd03256  239 E 239
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
 7-213 1.19e-52

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: 173.75  E-value: 1.19e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   7 FKKVTKKF-DDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANK-----RRVNT 80
Cdd:cd03292    3 FINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipylrRKIGV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  81 VFQDYALFPHLNVYENIAFGLRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDE 160
Cdd:cd03292   83 VFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADE 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 488386109 161 SLSALDLKLRTEMQYELRELQKRlGITFIFVTHDQEEALALSDYIFVMKDGEI 213
Cdd:cd03292  163 PTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
ECF_ATPase_1 TIGR04520
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
 5-223 1.96e-50

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: 169.53  E-value: 1.96e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109    5 LSFKKVTKKFDDTT--ILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQII---YKNQSIEKLPANKRRVN 79
Cdd:TIGR04520   1 IEVENVSFSYPESEkpALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTvdgLDTLDEENLWEIRKKVG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   80 TVFQdyalfphlN---------VYENIAFGLRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIV 150
Cdd:TIGR04520  81 MVFQ--------NpdnqfvgatVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLA 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488386109  151 NKPEILLLDESLSALDLKLRTEMQYELRELQKRLGITFIFVTHDQEEAlALSDYIFVMKDGEIQQFGTPTDIY 223
Cdd:TIGR04520 153 MRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEA-VLADRVIVMNKGKIVAEGTPREIF 224
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
 24-227 3.59e-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: 171.45  E-value: 3.59e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   24 NLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKN---QSIEK---LPANKRRVNTVFQDYALFPHLNVYENI 97
Cdd:TIGR02142  17 DFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlFDSRKgifLPPEKRRIGYVFQEARLFPHLSVRGNL 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   98 AFGLRLKKFSKQEIDKEvkealKLVKLTGYE---QRHIDEMSGGQKQRVAIARAIVNKPEILLLDESLSALDLKLRTEMQ 174
Cdd:TIGR02142  97 RYGMKRARPSERRISFE-----RVIELLGIGhllGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEIL 171

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 488386109  175 YELRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIYDEPV 227
Cdd:TIGR02142 172 PYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPD 224
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
 5-219 6.36e-50

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: 177.72  E-value: 6.36e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   5 LSFKKVTKKFDDTT--ILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANKRR--VNT 80
Cdd:COG2274  474 IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRrqIGV 553

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  81 VFQDYALFpHLNVYENIAFGlrlkkfsKQEI-DKEVKEALKLVKLT--------GYEQRhIDEM----SGGQKQRVAIAR 147
Cdd:COG2274  554 VLQDVFLF-SGTIRENITLG-------DPDAtDEEIIEAARLAGLHdfiealpmGYDTV-VGEGgsnlSGGQRQRLAIAR 624

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488386109 148 AIVNKPEILLLDESLSALDLKLRTEMQYELRELQKrlGITFIFVTHDqEEALALSDYIFVMKDGEIQQFGTP 219
Cdd:COG2274  625 ALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHR-LSTIRLADRIIVLDKGRIVEDGTH 693
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 20-160 6.95e-50

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: 164.36  E-value: 6.95e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   20 LNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANKRRVN--TVFQDYALFPHLNVYENI 97
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEigYVFQDPQLFPRLTVRENL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488386109   98 AFGLRLKKFSKQEIDKEVKEALKLVKLTGYEQRHID----EMSGGQKQRVAIARAIVNKPEILLLDE 160
Cdd:pfam00005  81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGerpgTLSGGQRQRVAIARALLTKPKLLLLDE 147
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
 4-226 7.15e-50

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: 169.85  E-value: 7.15e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   4 LLSFKKVTKKFD----DTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPN---EGQIIYKNQSIEKLPANK- 75
Cdd:COG0444    1 LLEVRNLKVYFPtrrgVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKLSEKEl 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  76 -----RRVNTVFQD-Y-ALFPHLNVYENIAFGLRL-KKFSKQEIDKEVKEALKLVKLTGYEQR-----HidEMSGGQKQR 142
Cdd:COG0444   81 rkirgREIQMIFQDpMtSLNPVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLPDPERRldrypH--ELSGGMRQR 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 143 VAIARAIVNKPEILLLDESLSALD-------LKLrtemqyeLRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQ 215
Cdd:COG0444  159 VMIARALALEPKLLIADEPTTALDvtiqaqiLNL-------LKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVE 231

                        250
                 ....*....|.
gi 488386109 216 FGTPTDIYDEP 226
Cdd:COG0444  232 EGPVEELFENP 242
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
 13-213 7.21e-50

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: 166.13  E-value: 7.21e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  13 KFDDTTIL---NNMNLD--IESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANKRRVNTVFQDYAL 87
Cdd:cd03298    2 RLDKIRFSygeQPMHFDltFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQENNL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  88 FPHLNVYENIAFG----LRLKKFSKQEIDKevkeALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDESLS 163
Cdd:cd03298   82 FAHLTVEQNVGLGlspgLKLTAEDRQAIEV----ALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFA 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 488386109 164 ALDLKLRTEMQYELRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEI 213
Cdd:cd03298  158 ALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...
 1-222 2.55e-49

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: 166.37  E-value: 2.55e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   1 MESLLSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANKR---- 76
Cdd:COG0411    1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIarlg 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  77 --RvnTvFQDYALFPHLNVYENIAFG-------------LRLKKFSKQE--IDKEVKEALKLVKLTGYEQRHIDEMSGGQ 139
Cdd:COG0411   81 iaR--T-FQNPRLFPELTVLENVLVAaharlgrgllaalLRLPRARREEreARERAEELLERVGLADRADEPAGNLSYGQ 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 140 KQRVAIARAIVNKPEILLLDESLSALDLKLRTEMQYELRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTP 219
Cdd:COG0411  158 QRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTP 237


                 ...
gi 488386109 220 TDI 222
Cdd:COG0411  238 AEV 240
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
1-248 3.02e-49

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


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 170.21  E-value: 3.02e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   1 MESLLSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLP------AN 74
Cdd:PRK10070  25 IEQGLSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISdaelreVR 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  75 KRRVNTVFQDYALFPHLNVYENIAFGLRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPE 154
Cdd:PRK10070 105 RKKIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPD 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 155 ILLLDESLSALDLKLRTEMQYELRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIYDEPVNRFVADF 234
Cdd:PRK10070 185 ILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTF 264

                        250
                 ....*....|....
gi 488386109 235 IGESNIVDGTMVKD 248
Cdd:PRK10070 265 FRGVDISQVFSAKD 278
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
 6-209 5.27e-49

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: 164.24  E-value: 5.27e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   6 SFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPankRRVNTVFQDY 85
Cdd:cd03235    1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKER---KRIGYVPQRR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  86 AL---FPhLNVYENIAFGLR-----LKKFSKQEIDKeVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILL 157
Cdd:cd03235   78 SIdrdFP-ISVRDVVLMGLYghkglFRRLSKADKAK-VDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLL 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488386109 158 LDESLSALDLKlrTEMQ-YE-LRELQkRLGITFIFVTHDQEEALALSDYIFVMK 209
Cdd:cd03235  156 LDEPFAGVDPK--TQEDiYElLRELR-REGMTILVVTHDLGLVLEYFDRVLLLN 206
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
 5-213 5.51e-49

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 165.62  E-value: 5.51e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   5 LSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANKRrvnTVFQD 84
Cdd:PRK11247  13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTR---LMFQD 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  85 YALFPHLNVYENIAFGLRLKkfskqeIDKEVKEALKLVkltGYEQRHID---EMSGGQKQRVAIARAIVNKPEILLLDES 161
Cdd:PRK11247  90 ARLLPWKKVIDNVGLGLKGQ------WRDAALQALAAV---GLADRANEwpaALSGGQKQRVALARALIHRPGLLLLDEP 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 488386109 162 LSALDLKLRTEMQYELRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEI 213
Cdd:PRK11247 161 LGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
 10-222 2.01e-48

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: 163.38  E-value: 2.01e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  10 VTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANKR------RvntVFQ 83
Cdd:cd03219    6 LTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIarlgigR---TFQ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  84 DYALFPHLNVYENIAFGLRLKK----------FSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKP 153
Cdd:cd03219   83 IPRLFPELTVLENVMVAAQARTgsglllararREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDP 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488386109 154 EILLLDESLSALDLKLRTEMQYELRELqKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDI 222
Cdd:cd03219  163 KLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEV 230
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
 5-219 3.32e-48

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: 162.29  E-value: 3.32e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   5 LSFKKVTKKF--DDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEK-LPANKRRVNTV 81
Cdd:cd03263    1 LQIRNLTKTYkkGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTdRKAARQSLGYC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  82 FQDYALFPHLNVYENIAFGLRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDES 161
Cdd:cd03263   81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 488386109 162 LSALDLKLRTEM-QYELRELQKRlgiTFIFVTHDQEEALALSDYIFVMKDGEIQQFGTP 219
Cdd:cd03263  161 TSGLDPASRRAIwDLILEVRKGR---SIILTTHSMDEAEALCDRIAIMSDGKLRCIGSP 216
ABC_phnC TIGR02315
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ...
 4-229 7.55e-48

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: 162.08  E-value: 7.55e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109    4 LLSFKKVTKKF-DDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANK-----RR 77
Cdd:TIGR02315   1 MLEVENLSKVYpNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKlrklrRR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   78 VNTVFQDYALFPHLNVYENIAFGlRL----------KKFSKQEIdKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIAR 147
Cdd:TIGR02315  81 IGMIFQHYNLIERLTVLENVLHG-RLgykptwrsllGRFSEEDK-ERALSALERVGLADKAYQRADQLSGGQQQRVAIAR 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  148 AIVNKPEILLLDESLSALDLKLRTEMQYELRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIYDEPV 227
Cdd:TIGR02315 159 ALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDDEVL 238


                  ..
gi 488386109  228 NR 229
Cdd:TIGR02315 239 RH 240
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
 6-212 8.35e-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: 158.95  E-value: 8.35e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   6 SFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLP--ANKRRVNTVFQ 83
Cdd:cd00267    1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPleELRRRIGYVPQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  84 dyalfphlnvyeniafglrlkkfskqeidkevkealklvkltgyeqrhideMSGGQKQRVAIARAIVNKPEILLLDESLS 163
Cdd:cd00267   81 ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 488386109 164 ALDLKLRTEMQYELRELQKRlGITFIFVTHDQEEALALSDYIFVMKDGE 212
Cdd:cd00267  110 GLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
 7-238 6.94e-47

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 162.66  E-value: 6.94e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   7 FKKVTKKFD----DTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPAN-----KRR 77
Cdd:PRK11153   4 LKNISKVFPqggrTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKelrkaRRQ 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  78 VNTVFQDYALFPHLNVYENIAFGLRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILL 157
Cdd:PRK11153  84 IGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLL 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 158 LDESLSALD-------LKLrtemqyeLRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIYDEPVNRF 230
Cdd:PRK11153 164 CDEATSALDpattrsiLEL-------LKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPL 236


                 ....*...
gi 488386109 231 VADFIGES 238
Cdd:PRK11153 237 TREFIQST 244
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
 35-226 8.88e-47

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


Pssm-ID: 443332 [Multi-domain]  Cd Length: 533  Bit Score: 166.40  E-value: 8.88e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  35 LLGPSGCGKTT----ILKLIagfeqPNEGQIIYKNQSIEKLPAN-----KRRVNTVFQD-YA-LFPHLNVYENIAFGLRL 103
Cdd:COG4172  317 LVGESGSGKSTlglaLLRLI-----PSEGEIRFDGQDLDGLSRRalrplRRRMQVVFQDpFGsLSPRMTVGQIIAEGLRV 391

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 104 --KKFSKQEIDKEVKEALKLVKLT-GYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDESLSALD-------LKLrtem 173
Cdd:COG4172  392 hgPGLSAAERRARVAEALEEVGLDpAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDvsvqaqiLDL---- 467

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 488386109 174 qyeLRELQKRLGITFIFVTHDqeeaL----ALSDYIFVMKDGEIQQFGTPTDIYDEP 226
Cdd:COG4172  468 ---LRDLQREHGLAYLFISHD----LavvrALAHRVMVMKDGKVVEQGPTEQVFDAP 517
thiQ TIGR01277
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ...
 24-217 2.55e-46

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: 157.33  E-value: 2.55e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   24 NLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANKRRVNTVFQDYALFPHLNVYENIAFGLR- 102
Cdd:TIGR01277  18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSMLFQENNLFAHLTVRQNIGLGLHp 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  103 -LKKFSKQEidKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDESLSALDLKLRTEMQYELRELQ 181
Cdd:TIGR01277  98 gLKLNAEQQ--EKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLC 175

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 488386109  182 KRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFG 217
Cdd:TIGR01277 176 SERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
CeuD COG4604
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ...
 8-227 4.86e-45

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: 4.86e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   8 KKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANK--RRVNTVFQDY 85
Cdd:COG4604    5 KNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRElaKRLAILRQEN 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  86 ALFPHLNVYENIAFGL------RLKKFSKQEIDkevkEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLD 159
Cdd:COG4604   85 HINSRLTVRELVAFGRfpyskgRLTAEDREIID----EAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLD 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488386109 160 ESLSALDLKLRTEMQYELRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIYDEPV 227
Cdd:COG4604  161 EPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIITPEV 228
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
 4-204 9.52e-45

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: 152.63  E-value: 9.52e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   4 LLSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPAN-KRRVNTVF 82
Cdd:COG4133    2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDyRRRLAYLG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  83 QDYALFPHLNVYENIAFGLRLKKFSKQEIDkeVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDESL 162
Cdd:COG4133   82 HADGLKPELTVRENLRFWAALYGLRADREA--IDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPF 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 488386109 163 SALDLKLRTEMQYELRELQKRLGItFIFVTHDQEEA-----LALSDY 204
Cdd:COG4133  160 TALDAAGVALLAELIAAHLARGGA-VLLTTHQPLELaaarvLDLGDF 205
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
5-221 1.12e-44

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 161.49  E-value: 1.12e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   5 LSFKKVTkkF---DDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANK--RRVN 79
Cdd:COG1132  340 IEFENVS--FsypGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESlrRQIG 417

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  80 TVFQDYALFpHLNVYENIAFGlrlkkfsKQEI-DKEVKEALKLVKLT--------GYEQRhIDE----MSGGQKQRVAIA 146
Cdd:COG1132  418 VVPQDTFLF-SGTIRENIRYG-------RPDAtDEEVEEAAKAAQAHefiealpdGYDTV-VGErgvnLSGGQRQRIAIA 488

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 147 RAIVNKPEILLLDESLSALDlkLRTEmqyelRELQKRL-----GITFIFVTHDqeealaLS-----DYIFVMKDGEIQQF 216
Cdd:COG1132  489 RALLKDPPILILDEATSALD--TETE-----ALIQEALerlmkGRTTIVIAHR------LStirnaDRILVLDDGRIVEQ 555


                 ....*
gi 488386109 217 GTPTD 221
Cdd:COG1132  556 GTHEE 560
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
 1-235 1.14e-44

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


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 154.04  E-value: 1.14e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   1 MESLLSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILK-------LIAGFEQpnEGQIIYKNQSI----E 69
Cdd:COG1117    8 LEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRclnrmndLIPGARV--EGEILLDGEDIydpdV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  70 KLPANKRRVNTVFQDYALFPHlNVYENIAFGLRLKKF-SKQEIDKEVKEALKLVKLTgyeqrhiDE-----------MSG 137
Cdd:COG1117   86 DVVELRRRVGMVFQKPNPFPK-SIYDNVAYGLRLHGIkSKSELDEIVEESLRKAALW-------DEvkdrlkksalgLSG 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 138 GQKQRVAIARAIVNKPEILLLDESLSALD----LKLrtEmqyEL-RELQKRLgiTFIFVTHDQEEALALSDYIFVMKDGE 212
Cdd:COG1117  158 GQQQRLCIARALAVEPEVLLMDEPTSALDpistAKI--E---ELiLELKKDY--TIVIVTHNMQQAARVSDYTAFFYLGE 230

                        250       260
                 ....*....|....*....|...
gi 488386109 213 IQQFGTPTDIYDEPVNRFVADFI 235
Cdd:COG1117  231 LVEFGPTEQIFTNPKDKRTEDYI 253
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
 5-217 2.86e-44

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: 151.58  E-value: 2.86e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   5 LSFKKVTKKFDDTTILNNMNLDIESGyFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANKRR-VNTVFQ 83
Cdd:cd03264    1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRrIGYLPQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  84 DYALFPHLNVYENIAFGLRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDESLS 163
Cdd:cd03264   80 EFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 488386109 164 ALDLKLRTemqyELRELQKRLG--ITFIFVTHDQEEALALSDYIFVMKDGEIQQFG 217
Cdd:cd03264  160 GLDPEERI----RFRNLLSELGedRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
24-240 3.98e-44

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 152.04  E-value: 3.98e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  24 NLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANKRRVNTVFQDYALFPHLNVYENIAFGLR- 102
Cdd:PRK10771  19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQENNLFSHLTVAQNIGLGLNp 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 103 -LKKFSKQEidKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDESLSALDLKLRTEMQYELRELQ 181
Cdd:PRK10771  99 gLKLNAAQR--EKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVC 176

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 488386109 182 KRLGITFIFVTHDQEEALALSDYIFVMKDGEIqqfgtptdIYDEPVNRFVADFIGESNI 240
Cdd:PRK10771 177 QERQLTLLMVSHSLEDAARIAPRSLVVADGRI--------AWDGPTDELLSGKASASAL 227
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
 5-212 7.97e-44

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: 149.07  E-value: 7.97e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   5 LSFKKVTKKFDDTT--ILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANKRR--VNT 80
Cdd:cd03228    1 IEFKNVSFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRknIAY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  81 VFQDYALFpHLNVYENIafglrlkkfskqeidkevkealklvkltgyeqrhideMSGGQKQRVAIARAIVNKPEILLLDE 160
Cdd:cd03228   81 VPQDPFLF-SGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDE 122

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 488386109 161 SLSALDLKLRTEMQYELRELQKrlGITFIFVTHDqEEALALSDYIFVMKDGE 212
Cdd:cd03228  123 ATSALDPETEALILEALRALAK--GKTVIVIAHR-LSTIRDADRIIVLDDGR 171
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
 20-226 8.41e-44

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


Pssm-ID: 443658 [Multi-domain]  Cd Length: 329  Bit Score: 154.12  E-value: 8.41e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  20 LNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANK-----RRVNTVFQD-YA-LFPHLN 92
Cdd:COG4608   34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRElrplrRRMQMVFQDpYAsLNPRMT 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  93 VYENIAFGLRL-KKFSKQEIDKEVKEALKLVkltGYEQRHID----EMSGGQKQRVAIARAIVNKPEILLLDESLSALD- 166
Cdd:COG4608  114 VGDIIAEPLRIhGLASKAERRERVAELLELV---GLRPEHADryphEFSGGQRQRIGIARALALNPKLIVCDEPVSALDv 190

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 167 ------LKLrtemqyeLRELQKRLGITFIFVTHDqeeaLA----LSDYIFVMKDGEIQQFGTPTDIYDEP 226
Cdd:COG4608  191 siqaqvLNL-------LEDLQDELGLTYLFISHD----LSvvrhISDRVAVMYLGKIVEIAPRDELYARP 249
cbiO PRK13637
energy-coupling factor transporter ATPase;
16-225 2.03e-43

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 151.74  E-value: 2.03e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  16 DTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIE----KLPANKRRVNTVFQ--DYALFP 89
Cdd:PRK13637  19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkkvKLSDIRKKVGLVFQypEYQLFE 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  90 HlNVYENIAFGLRLKKFSKQEIDKEVKEALKLVKLT--GYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDESLSALDL 167
Cdd:PRK13637  99 E-TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDP 177

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 488386109 168 KLRTEMQYELRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIYDE 225
Cdd:PRK13637 178 KGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKE 235
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
 8-222 3.94e-43

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: 149.06  E-value: 3.94e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   8 KKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPAN-KRRVNTVFQDYA 86
Cdd:cd03265    4 ENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREvRRRIGIVFQDLS 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  87 LFPHLNVYENIAFGLRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDESLSALD 166
Cdd:cd03265   84 VDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLD 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 488386109 167 LKLRTEMQYELRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDI 222
Cdd:cd03265  164 PQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
35-229 6.35e-43

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 152.34  E-value: 6.35e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  35 LLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQ---SIEK---LPANKRRVNTVFQDYALFPHLNVYENIAFGLrlKKFSK 108
Cdd:PRK11144  29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAEKgicLPPEKRRIGYVFQDARLFPHYKVRGNLRYGM--AKSMV 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 109 QEIDKevkealkLVKLTGYE---QRHIDEMSGGQKQRVAIARAIVNKPEILLLDESLSALDLKLRTE-MQYeLRELQKRL 184
Cdd:PRK11144 107 AQFDK-------IVALLGIEpllDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRElLPY-LERLAREI 178

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 488386109 185 GITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIYDEPVNR 229
Cdd:PRK11144 179 NIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSAMR 223
nickel_nikE TIGR02769
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ...
 3-213 8.95e-43

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: 149.57  E-value: 8.95e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109    3 SLLSFKKVTKKFDDT---------TILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPA 73
Cdd:TIGR02769   1 SLLEVRDVTHTYRTGglfgakqraPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   74 NKRR-----VNTVFQDY--ALFPHLNVYENIAFGLR-LKKFSKQEIDKEVKEALKLVKL-TGYEQRHIDEMSGGQKQRVA 144
Cdd:TIGR02769  81 KQRRafrrdVQLVFQDSpsAVNPRMTVRQIIGEPLRhLTSLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRIN 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488386109  145 IARAIVNKPEILLLDESLSALDLKLRTEMQYELRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEI 213
Cdd:TIGR02769 161 IARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
5-218 1.71e-42

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


Pssm-ID: 443326 [Multi-domain]  Cd Length: 242  Bit Score: 148.24  E-value: 1.71e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   5 LSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQ--------SIEKLPANKR 76
Cdd:COG4161    3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfdfsqkpSEKAIRLLRQ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  77 RVNTVFQDYALFPHLNVYEN-IAFGLRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEI 155
Cdd:COG4161   83 KVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQV 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488386109 156 LLLDESLSALDLKLRTEMQYELRELQKrLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGT 218
Cdd:COG4161  163 LLFDEPTAALDPEITAQVVEIIRELSQ-TGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD 224
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
 2-224 1.08e-41

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 146.82  E-value: 1.08e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   2 ESLLSFKKVTKKF--DDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSI--EKLPANKRR 77
Cdd:PRK13648   5 NSIIVFKNVSFQYqsDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAItdDNFEKLRKH 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  78 VNTVFQD-YALFPHLNVYENIAFGLRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEIL 156
Cdd:PRK13648  85 IGIVFQNpDNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVI 164

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488386109 157 LLDESLSALDLKLRTEMQYELRELQKRLGITFIFVTHDQEEALAlSDYIFVMKDGEIQQFGTPTDIYD 224
Cdd:PRK13648 165 ILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFD 231
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
 3-236 1.74e-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: 1.74e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   3 SLLSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQI------IYKNQSIEKLPANKR 76
Cdd:PRK11264   2 SAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgditIDTARSLSQQKGLIR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  77 R----VNTVFQDYALFPHLNVYENIAFG-LRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVN 151
Cdd:PRK11264  82 QlrqhVGFVFQNFNLFPHRTVLENIIEGpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAM 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 152 KPEILLLDESLSALDLKLRTEMQYELREL--QKRlgiTFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIYDEP--- 226
Cdd:PRK11264 162 RPEVILFDEPTSALDPELVGEVLNTIRQLaqEKR---TMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPqqp 238

                        250
                 ....*....|.
gi 488386109 227 -VNRFVADFIG 236
Cdd:PRK11264 239 rTRQFLEKFLL 249
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
1-213 1.89e-41

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 151.32  E-value: 1.89e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   1 MESLLSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLP---ANKRR 77
Cdd:COG1129    1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSprdAQAAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  78 VNTVFQDYALFPHLNVYENIAFGLRLKKF---SKQEIDKEVKEALKLVKLtgyeqrHID------EMSGGQKQRVAIARA 148
Cdd:COG1129   81 IAIIHQELNLVPNLSVAENIFLGREPRRGgliDWRAMRRRARELLARLGL------DIDpdtpvgDLSVAQQQLVEIARA 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488386109 149 IVNKPEILLLDESLSALDLKlRTEMQYEL-RELQKRlGITFIFVTHDQEEALALSDYIFVMKDGEI 213
Cdd:COG1129  155 LSRDARVLILDEPTASLTER-EVERLFRIiRRLKAQ-GVAIIYISHRLDEVFEIADRVTVLRDGRL 218
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
 16-221 3.00e-41

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: 144.60  E-value: 3.00e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  16 DTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANKRR--VNTVFQDYALFPhLNV 93
Cdd:cd03249   15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRsqIGLVSQEPVLFD-GTI 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  94 YENIAFGlrlkKFSkqEIDKEVKEALKLVKLT--------GYEQR---HIDEMSGGQKQRVAIARAIVNKPEILLLDESL 162
Cdd:cd03249   94 AENIRYG----KPD--ATDEEVEEAAKKANIHdfimslpdGYDTLvgeRGSQLSGGQKQRIAIARALLRNPKILLLDEAT 167

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488386109 163 SALDLKLRTEMQYELRELqkRLGITFIFVTHdqeealALS-----DYIFVMKDGEIQQFGTPTD 221
Cdd:cd03249  168 SALDAESEKLVQEALDRA--MKGRTTIVIAH------RLStirnaDLIAVLQNGQVVEQGTHDE 223
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
 5-218 6.31e-41

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 144.00  E-value: 6.31e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   5 LSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQS--IEKLPANK------R 76
Cdd:PRK11124   3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHfdFSKTPSDKairelrR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  77 RVNTVFQDYALFPHLNVYEN-IAFGLRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEI 155
Cdd:PRK11124  83 NVGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQV 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488386109 156 LLLDESLSALDLKLRTEMQYELRELQKrLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGT 218
Cdd:PRK11124 163 LLFDEPTAALDPEITAQIVSIIRELAE-TGITQVIVTHEVEVARKTASRVVYMENGHIVEQGD 224
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
18-229 6.89e-41

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 144.83  E-value: 6.89e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  18 TILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLP-----ANKRRVNTVFQDY--ALFPH 90
Cdd:PRK10419  26 TVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqrkAFRRDIQMVFQDSisAVNPR 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  91 LNVYENIAFGLR-LKKFSKQEIDKEVKEALKLVKLT-GYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDESLSALDLK 168
Cdd:PRK10419 106 KTVREIIREPLRhLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLV 185

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488386109 169 LRTEMQYELRELQKRLGITFIFVTHDqeeaLALSDY----IFVMKDGEI--QQFGTPTDIYDEPVNR 229
Cdd:PRK10419 186 LQAGVIRLLKKLQQQFGTACLFITHD----LRLVERfcqrVMVMDNGQIveTQPVGDKLTFSSPAGR 248
cbiO PRK13650
energy-coupling factor transporter ATPase;
1-223 8.94e-41

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 144.87  E-value: 8.94e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   1 MESLLSFKKVTKKFDDTT---ILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQ--SIEKLPANK 75
Cdd:PRK13650   1 MSNIIEVKNLTFKYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDllTEENVWDIR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  76 RRVNTVFQDY-ALFPHLNVYENIAFGLRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPE 154
Cdd:PRK13650  81 HKIGMVFQNPdNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPK 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488386109 155 ILLLDESLSALDLKLRTEMQYELRELQKRLGITFIFVTHDQEEaLALSDYIFVMKDGEIQQFGTPTDIY 223
Cdd:PRK13650 161 IIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDE-VALSDRVLVMKNGQVESTSTPRELF 228
SapF COG4167
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
1-226 1.54e-40

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


Pssm-ID: 443328 [Multi-domain]  Cd Length: 265  Bit Score: 143.82  E-value: 1.54e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   1 MESLLSFKKVTKKFDDTT---------ILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKL 71
Cdd:COG4167    1 MSALLEVRNLSKTFKYRTglfrrqqfeAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  72 PANKR--RVNTVFQD--YALFPHLNVYENIAFGLRLK-KFSKQEIDKEVKEALKLVKLTG-YEQRHIDEMSGGQKQRVAI 145
Cdd:COG4167   81 DYKYRckHIRMIFQDpnTSLNPRLNIGQILEEPLRLNtDLTAEEREERIFATLRLVGLLPeHANFYPHMLSSGQKQRVAL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 146 ARAIVNKPEILLLDESLSALDLKLRTEMQYELRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIYDE 225
Cdd:COG4167  161 ARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVFAN 240


                 .
gi 488386109 226 P 226
Cdd:COG4167  241 P 241
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
 15-226 1.66e-40

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 144.06  E-value: 1.66e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  15 DDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIE----KLPANKRRVNTVFQ--DYALF 88
Cdd:PRK13639  13 DGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydkkSLLEVRKTVGIVFQnpDDQLF 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  89 PHlNVYENIAFGLRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDESLSALDLK 168
Cdd:PRK13639  93 AP-TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPM 171

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 488386109 169 LRTEMQYELRELQKRlGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIYDEP 226
Cdd:PRK13639 172 GASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDI 228
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
 5-224 3.40e-40

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: 141.98  E-value: 3.40e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   5 LSFKKVTKKF--DDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIE--KLPANKRRVNT 80
Cdd:cd03251    1 VEFKNVTFRYpgDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRdyTLASLRRQIGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  81 VFQDYALFpHLNVYENIAFGLRlkkfskQEIDKEVKEALKLVKLT--------GYEQRhIDE----MSGGQKQRVAIARA 148
Cdd:cd03251   81 VSQDVFLF-NDTVAENIAYGRP------GATREEVEEAARAANAHefimelpeGYDTV-IGErgvkLSGGQRQRIAIARA 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 149 IVNKPEILLLDESLSALDLKLRTEMQYELRELQKrlGITFIFVTHdqeealALS-----DYIFVMKDGEIQQFGTPTDIY 223
Cdd:cd03251  153 LLKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAH------RLStienaDRIVVLEDGKIVERGTHEELL 224


                 .
gi 488386109 224 D 224
Cdd:cd03251  225 A 225
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
 5-221 3.53e-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: 149.14  E-value: 3.53e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   5 LSFKKVTKKFDD-TTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPAN--KRRVNTV 81
Cdd:COG4988  337 IELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPAswRRQIAWV 416

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  82 FQDYALFpHLNVYENIAFGlrlkkfsKQEI-DKEVKEALKLVKLT--------GYEQRhIDE----MSGGQKQRVAIARA 148
Cdd:COG4988  417 PQNPYLF-AGTIRENLRLG-------RPDAsDEELEAALEAAGLDefvaalpdGLDTP-LGEggrgLSGGQAQRLALARA 487

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488386109 149 IVNKPEILLLDESLSALDLKLRTEMQYELRELQKrlGITFIFVTHDqEEALALSDYIFVMKDGEIQQFGTPTD 221
Cdd:COG4988  488 LLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHR-LALLAQADRILVLDDGRIVEQGTHEE 557
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
 2-222 4.64e-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: 141.76  E-value: 4.64e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   2 ESLLSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQII------YKNQSIEKLpanK 75
Cdd:COG1119    1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVrlfgerRGGEDVWEL---R 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  76 RR---VNTVFQDYaLFPHLNVYENIAFGL-----RLKKFSKQEIDKeVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIAR 147
Cdd:COG1119   78 KRiglVSPALQLR-FPRDETVLDVVLSGFfdsigLYREPTDEQRER-ARELLELLGLAHLADRPFGTLSQGEQRRVLIAR 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488386109 148 AIVNKPEILLLDESLSALDLKLRTEMQYELRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDI 222
Cdd:COG1119  156 ALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEV 230
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
1-223 4.90e-40

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 142.85  E-value: 4.90e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   1 MESLLSFKKVTKKFDDTT--ILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQ--SIEKLPANKR 76
Cdd:PRK13635   2 KEEIIRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMvlSEETVWDVRR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  77 RVNTVFQDY-ALFPHLNVYENIAFGLRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEI 155
Cdd:PRK13635  82 QVGMVFQNPdNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDI 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488386109 156 LLLDESLSALDLKLRTEMQYELRELQKRLGITFIFVTHDQEEAlALSDYIFVMKDGEIQQFGTPTDIY 223
Cdd:PRK13635 162 IILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEA-AQADRVIVMNKGEILEEGTPEEIF 228
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
 10-213 5.15e-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: 137.73  E-value: 5.15e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  10 VTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANKRRVNTVFQDYALFP 89
Cdd:cd03268    6 LTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIEAPGFYP 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  90 HLNVYENIAFGLRLKKFSKQEIDkevkEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDESLSALDLKL 169
Cdd:cd03268   86 NLTARENLRLLARLLGIRKKRID----EVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDG 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 488386109 170 RTEMQYELRELQKRlGITFIFVTHDQEEALALSDYIFVMKDGEI 213
Cdd:cd03268  162 IKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKL 204
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
 2-225 5.71e-39

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 139.74  E-value: 5.71e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   2 ESLLSFKKVTKKFDDTT--ILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQI-IYKNQ-SIEKLPANKRR 77
Cdd:PRK13632   5 SVMIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIkIDGITiSKENLKEIRKK 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  78 VNTVFQDY-ALFPHLNVYENIAFGLRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEIL 156
Cdd:PRK13632  85 IGIIFQNPdNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEII 164

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488386109 157 LLDESLSALDLKLRTEMQYELRELQKRLGITFIFVTHDQEEALaLSDYIFVMKDGEIQQFGTPTDIYDE 225
Cdd:PRK13632 165 IFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEILNN 232
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
 5-217 6.93e-39

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: 137.80  E-value: 6.93e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   5 LSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEklPANKRRVNTVFQD 84
Cdd:cd03269    1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD--IAARNRIGYLPEE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  85 YALFPHLNVYENIAFGLRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDESLSA 164
Cdd:cd03269   79 RGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSG 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 488386109 165 LDLKLRTEMQYELRELqKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFG 217
Cdd:cd03269  159 LDPVNVELLKDVIREL-ARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
 5-229 1.17e-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: 137.67  E-value: 1.17e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   5 LSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANKR-RVNTVF- 82
Cdd:cd03218    1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRaRLGIGYl 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  83 -QDYALFPHLNVYENIAFGLRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDES 161
Cdd:cd03218   81 pQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488386109 162 LSALDLKLRTEMQYELRELQKRlGITfIFVT-HDQEEALALSDYIFVMKDGEIQQFGTPTDIYDEPVNR 229
Cdd:cd03218  161 FAGVDPIAVQDIQKIIKILKDR-GIG-VLITdHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVR 227
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
 3-226 4.47e-38

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 136.97  E-value: 4.47e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   3 SLLSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILK----LIAGFEQPN-EGQIIYKNQSIEKLPAN--K 75
Cdd:PRK14247   2 NKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRvfnrLIELYPEARvSGEVYLDGQDIFKMDVIelR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  76 RRVNTVFQDYALFPHLNVYENIAFGLRLKKF--SKQEIDKEVKEALKLVKLTGYEQRHID----EMSGGQKQRVAIARAI 149
Cdd:PRK14247  82 RRVQMVFQIPNPIPNLSIFENVALGLKLNRLvkSKKELQERVRWALEKAQLWDEVKDRLDapagKLSGGQQQRLCIARAL 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488386109 150 VNKPEILLLDESLSALDLKLRTEMQYELRELQKRLgiTFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIYDEP 226
Cdd:PRK14247 162 AFQPEVLLADEPTANLDPENTAKIESLFLELKKDM--TIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNP 236
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 5-213 6.77e-38

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


Pssm-ID: 440718 [Multi-domain]  Cd Length: 264  Bit Score: 136.75  E-value: 6.77e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   5 LSFKKVTKKF-----DDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANKR--R 77
Cdd:COG1101    2 LELKNLSKTFnpgtvNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRakY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  78 VNTVFQDYAL--FPHLNVYENIA--------FGLRLKKfSKQEIDkEVKEALKLVKLtGYEQRHIDEM---SGGQKQRVA 144
Cdd:COG1101   82 IGRVFQDPMMgtAPSMTIEENLAlayrrgkrRGLRRGL-TKKRRE-LFRELLATLGL-GLENRLDTKVgllSGGQRQALS 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 145 IARAIVNKPEILLLDESLSALDLKlRTEMQYEL-RELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEI 213
Cdd:COG1101  159 LLMATLTKPKLLLLDEHTAALDPK-TAALVLELtEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRI 227
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
3-215 7.26e-38

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 135.71  E-value: 7.26e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   3 SLLSFKKVTKKFDD----TTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPA----- 73
Cdd:PRK11629   4 ILLQCDNLCKRYQEgsvqTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSaakae 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  74 -NKRRVNTVFQDYALFPHLNVYENIAFGLRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNK 152
Cdd:PRK11629  84 lRNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNN 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488386109 153 PEILLLDESLSALDLKLRTEMQYELRELQKRLGITFIFVTHDQEEALALSDYIfVMKDGEIQQ 215
Cdd:PRK11629 164 PRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQL-EMRDGRLTA 225
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
 5-222 7.82e-38

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: 135.25  E-value: 7.82e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   5 LSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANKR-R--VNTV 81
Cdd:cd03224    1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERaRagIGYV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  82 FQDYALFPHLNVYENIAFGLRLKKfsKQEIDKEVKEALKLV-KLtgYEQRH--IDEMSGGQKQRVAIARAIVNKPEILLL 158
Cdd:cd03224   81 PEGRRIFPELTVEENLLLGAYARR--RAKRKARLERVYELFpRL--KERRKqlAGTLSGGEQQMLAIARALMSRPKLLLL 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488386109 159 DESLSALDLKLRTEMQYELRELqKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDI 222
Cdd:cd03224  157 DEPSEGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 5-213 9.23e-38

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


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 137.16  E-value: 9.23e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   5 LSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEklPANKRRVNtvfqd 84
Cdd:COG4152    2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD--PEDRRRIG----- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  85 Y-----ALFPHLNVYENIAFGLRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLD 159
Cdd:COG4152   75 YlpeerGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILD 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488386109 160 ESLSALDLKLRTEMQYELRELQKRlGITFIFVTHDQEEALALSDYIFVMKDGEI 213
Cdd:COG4152  155 EPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRK 207
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
 20-226 2.72e-37

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 135.92  E-value: 2.72e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  20 LNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIE------KLPANKRRVNTVFQdyalFPHLNV 93
Cdd:PRK13634  23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkknkKLKPLRKKVGIVFQ----FPEHQL 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  94 YE-----NIAFGLRLKKFSKQEIDKEVKEALKLVKLT-GYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDESLSALDL 167
Cdd:PRK13634  99 FEetvekDICFGPMNFGVSEEDAKQKAREMIELVGLPeELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDP 178

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 488386109 168 KLRTEMQYELRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIYDEP 226
Cdd:PRK13634 179 KGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP 237
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
 2-220 5.26e-37

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: 133.33  E-value: 5.26e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   2 ESLLSFKKVTKKFDDT----TILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANKR- 76
Cdd:COG4181    6 APIIELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARa 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  77 -----RVNTVFQDYALFPHLNVYENIAFGLRLKkfSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVN 151
Cdd:COG4181   86 rlrarHVGFVFQSFQLLPTLTALENVMLPLELA--GRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFAT 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488386109 152 KPEILLLDESLSALDLKLRTEMQYELRELQKRLGITFIFVTHDQEEAlALSDYIFVMKDGEIQQFGTPT 220
Cdd:COG4181  164 EPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALA-ARCDRVLRLRAGRLVEDTAAT 231
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
 7-213 2.39e-36

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: 131.17  E-value: 2.39e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   7 FKKVTKKFDDTTI--LNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKL-PANKRR-VNTVF 82
Cdd:cd03245    5 FRNVSFSYPNQEIpaLDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLdPADLRRnIGYVP 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  83 QDYALFpHLNVYENIAFGLRLKKfskqeiDKEVKEALKLVKLTGYEQRH-------IDE----MSGGQKQRVAIARAIVN 151
Cdd:cd03245   85 QDVTLF-YGTLRDNITLGAPLAD------DERILRAAELAGVTDFVNKHpngldlqIGErgrgLSGGQRQAVALARALLN 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488386109 152 KPEILLLDESLSALDlkLRTEMQY--ELRELQKrlGITFIFVTHDQeEALALSDYIFVMKDGEI 213
Cdd:cd03245  158 DPPILLLDEPTSAMD--MNSEERLkeRLRQLLG--DKTLIIITHRP-SLLDLVDRIIVMDSGRI 216
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
1-243 2.71e-36

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 132.58  E-value: 2.71e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   1 MESLLSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSI-----EKLPANK 75
Cdd:PRK11831   4 VANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamsrSRLYTVR 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  76 RRVNTVFQDYALFPHLNVYENIAFGLR-LKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPE 154
Cdd:PRK11831  84 KRMSMLFQSGALFTDMNVFDNVAYPLReHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPD 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 155 ILLLDESLSALD-------LKLrtemqyeLRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIYDEPV 227
Cdd:PRK11831 164 LIMFDEPFVGQDpitmgvlVKL-------ISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPD 236

                        250
                 ....*....|....*.
gi 488386109 228 NRfVADFIgeSNIVDG 243
Cdd:PRK11831 237 PR-VRQFL--DGIADG 249
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
 5-219 6.73e-36

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: 130.43  E-value: 6.73e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   5 LSFKKVTKKFDDT-TILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEK--LPANKRRVNTV 81
Cdd:cd03253    1 IEFENVTFAYDPGrPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREvtLDSLRRAIGVV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  82 FQDYALFpHLNVYENIAFGlRLKKfSKQEIDKEVKEAL---KLVKLT-GYEQRhIDE----MSGGQKQRVAIARAIVNKP 153
Cdd:cd03253   81 PQDTVLF-NDTIGYNIRYG-RPDA-TDEEVIEAAKAAQihdKIMRFPdGYDTI-VGErglkLSGGEKQRVAIARAILKNP 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488386109 154 EILLLDESLSALDLKLRTEMQYELRELQKrlGITFIFVTHDQEEALAlSDYIFVMKDGEIQQFGTP 219
Cdd:cd03253  157 PILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTH 219
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
 5-213 1.02e-35

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: 127.93  E-value: 1.02e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   5 LSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKL-P--ANKRRVNTV 81
Cdd:cd03216    1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFAsPrdARRAGIAMV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  82 FQdyalfphlnvyeniafglrlkkfskqeidkevkealklvkltgyeqrhideMSGGQKQRVAIARAIVNKPEILLLDES 161
Cdd:cd03216   81 YQ---------------------------------------------------LSVGERQMVEIARALARNARLLILDEP 109

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 488386109 162 LSALDLKLRTEMQYELRELQKRlGITFIFVTHDQEEALALSDYIFVMKDGEI 213
Cdd:cd03216  110 TAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRV 160
cbiO PRK13640
energy-coupling factor transporter ATPase;
2-227 1.06e-35

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 131.46  E-value: 1.06e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   2 ESLLSFKKVTKKFDDT--TILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPAN----- 74
Cdd:PRK13640   3 DNIVEFKHVSFTYPDSkkPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLTAKtvwdi 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  75 KRRVNTVFQDY-ALFPHLNVYENIAFGLRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKP 153
Cdd:PRK13640  83 REKVGIVFQNPdNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEP 162

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488386109 154 EILLLDESLSALDLKLRTEMQYELRELQKRLGITFIFVTHDQEEAlALSDYIFVMKDGEIQQFGTPTDIYDEPV 227
Cdd:PRK13640 163 KIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKVE 235
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
1-224 2.21e-35

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 131.08  E-value: 2.21e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   1 MESLLSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSI-EKLPANKRRVN 79
Cdd:PRK13537   4 SVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVpSRARHARQRVG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  80 TVFQDYALFPHLNVYENIAFGLRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLD 159
Cdd:PRK13537  84 VVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLD 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488386109 160 ESLSALDLKLRTEMQYELRELQKRlGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIYD 224
Cdd:PRK13537 164 EPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIE 227
COG4559 COG4559
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
18-221 2.88e-35

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


Pssm-ID: 443620 [Multi-domain]  Cd Length: 258  Bit Score: 129.47  E-value: 2.88e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  18 TILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPAN---KRRvnTVF-QDYAL-FPhLN 92
Cdd:COG4559   15 TLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWelaRRR--AVLpQHSSLaFP-FT 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  93 VYENIAFGLRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIV-------NKPEILLLDESLSAL 165
Cdd:COG4559   92 VEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdGGPRWLFLDEPTSAL 171

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 488386109 166 DLKLrtemQYELRELQKRL---GITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTD 221
Cdd:COG4559  172 DLAH----QHAVLRLARQLarrGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEE 226
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
 15-213 5.59e-35

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


Pssm-ID: 213193 [Multi-domain]  Cd Length: 205  Bit Score: 127.37  E-value: 5.59e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  15 DDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIeKLPANKRRVNTVFQD--YALFPHlN 92
Cdd:cd03226   11 KGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI-KAKERRKSIGYVMQDvdYQLFTD-S 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  93 VYENIAFGLRLKKFSKQEIDkevkEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDESLSALDLKLRTE 172
Cdd:cd03226   89 VREELLLGLKELDAGNEQAE----TVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMER 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 488386109 173 MQYELRELQKRlGITFIFVTHDQEEALALSDYIFVMKDGEI 213
Cdd:cd03226  165 VGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAI 204
urea_trans_UrtE TIGR03410
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ...
 5-232 9.87e-35

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: 127.26  E-value: 9.87e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109    5 LSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANKRR---VNTV 81
Cdd:TIGR03410   1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERAragIAYV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   82 FQDYALFPHLNVYENIAFGLRLKKFSKQEIDKEVKE---ALKLVKltgyeQRHIDEMSGGQKQRVAIARAIVNKPEILLL 158
Cdd:TIGR03410  81 PQGREIFPRLTVEENLLTGLAALPRRSRKIPDEIYElfpVLKEML-----GRRGGDLSGGQQQQLAIARALVTRPKLLLL 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488386109  159 DESLSALDLKLRTEMQYELRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIYDEPVNRFVA 232
Cdd:TIGR03410 156 DEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDELDEDKVRRYLA 229
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
 4-221 1.14e-34

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 127.97  E-value: 1.14e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   4 LLSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANK--RRVNTV 81
Cdd:PRK13548   2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElaRRRAVL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  82 FQDYAL-FPhLNVYENIAFGLRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIV------NKPE 154
Cdd:PRK13548  82 PQHSSLsFP-FTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPR 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488386109 155 ILLLDESLSALDLK-----LRTemqyeLRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTD 221
Cdd:PRK13548 161 WLLLDEPTSALDLAhqhhvLRL-----ARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAE 227
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
 14-235 1.65e-34

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 127.85  E-value: 1.65e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  14 FDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGF-----EQPNEGQIIYKNQSIEKLPAN----KRRVNTVFQD 84
Cdd:PRK14258  17 YDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMnelesEVRVEGRVEFFNQNIYERRVNlnrlRRQVSMVHPK 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  85 YALFPhLNVYENIAFGLRLKKF-SKQEIDKEVKEALKLVKLTGYEQRHID----EMSGGQKQRVAIARAIVNKPEILLLD 159
Cdd:PRK14258  97 PNLFP-MSVYDNVAYGVKIVGWrPKLEIDDIVESALKDADLWDEIKHKIHksalDLSGGQQQRLCIARALAVKPKVLLMD 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 160 ESLSALDLKLRTEMQYELRELQKRLGITFIFVTHDQEEALALSDYIFVMKD-----GEIQQFGTPTDIYDEPVNRFVADF 234
Cdd:PRK14258 176 EPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIFNSPHDSRTREY 255


                 .
gi 488386109 235 I 235
Cdd:PRK14258 256 V 256
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
 7-219 2.03e-34

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: 126.57  E-value: 2.03e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   7 FKKVTKKFDDTT-ILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPAN--KRRVNTVFQ 83
Cdd:cd03254    5 FENVNFSYDEKKpVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKslRSMIGVVLQ 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  84 DYALFPHlNVYENIafglrlkKFSKQEI-DKEVKEALKLVKLT--------GYEQrHIDE----MSGGQKQRVAIARAIV 150
Cdd:cd03254   85 DTFLFSG-TIMENI-------RLGRPNAtDEEVIEAAKEAGAHdfimklpnGYDT-VLGEnggnLSQGERQLLAIARAML 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488386109 151 NKPEILLLDESLSALDLKLRTEMQYELRELQKrlGITFIFVTHdqeealALS-----DYIFVMKDGEIQQFGTP 219
Cdd:cd03254  156 RDPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAH------RLStiknaDKILVLDDGKIIEEGTH 221
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
 1-226 2.25e-34

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: 132.50  E-value: 2.25e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   1 MESLLSFKKVTKKFDD----TTILNNMNLDIESGYFYTLLGPSGCGKT----TILKLIAGFEQPNEGQIIYKNQSIEKLP 72
Cdd:COG4172    3 SMPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  73 ANK------RRVNTVFQD--YALFPHLNVYENIAFGLRL-KKFSKQEIDKEVKEALKLVKLTGYEQR-----HidEMSGG 138
Cdd:COG4172   83 ERElrrirgNRIAMIFQEpmTSLNPLHTIGKQIAEVLRLhRGLSGAAARARALELLERVGIPDPERRldaypH--QLSGG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 139 QKQRVAIARAIVNKPEILLLDESLSALDLKLRTEMQYELRELQKRLGITFIFVTHDqeeaLAL----SDYIFVMKDGEIQ 214
Cdd:COG4172  161 QRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHD----LGVvrrfADRVAVMRQGEIV 236

                        250
                 ....*....|..
gi 488386109 215 QFGTPTDIYDEP 226
Cdd:COG4172  237 EQGPTAELFAAP 248
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
 1-212 5.23e-34

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 131.30  E-value: 5.23e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   1 MESLLSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIE-KLP--ANKRR 77
Cdd:COG3845    2 MPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRiRSPrdAIALG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  78 VNTVFQDYALFPHLNVYENIAFGLRLKKFSKQEIDKEVKEALKLVKLTGYE---QRHIDEMSGGQKQRVAIARAIVNKPE 154
Cdd:COG3845   82 IGMVHQHFMLVPNLTVAENIVLGLEPTKGGRLDRKAARARIRELSERYGLDvdpDAKVEDLSVGEQQRVEILKALYRGAR 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488386109 155 ILLLDESLSAL------DLkLRTemqyeLRELqKRLGITFIFVTHDQEEALALSDYIFVMKDGE 212
Cdd:COG3845  162 ILILDEPTAVLtpqeadEL-FEI-----LRRL-AAEGKSIIFITHKLREVMAIADRVTVLRRGK 218
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
 10-213 7.00e-34

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: 124.79  E-value: 7.00e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  10 VTKKFDDTT----ILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPAN-KRRVNTVFQD 84
Cdd:cd03266    7 LTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEaRRRLGFVSDS 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  85 YALFPHLNVYENIAFGLRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDESLSA 164
Cdd:cd03266   87 TGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTG 166

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 488386109 165 LDLKLRTEMQYELRELqKRLGITFIFVTHDQEEALALSDYIFVMKDGEI 213
Cdd:cd03266  167 LDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRV 214
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
1-225 7.90e-34

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 126.36  E-value: 7.90e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   1 MESLLSFKKVTKKFDD------TTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKN---QSIEKL 71
Cdd:PRK13633   1 MNEMIKCKNVSYKYESneesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtSDEENL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  72 PANKRRVNTVFQ--DYALFPHLnVYENIAFGLRLKKFSKQEIDKEVKEALKLVKLTGYeQRHIDEM-SGGQKQRVAIARA 148
Cdd:PRK13633  81 WDIRNKAGMVFQnpDNQIVATI-VEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEY-RRHAPHLlSGGQKQRVAIAGI 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488386109 149 IVNKPEILLLDESLSALDLKLRTEMQYELRELQKRLGITFIFVTHDQEEAlALSDYIFVMKDGEIQQFGTPTDIYDE 225
Cdd:PRK13633 159 LAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEA-VEADRIIVMDSGKVVMEGTPKEIFKE 234
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
 5-226 1.20e-33

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: 131.04  E-value: 1.20e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   5 LSFKKVTKKFDDTT--ILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANK--RRVNT 80
Cdd:COG4987  334 LELEDVSFRYPGAGrpVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDlrRRIAV 413

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  81 VFQDYALFpHLNVYENIAFGlrlkkfsKQEI-DKEVKEALKLVKLT--------GYEQRhIDE----MSGGQKQRVAIAR 147
Cdd:COG4987  414 VPQRPHLF-DTTLRENLRLA-------RPDAtDEELWAALERVGLGdwlaalpdGLDTW-LGEggrrLSGGERRRLALAR 484

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 148 AIVNKPEILLLDESLSALDLKlrTEMQYeLRELQKRL-GITFIFVTHDqEEALALSDYIFVMKDGEIQQFGTPTDIYDEP 226
Cdd:COG4987  485 ALLRDAPILLLDEPTEGLDAA--TEQAL-LADLLEALaGRTVLLITHR-LAGLERMDRILVLEDGRIVEQGTHEELLAQN 560
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
 2-235 1.43e-33

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 125.16  E-value: 1.43e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   2 ESLLSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQ------PNEGQIIYKNQSIEKLPANK 75
Cdd:PRK14246   8 EDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIK 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  76 RR--VNTVFQDYALFPHLNVYENIAFGLRLKKFS-KQEIDKEVKEALKLVKLtgYEQRH------IDEMSGGQKQRVAIA 146
Cdd:PRK14246  88 LRkeVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKeKREIKKIVEECLRKVGL--WKEVYdrlnspASQLSGGQQQRLTIA 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 147 RAIVNKPEILLLDESLSALDLKLRTEMQYELRELQKRlgITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIYDEP 226
Cdd:PRK14246 166 RALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSP 243


                 ....*....
gi 488386109 227 VNRFVADFI 235
Cdd:PRK14246 244 KNELTEKYV 252
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
13-223 1.63e-33

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 125.50  E-value: 1.63e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  13 KFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIE----KLPANKRRVNTVFQD--YA 86
Cdd:PRK13638  10 RYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDyskrGLLALRQQVATVFQDpeQQ 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  87 LFpHLNVYENIAFGLRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDESLSALD 166
Cdd:PRK13638  90 IF-YTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLD 168

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 488386109 167 LKLRTEMQYELRELQKRlGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIY 223
Cdd:PRK13638 169 PAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
4-194 2.21e-33

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 123.45  E-value: 2.21e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   4 LLSFKKVTKKF-DDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKL-----PANKRR 77
Cdd:PRK10908   1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLknrevPFLRRQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  78 VNTVFQDYALFPHLNVYENIAFGLRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILL 157
Cdd:PRK10908  81 IGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLL 160

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 488386109 158 LDESLSALDLKLrTEMQYELRELQKRLGITFIFVTHD 194
Cdd:PRK10908 161 ADEPTGNLDDAL-SEGILRLFEEFNRVGVTVLMATHD 196
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
 1-238 2.50e-33

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


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 124.33  E-value: 2.50e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   1 MESLLSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLP----ANKR 76
Cdd:PRK11300   2 SQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPghqiARMG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  77 RVNTvFQDYALFPHLNVYEN-------------IAFGLRLKKFSKQEIDKEVKEA--LKLVKLTGYEQRHIDEMSGGQKQ 141
Cdd:PRK11300  82 VVRT-FQHVRLFREMTVIENllvaqhqqlktglFSGLLKTPAFRRAESEALDRAAtwLERVGLLEHANRQAGNLAYGQQR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 142 RVAIARAIVNKPEILLLDESLSALDLKLRTEMQYELRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTD 221
Cdd:PRK11300 161 RLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEE 240

                        250
                 ....*....|....*..
gi 488386109 222 IYDEPvnRFVADFIGES 238
Cdd:PRK11300 241 IRNNP--DVIKAYLGEA 255
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
 7-230 2.80e-33

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 129.44  E-value: 2.80e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   7 FKKVTkkfDDTTILNNMNLDIESGYFYTLLGPSGCGKTT----ILKLIAgfeqpNEGQIIYKNQSIEK------LPAnKR 76
Cdd:PRK15134 292 LKRTV---DHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLHNlnrrqlLPV-RH 362

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  77 RVNTVFQD--YALFPHLNVYENIAFGLRL--KKFSKQEIDKEVKEALKLVKL-TGYEQRHIDEMSGGQKQRVAIARAIVN 151
Cdd:PRK15134 363 RIQVVFQDpnSSLNPRLNVLQIIEEGLRVhqPTLSAAQREQQVIAVMEEVGLdPETRHRYPAEFSGGQRQRIAIARALIL 442

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488386109 152 KPEILLLDESLSALDLKLRTEMQYELRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIYDEPVNRF 230
Cdd:PRK15134 443 KPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEY 521
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
 15-225 3.63e-33

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 124.57  E-value: 3.63e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  15 DDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIE----KLPANKRRVNTVFQ--DYALF 88
Cdd:PRK13636  17 DGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDysrkGLMKLRESVGMVFQdpDNQLF 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  89 PhLNVYENIAFGLRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDESLSALDLK 168
Cdd:PRK13636  97 S-ASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPM 175

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 488386109 169 LRTEMQYELRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIYDE 225
Cdd:PRK13636 176 GVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAE 232
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
 2-229 5.34e-33

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


Pssm-ID: 440752 [Multi-domain]  Cd Length: 240  Bit Score: 122.83  E-value: 5.34e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   2 ESLLSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANKR-R--V 78
Cdd:COG1137    1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRaRlgI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  79 NTVFQDYALFPHLNVYENIAFGLRLKKFSKQEIDKEVKEALKLVKLTgyeqrHI-----DEMSGGQKQRVAIARAIVNKP 153
Cdd:COG1137   81 GYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGIT-----HLrkskaYSLSGGERRRVEIARALATNP 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488386109 154 EILLLDESLSALDLKLRTEMQYELRELQKRlGITfIFVT-HDQEEALALSDYIFVMKDGEIQQFGTPTDIYDEPVNR 229
Cdd:COG1137  156 KFILLDEPFAGVDPIAVADIQKIIRHLKER-GIG-VLITdHNVRETLGICDRAYIISEGKVLAEGTPEEILNNPLVR 230
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
 2-226 6.41e-33

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: 122.78  E-value: 6.41e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   2 ESLLSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANKRR---V 78
Cdd:COG0410    1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIArlgI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  79 NTVFQDYALFPHLNVYENIAFGLRLKKfSKQEIDKEVKEALKLV-KLtgYEQRHID--EMSGGQKQRVAIARAIVNKPEI 155
Cdd:COG0410   81 GYVPEGRRIFPSLTVEENLLLGAYARR-DRAEVRADLERVYELFpRL--KERRRQRagTLSGGEQQMLAIGRALMSRPKL 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488386109 156 LLLDE-SLsALDLKLRTEMQYELRELqKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIYDEP 226
Cdd:COG0410  158 LLLDEpSL-GLAPLIVEEIFEIIRRL-NREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADP 227
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
 4-197 7.81e-33

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 122.13  E-value: 7.81e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   4 LLSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANKRR--VNTV 81
Cdd:PRK10247   7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRqqVSYC 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  82 FQDYALFPHlNVYENIAFGLRLKKFSKQE---IDKEVKEALKLVKLtgyeQRHIDEMSGGQKQRVAIARAIVNKPEILLL 158
Cdd:PRK10247  87 AQTPTLFGD-TVYDNLIFPWQIRNQQPDPaifLDDLERFALPDTIL----TKNIAELSGGEKQRISLIRNLQFMPKVLLL 161

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 488386109 159 DESLSALDLKLRTEMQYELRELQKRLGITFIFVTHDQEE 197
Cdd:PRK10247 162 DEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE 200
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
 1-235 1.09e-32

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 122.58  E-value: 1.09e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   1 MESLLSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLI--AGFEQPN---EGQIIYKNQSIEKLPAN- 74
Cdd:PRK14239   2 TEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGHNIYSPRTDt 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  75 ---KRRVNTVFQDYALFPhLNVYENIAFGLRLKKF-SKQEIDKEVKEALKLVKLTGYEQRHIDE----MSGGQKQRVAIA 146
Cdd:PRK14239  82 vdlRKEIGMVFQQPNPFP-MSIYENVVYGLRLKGIkDKQVLDEAVEKSLKGASIWDEVKDRLHDsalgLSGGQQQRVCIA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 147 RAIVNKPEILLLDESLSALDLKLRTEMQYELRELQKRLgiTFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIYDEP 226
Cdd:PRK14239 161 RVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNP 238


                 ....*....
gi 488386109 227 VNRFVADFI 235
Cdd:PRK14239 239 KHKETEDYI 247
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
2-226 1.49e-32

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 122.38  E-value: 1.49e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   2 ESLLSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSI------------- 68
Cdd:PRK10619   3 ENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdkdgqlkva 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  69 --EKLPANKRRVNTVFQDYALFPHLNVYENIAFG-LRLKKFSKQEIDKEVKEALKLVKLTGYEQ-RHIDEMSGGQKQRVA 144
Cdd:PRK10619  83 dkNQLRLLRTRLTMVFQHFNLWSHMTVLENVMEApIQVLGLSKQEARERAVKYLAKVGIDERAQgKYPVHLSGGQQQRVS 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 145 IARAIVNKPEILLLDESLSALDLKLRTEMqyeLRELQK--RLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDI 222
Cdd:PRK10619 163 IARALAMEPEVLLFDEPTSALDPELVGEV---LRIMQQlaEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQL 239


                 ....
gi 488386109 223 YDEP 226
Cdd:PRK10619 240 FGNP 243
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
 21-226 1.69e-32

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 124.05  E-value: 1.69e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  21 NNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANKRR-----VNTVFQD--YALFPHLNV 93
Cdd:PRK15079  38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRavrsdIQMIFQDplASLNPRMTI 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  94 YENIAFGLRL--KKFSKQEIDKEVKEALKLVKL-TGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDESLSALDLKLR 170
Cdd:PRK15079 118 GEIIAEPLRTyhPKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQ 197

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 488386109 171 TEMQYELRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIYDEP 226
Cdd:PRK15079 198 AQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNP 253
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
 14-235 1.88e-32

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 121.87  E-value: 1.88e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  14 FDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPN-----EGQIIYKNQSIEKLPAN----KRRVNTVFQD 84
Cdd:PRK14267  14 YGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSPDVDpievRREVGMVFQY 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  85 YALFPHLNVYENIAFGLRLKKF--SKQEIDKEVKEALKLVKLTGYEQRHIDE----MSGGQKQRVAIARAIVNKPEILLL 158
Cdd:PRK14267  94 PNPFPHLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALWDEVKDRLNDypsnLSGGQRQRLVIARALAMKPKILLM 173

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488386109 159 DESLSALDLKLRTEMQYELRELQKRLgiTFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIYDEPVNRFVADFI 235
Cdd:PRK14267 174 DEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELTEKYV 248
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
 1-226 2.41e-32

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 127.92  E-value: 2.41e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109    1 MESLLSFKKVTKKF---DDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPAN--K 75
Cdd:TIGR00958 475 LEGLIEFQDVSFSYpnrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHylH 554

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   76 RRVNTVFQDYALFPHlNVYENIAFGLRlkKFSKQEIDKEVKEALKLVKLTGYEQRH---IDE----MSGGQKQRVAIARA 148
Cdd:TIGR00958 555 RQVALVGQEPVLFSG-SVRENIAYGLT--DTPDEEIMAAAKAANAHDFIMEFPNGYdteVGEkgsqLSGGQKQRIAIARA 631

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488386109  149 IVNKPEILLLDESLSALDlklrTEMQYELRELQKRLGITFIFVTHdQEEALALSDYIFVMKDGEIQQFGTPTDIYDEP 226
Cdd:TIGR00958 632 LVRKPRVLILDEATSALD----AECEQLLQESRSRASRTVLLIAH-RLSTVERADQILVLKKGSVVEMGTHKQLMEDQ 704
cbiO PRK13642
energy-coupling factor transporter ATPase;
1-223 1.40e-31

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 120.20  E-value: 1.40e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   1 MESLLSFKKVTKKFD---DTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEG--QIIYKNQSIEKLPANK 75
Cdd:PRK13642   1 MNKILEVENLVFKYEkesDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGkvKIDGELLTAENVWNLR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  76 RRVNTVFQDY-ALFPHLNVYENIAFGLRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPE 154
Cdd:PRK13642  81 RKIGMVFQNPdNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPE 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488386109 155 ILLLDESLSALDLKLRTEMQYELRELQKRLGITFIFVTHDQEEAlALSDYIFVMKDGEIQQFGTPTDIY 223
Cdd:PRK13642 161 IIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEA-ASSDRILVMKAGEIIKEAAPSELF 228
cbiO PRK13649
energy-coupling factor transporter ATPase;
20-225 2.06e-31

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 119.85  E-value: 2.06e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  20 LNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANK------RRVNTVFQdyalFPHLNV 93
Cdd:PRK13649  23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKdikqirKKVGLVFQ----FPESQL 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  94 YE-----NIAFGLRLKKFSKQEIDKEVKEALKLVKLT-GYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDESLSALDL 167
Cdd:PRK13649  99 FEetvlkDVAFGPQNFGVSQEEAEALAREKLALVGISeSLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDP 178

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 488386109 168 KLRTEMQYELRELQkRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIYDE 225
Cdd:PRK13649 179 KGRKELMTLFKKLH-QSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
5-233 2.48e-31

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 118.96  E-value: 2.48e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   5 LSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANK--RRVntvf 82
Cdd:PRK11231   3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQlaRRL---- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  83 qdyALFP--HL-----NVYENIAFG----LRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVN 151
Cdd:PRK11231  79 ---ALLPqhHLtpegiTVRELVAYGrspwLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQ 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 152 KPEILLLDESLSALDLKLRTEMQYELRELQKRlGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIYDEPVNRFV 231
Cdd:PRK11231 156 DTPVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGLLRTV 234


                 ..
gi 488386109 232 AD 233
Cdd:PRK11231 235 FD 236
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
 2-224 8.87e-31

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: 122.90  E-value: 8.87e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109    2 ESLLSFKKVTKKF--DDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIE--KLPANKRR 77
Cdd:TIGR02203 328 RGDVEFRNVTFRYpgRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLAdyTLASLRRQ 407

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   78 VNTVFQDYALFPHlNVYENIAFGlRLKKFSKQEIDKEVKEAlklvkltgYEQRHIDEM---------------SGGQKQR 142
Cdd:TIGR02203 408 VALVSQDVVLFND-TIANNIAYG-RTEQADRAEIERALAAA--------YAQDFVDKLplgldtpigengvllSGGQRQR 477

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  143 VAIARAIVNKPEILLLDESLSALDLKLRTEMQYELRELQKrlGITFIFVTHdQEEALALSDYIFVMKDGEIQQFGTPTDI 222
Cdd:TIGR02203 478 LAIARALLKDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAH-RLSTIEKADRIVVMDDGRIVERGTHNEL 554


                  ..
gi 488386109  223 YD 224
Cdd:TIGR02203 555 LA 556
cbiO PRK13643
energy-coupling factor transporter ATPase;
4-225 1.05e-30

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 118.30  E-value: 1.05e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   4 LLSFKKVTKKFDDTT-----ILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEG-----QIIYKNQSIEK-LP 72
Cdd:PRK13643   1 MIKFEKVNYTYQPNSpfasrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGkvtvgDIVVSSTSKQKeIK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  73 ANKRRVNTVFQdyalFPHLNVYE-----NIAFGLRLKKFSKQEIDKEVKEALKLVKLTG-YEQRHIDEMSGGQKQRVAIA 146
Cdd:PRK13643  81 PVRKKVGVVFQ----FPESQLFEetvlkDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADeFWEKSPFELSGGQMRRVAIA 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488386109 147 RAIVNKPEILLLDESLSALDLKLRTEMQyELRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIYDE 225
Cdd:PRK13643 157 GILAMEPEVLVLDEPTAGLDPKARIEMM-QLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQE 234
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
5-273 1.22e-30

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 119.17  E-value: 1.22e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   5 LSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQI-IYKNQSIEKLPANKRRVNTVFQ 83
Cdd:PRK13536  42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKItVLGVPVPARARLARARIGVVPQ 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  84 DYALFPHLNVYEN-IAFGlRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDESL 162
Cdd:PRK13536 122 FDNLDLEFTVRENlLVFG-RYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPT 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 163 SALDLKLRTEMQYELRELQKRlGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIYDEpvnrfvadFIGESnivd 242
Cdd:PRK13536 201 TGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDE--------HIGCQ---- 267

                        250       260       270
                 ....*....|....*....|....*....|..
gi 488386109 243 gtmvkdfVVNIYGQDFECVDARI-PSGKKIEV 273
Cdd:PRK13536 268 -------VIEIYGGDPHELSSLVkPYARRIEV 292
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
 18-217 1.47e-30

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: 116.09  E-value: 1.47e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  18 TILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLpankrRVNTVFQdyalfPHLNVYENI 97
Cdd:cd03220   36 WALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLL-----GLGGGFN-----PELTGRENI 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  98 AFGLRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDESLSALDLKLRTEMQYEL 177
Cdd:cd03220  106 YLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRL 185

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 488386109 178 RELQKRlGITFIFVTHDQEEALALSDYIFVMKDGEIQQFG 217
Cdd:cd03220  186 RELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
 19-213 2.89e-30

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: 113.85  E-value: 2.89e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  19 ILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKL-PANKRR-VNTVFQDYALFPHlNVYEN 96
Cdd:cd03246   17 VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWdPNELGDhVGYLPQDDELFSG-SIAEN 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  97 IafglrlkkfskqeidkevkealklvkltgyeqrhideMSGGQKQRVAIARAIVNKPEILLLDESLSALDLKLRTEMQYE 176
Cdd:cd03246   96 I-------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQA 138

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 488386109 177 LRELQKRlGITFIFVTHdQEEALALSDYIFVMKDGEI 213
Cdd:cd03246  139 IAALKAA-GATRIVIAH-RPETLASADRILVLEDGRV 173
LPS_export_lptB TIGR04406
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ...
 5-238 2.91e-30

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


Pssm-ID: 275199 [Multi-domain]  Cd Length: 239  Bit Score: 115.83  E-value: 2.91e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109    5 LSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANKR-RVNTVF- 82
Cdd:TIGR04406   2 LVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERaRLGIGYl 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   83 -QDYALFPHLNVYENIAFGLRL-KKFSKQEIDKEVKEALKLVKLTgyeqrHIDE-----MSGGQKQRVAIARAIVNKPEI 155
Cdd:TIGR04406  82 pQEASIFRKLTVEENIMAVLEIrKDLDRAEREERLEALLEEFQIS-----HLRDnkamsLSGGERRRVEIARALATNPKF 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  156 LLLDESLSALDLKLRTEMQYELRELQKRlGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIYDEPVNRFVadFI 235
Cdd:TIGR04406 157 ILLDEPFAGVDPIAVGDIKKIIKHLKER-GIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVANEKVRRV--YL 233


                  ...
gi 488386109  236 GES 238
Cdd:TIGR04406 234 GEQ 236
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
 5-208 6.02e-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: 120.08  E-value: 6.02e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109    5 LSFKKVTKKFDDTT-ILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPAN--KRRVNTV 81
Cdd:TIGR02857 322 LEFSGVSVAYPGRRpALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADswRDQIAWV 401

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   82 FQDYALFPHlNVYENIAFGLRLKKfskqeiDKEVKEALKLVKLTGYEQ-------RHIDE----MSGGQKQRVAIARAIV 150
Cdd:TIGR02857 402 PQHPFLFAG-TIAENIRLARPDAS------DAEIREALERAGLDEFVAalpqgldTPIGEggagLSGGQAQRLALARAFL 474

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 488386109  151 NKPEILLLDESLSALDLKLRTEMQYELRELQKrlGITFIFVTHDqEEALALSDYIFVM 208
Cdd:TIGR02857 475 RDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHR-LALAALADRIVVL 529
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
 16-226 6.43e-30

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 115.67  E-value: 6.43e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  16 DTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEK--LPANKRRVNTVFQ--DYALFPHl 91
Cdd:PRK13652  16 SKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKenIREVRKFVGLVFQnpDDQIFSP- 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  92 NVYENIAFGLRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDESLSALDLKLRT 171
Cdd:PRK13652  95 TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVK 174

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 488386109 172 EMQYELRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIYDEP 226
Cdd:PRK13652 175 ELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
 20-235 9.48e-30

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 114.88  E-value: 9.48e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  20 LNNMNLDIESGYFYTLLGPSGCGKTTILK-------LIAGFEQpnEGQIIYKNQSI---EKLPAN-KRRVNTVFQDYALF 88
Cdd:PRK14243  26 VKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGFRV--EGKVTFHGKNLyapDVDPVEvRRRIGMVFQKPNPF 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  89 PHlNVYENIAFGLRLKKFsKQEIDKEVKEALKLVKLTGYEQRHIDE----MSGGQKQRVAIARAIVNKPEILLLDESLSA 164
Cdd:PRK14243 104 PK-SIYDNIAYGARINGY-KGDMDELVERSLRQAALWDEVKDKLKQsglsLSGGQQQRLCIARAIAVQPEVILMDEPCSA 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 165 LD--LKLRTEmqyelrELQKRLG--ITFIFVTHDQEEALALSDYIFVM---------KDGEIQQFGTPTDIYDEPVNRFV 231
Cdd:PRK14243 182 LDpiSTLRIE------ELMHELKeqYTIIIVTHNMQQAARVSDMTAFFnveltegggRYGYLVEFDRTEKIFNSPQQQAT 255


                 ....
gi 488386109 232 ADFI 235
Cdd:PRK14243 256 RDYV 259
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
 1-225 1.40e-29

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


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 114.02  E-value: 1.40e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   1 MESLLSFKKVTKKF----------------------DDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNE 58
Cdd:COG1134    1 MSSMIEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  59 GQIIyknqsieklpANKRR-----VNTVFQdyalfPHLNVYENIAFGLRLKKFSKQEIDKEVKEALKLVKLtgyeQRHID 133
Cdd:COG1134   81 GRVE----------VNGRVsalleLGAGFH-----PELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAEL----GDFID 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 134 E----MSGGQKQRVAIARAIVNKPEILLLDESLSALDLKLRTEMQYELRELQKRlGITFIFVTHDQEEALALSDYIFVMK 209
Cdd:COG1134  142 QpvktYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLE 220

                        250
                 ....*....|....*.
gi 488386109 210 DGEIQQFGTPTDIYDE 225
Cdd:COG1134  221 KGRLVMDGDPEEVIAA 236
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
 15-227 6.71e-29

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 112.91  E-value: 6.71e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  15 DDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIiyKNQSIEKLPANKR----RVNTVFQDY--ALF 88
Cdd:PRK13647  16 DGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRV--KVMGREVNAENEKwvrsKVGLVFQDPddQVF 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  89 PhLNVYENIAFGLRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDESLSALDLK 168
Cdd:PRK13647  94 S-STVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPR 172

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 488386109 169 LRTEMQYELRELQKRlGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIYDEPV 227
Cdd:PRK13647 173 GQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDEDI 230
cbiO PRK13644
energy-coupling factor transporter ATPase;
4-226 1.31e-28

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 112.39  E-value: 1.31e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   4 LLSFKKVTKKF-DDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQS---IEKLPANKRRVN 79
Cdd:PRK13644   1 MIRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDtgdFSKLQGIRKLVG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  80 TVFQD-YALFPHLNVYENIAFGLRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLL 158
Cdd:PRK13644  81 IVFQNpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIF 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488386109 159 DESLSALDLKLRTEMQYELRELQKRlGITFIFVTHDQEEaLALSDYIFVMKDGEIQQFGTPTDIYDEP 226
Cdd:PRK13644 161 DEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDV 226
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
 22-226 3.98e-28

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 115.34  E-value: 3.98e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  22 NMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANK-----RRVNTVFQD-YA-LFPHLNVY 94
Cdd:PRK10261 342 KVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKlqalrRDIQFIFQDpYAsLDPRQTVG 421

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  95 ENIAFGLRLKKF-SKQEIDKEVKEALKLVKLT-GYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDESLSALDLKLRTE 172
Cdd:PRK10261 422 DSIMEPLRVHGLlPGKAAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQ 501

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488386109 173 MQYELRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIYDEP 226
Cdd:PRK10261 502 IINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENP 555
cbiO PRK13641
energy-coupling factor transporter ATPase;
20-234 6.76e-28

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 110.69  E-value: 6.76e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  20 LNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQI------IYKNQSIEKLPANKRRVNTVFQdyalFPHLNV 93
Cdd:PRK13641  23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTItiagyhITPETGNKNLKKLRKKVSLVFQ----FPEAQL 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  94 YEN-----IAFGLRLKKFSkqeiDKEVKE-ALKLVKLTGYEQRHID----EMSGGQKQRVAIARAIVNKPEILLLDESLS 163
Cdd:PRK13641  99 FENtvlkdVEFGPKNFGFS----EDEAKEkALKWLKKVGLSEDLISkspfELSGGQMRRVAIAGVMAYEPEILCLDEPAA 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 164 ALDLKLRTEMQYELRELQKRlGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIY-----------DEPV-NRFV 231
Cdd:PRK13641 175 GLDPEGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFsdkewlkkhylDEPAtSRFA 253


                 ...
gi 488386109 232 ADF 234
Cdd:PRK13641 254 SKL 256
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
1-238 6.93e-28

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 109.88  E-value: 6.93e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   1 MESLLSFKKVTKKFDDTTIL---------NNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKL 71
Cdd:PRK15112   1 VETLLEVRNLSKTFRYRTGWfrrqtveavKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  72 PANKR--RVNTVFQD--YALFPHLNVYENIAFGLRLK-KFSKQEIDKEVKEALKLVKLTGYEQRHIDEM-SGGQKQRVAI 145
Cdd:PRK15112  81 DYSYRsqRIRMIFQDpsTSLNPRQRISQILDFPLRLNtDLEPEQREKQIIETLRQVGLLPDHASYYPHMlAPGQKQRLGL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 146 ARAIVNKPEILLLDESLSALDLKLRTEMQYELRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIYDE 225
Cdd:PRK15112 161 ARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLAS 240

                        250
                 ....*....|....*..
gi 488386109 226 PVN----RFVADFIGES 238
Cdd:PRK15112 241 PLHeltkRLIAGHFGEA 257
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
 16-218 7.08e-28

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: 114.53  E-value: 7.08e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  16 DTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKL-PANKRR-VNTVFQDYALFphlN- 92
Cdd:COG5265  370 ERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVtQASLRAaIGIVPQDTVLF---Nd 446

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  93 -VYENIAFGlRLkkfskQEIDKEVKEALKLVKLT--------GYEQRhIDE----MSGGQKQRVAIARAIVNKPEILLLD 159
Cdd:COG5265  447 tIAYNIAYG-RP-----DASEEEVEAAARAAQIHdfieslpdGYDTR-VGErglkLSGGEKQRVAIARTLLKNPPILIFD 519

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488386109 160 ESLSALDLKLRTEMQYELRELQKrlGITFIFVTHdqeealALS-----DYIFVMKDGEIQQFGT 218
Cdd:COG5265  520 EATSALDSRTERAIQAALREVAR--GRTTLVIAH------RLStivdaDEILVLEAGRIVERGT 575
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
 8-222 8.04e-28

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 110.95  E-value: 8.04e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   8 KKVTKKFDDTT-----ILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQI--IYKNQSIEKLPANK----- 75
Cdd:PRK13651   6 KNIVKIFNKKLptelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewIFKDEKNKKKTKEKekvle 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  76 -------------------RRVNTVFQ--DYALFPHlNVYENIAFGLRLKKFSKQEIDKEVKEALKLVKL-TGYEQRHID 133
Cdd:PRK13651  86 klviqktrfkkikkikeirRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdESYLQRSPF 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 134 EMSGGQKQRVAIARAIVNKPEILLLDESLSALDLKLRTEMQYELRELQKRlGITFIFVTHDQEEALALSDYIFVMKDGEI 213
Cdd:PRK13651 165 ELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFKDGKI 243


                 ....*....
gi 488386109 214 QQFGTPTDI 222
Cdd:PRK13651 244 IKDGDTYDI 252
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
 16-222 8.69e-28

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: 114.07  E-value: 8.69e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  16 DTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQI------IYKN------QSIEKLPankrrvntvfQ 83
Cdd:COG4618  344 KRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVrldgadLSQWdreelgRHIGYLP----------Q 413

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  84 DYALFPHlNVYENIAfglRLkkfskQEIDKE-VKEALKLV-------KLT-GYEQRhIDE----MSGGQKQRVAIARAIV 150
Cdd:COG4618  414 DVELFDG-TIAENIA---RF-----GDADPEkVVAAAKLAgvhemilRLPdGYDTR-IGEggarLSGGQRQRIGLARALY 483

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488386109 151 NKPEILLLDESLSALD----LKLRTemqyELRELQKRlGITFIFVTHDQeEALALSDYIFVMKDGEIQQFGTPTDI 222
Cdd:COG4618  484 GDPRLVVLDEPNSNLDdegeAALAA----AIRALKAR-GATVVVITHRP-SLLAAVDKLLVLRDGRVQAFGPRDEV 553
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
14-200 9.24e-28

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 107.70  E-value: 9.24e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  14 FDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGqiiyknqSIEKLPAnkRRVNTVFQDYAL---FPh 90
Cdd:NF040873   2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSG-------TVRRAGG--ARVAYVPQRSEVpdsLP- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  91 LNVYENIAFGL--------RLKKFSKQEIDkevkEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDESL 162
Cdd:NF040873  72 LTVRDLVAMGRwarrglwrRLTRDDRAAVD----DALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPT 147

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 488386109 163 SALDLKLRTEMQYELRELQKRlGITFIFVTHDQEEALA 200
Cdd:NF040873 148 TGLDAESRERIIALLAEEHAR-GATVVVVTHDLELVRR 184
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
 5-222 1.21e-27

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 112.24  E-value: 1.21e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   5 LSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANK--RRVNTVF 82
Cdd:PRK09536   4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAasRRVASVP 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  83 QDYALFPHLNVYENIAFGL--RLKKFSKQEIDKE--VKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLL 158
Cdd:PRK09536  84 QDTSLSFEFDVRQVVEMGRtpHRSRFDTWTETDRaaVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLL 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488386109 159 DESLSALDL--KLRTemqyelRELQKRL---GITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDI 222
Cdd:PRK09536 164 DEPTASLDInhQVRT------LELVRRLvddGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADV 226
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
 2-213 1.29e-27

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


Pssm-ID: 213201 [Multi-domain]  Cd Length: 226  Bit Score: 108.13  E-value: 1.29e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   2 ESLLSFKKVTKKF----DDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNE---GQIIYKNQSIEKlPAN 74
Cdd:cd03234    1 QRVLPWWDVGLKAknwnKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRKP-DQF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  75 KRRVNTVFQDYALFPHLNVYENIAFGLRLK---KFSKQEIDKEVK-EALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIV 150
Cdd:cd03234   80 QKCVAYVRQDDILLPGLTVRETLTYTAILRlprKSSDAIRKKRVEdVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLL 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488386109 151 NKPEILLLDESLSALDLKLRTEMQYELRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEI 213
Cdd:cd03234  160 WDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEI 222
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
 5-231 1.33e-27

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


Pssm-ID: 132313 [Multi-domain]  Cd Length: 520  Bit Score: 113.36  E-value: 1.33e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109    5 LSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQ--PNEGQIIYK------------------ 64
Cdd:TIGR03269   1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIIYHvalcekcgyverpskvge 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   65 -----NQSIEKLPAN------------KRRVNTVFQ-DYALFPHLNVYENIAFGLRLKKFskqEIDKEVKEALKLVKLTG 126
Cdd:TIGR03269  81 pcpvcGGTLEPEEVDfwnlsdklrrriRKRIAIMLQrTFALYGDDTVLDNVLEALEEIGY---EGKEAVGRAVDLIEMVQ 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  127 YEQR--HI-DEMSGGQKQRVAIARAIVNKPEILLLDESLSALDLKLRTEMQYELRELQKRLGITFIFVTHDQEEALALSD 203
Cdd:TIGR03269 158 LSHRitHIaRDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSD 237

                         250       260
                  ....*....|....*....|....*...
gi 488386109  204 YIFVMKDGEIQQFGTPtdiyDEPVNRFV 231
Cdd:TIGR03269 238 KAIWLENGEIKEEGTP----DEVVAVFM 261
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
1-216 3.33e-27

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 108.18  E-value: 3.33e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   1 MESLLSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGF---EQPNEGQIIYKNQSIE---KLPAN 74
Cdd:PRK09984   1 MQTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQregRLARD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  75 --KRRVNT--VFQDYALFPHLNVYENIAFGLR---------LKKFSKQEiDKEVKEALKLVKLTGYEQRHIDEMSGGQKQ 141
Cdd:PRK09984  81 irKSRANTgyIFQQFNLVNRLSVLENVLIGALgstpfwrtcFSWFTREQ-KQRALQALTRVGMVHFAHQRVSTLSGGQQQ 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 142 RVAIARAIVNKPEILLLDESLSALDLKLRTEMQYELRELQKRLGITFIFVTHDQEEALALSDYIFVMK------DGEIQQ 215
Cdd:PRK09984 160 RVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRqghvfyDGSSQQ 239


                 .
gi 488386109 216 F 216
Cdd:PRK09984 240 F 240
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
8-222 4.26e-27

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 107.76  E-value: 4.26e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   8 KKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANK--RRVNTVFQDY 85
Cdd:PRK10253  11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvaRRIGLLAQNA 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  86 ALFPHLNVYENIAFGLRLKK--FSK--QEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDES 161
Cdd:PRK10253  91 TTPGDITVQELVARGRYPHQplFTRwrKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEP 170

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488386109 162 LSALDLKLRTEMQYELRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDI 222
Cdd:PRK10253 171 TTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
cbiO PRK13645
energy-coupling factor transporter ATPase;
20-223 1.29e-26

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 107.02  E-value: 1.29e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  20 LNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIeklPAN----------KRRVNTVFQ--DYAL 87
Cdd:PRK13645  27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAI---PANlkkikevkrlRKEIGLVFQfpEYQL 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  88 FPHlNVYENIAFGLRLKKFSKQEIDKEVKEALKLVKL-TGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDESLSALD 166
Cdd:PRK13645 104 FQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLD 182

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 488386109 167 LKLRTEMQYELRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIY 223
Cdd:PRK13645 183 PKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIF 239
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
 18-215 3.25e-26

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 104.48  E-value: 3.25e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  18 TILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANKR------RVNTVFQDYALFPHL 91
Cdd:PRK10584  24 SILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARaklrakHVGFVFQSFMLIPTL 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  92 NVYENIafglRLKKFSKQEIDKEVKE-ALKLVKLTGYEQR--HID-EMSGGQKQRVAIARAIVNKPEILLLDESLSALDL 167
Cdd:PRK10584 104 NALENV----ELPALLRGESSRQSRNgAKALLEQLGLGKRldHLPaQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDR 179

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 488386109 168 KLRTEMQYELRELQKRLGITFIFVTHDQEEAlALSDYIFVMKDGEIQQ 215
Cdd:PRK10584 180 QTGDKIADLLFSLNREHGTTLILVTHDLQLA-ARCDRRLRLVNGQLQE 226
type_I_sec_PrtD TIGR01842
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ...
 17-222 5.47e-26

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: 108.97  E-value: 5.47e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   17 TTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANK--RRVNTVFQDYALFPHlNVY 94
Cdd:TIGR01842 331 KPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETfgKHIGYLPQDVELFPG-TVA 409

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   95 ENIAfglrlkKFSKQEIDKEVKEALKL-------VKL-TGYEQrHIDE----MSGGQKQRVAIARAIVNKPEILLLDESL 162
Cdd:TIGR01842 410 ENIA------RFGENADPEKIIEAAKLagvheliLRLpDGYDT-VIGPggatLSGGQRQRIALARALYGDPKLVVLDEPN 482

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  163 SALDLKLRTEMQYELRELQKRlGITFIFVTHdQEEALALSDYIFVMKDGEIQQFGTPTDI 222
Cdd:TIGR01842 483 SNLDEEGEQALANAIKALKAR-GITVVVITH-RPSLLGCVDKILVLQDGRIARFGERDEV 540
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
 5-193 5.60e-26

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 108.74  E-value: 5.60e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   5 LSFKKVTKKF-DDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIyknqsiekLPANKRrvntvfq 83
Cdd:COG4178  363 LALEDLTLRTpDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIA--------RPAGAR------- 427

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  84 dyALF----PHL---NVYENIAFGLRLKKFSkqeiDKEVKEALKLVKLTGYEQRhIDE-------MSGGQKQRVAIARAI 149
Cdd:COG4178  428 --VLFlpqrPYLplgTLREALLYPATAEAFS----DAELREALEAVGLGHLAER-LDEeadwdqvLSLGEQQRLAFARLL 500

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 488386109 150 VNKPEILLLDESLSALDLKLRTEMqYELreLQKRL-GITFIFVTH 193
Cdd:COG4178  501 LHKPDWLFLDEATSALDEENEAAL-YQL--LREELpGTTVISVGH 542
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
5-218 6.49e-26

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 108.95  E-value: 6.49e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   5 LSFKKVTKKFD--DTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIE--KLPANKRRVNT 80
Cdd:PRK11176 342 IEFRNVTFTYPgkEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRdyTLASLRNQVAL 421

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  81 VFQDYALFpHLNVYENIAFGlRLKKFSKQEIDKEVKEAlklvkltgYEQRHIDEM---------------SGGQKQRVAI 145
Cdd:PRK11176 422 VSQNVHLF-NDTIANNIAYA-RTEQYSREQIEEAARMA--------YAMDFINKMdngldtvigengvllSGGQRQRIAI 491

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488386109 146 ARAIVNKPEILLLDESLSALDLKLRTEMQYELRELQKRLgiTFIFVTHDQ---EEAlalsDYIFVMKDGEIQQFGT 218
Cdd:PRK11176 492 ARALLRDSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLstiEKA----DEILVVEDGEIVERGT 561
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
 5-225 1.53e-25

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: 102.95  E-value: 1.53e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   5 LSFKKVTKKF--DDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPAN--KRRVNT 80
Cdd:cd03252    1 ITFEHVRFRYkpDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAwlRRQVGV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  81 VFQDYALFpHLNVYENIAFGlrlkkfsKQEIDKE-VKEALKLV-------KL-TGYEQRhIDE----MSGGQKQRVAIAR 147
Cdd:cd03252   81 VLQENVLF-NRSIRDNIALA-------DPGMSMErVIEAAKLAgahdfisELpEGYDTI-VGEqgagLSGGQRQRIAIAR 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488386109 148 AIVNKPEILLLDESLSALDLKLRTEMQYELRELQKrlGITFIFVTHdQEEALALSDYIFVMKDGEIQQFGTPTDIYDE 225
Cdd:cd03252  152 ALIHNPRILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAH-RLSTVKNADRIIVMEKGRIVEQGSHDELLAE 226
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
 20-226 2.49e-25

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 104.28  E-value: 2.49e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  20 LNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPAN-----KRRVNTVFQD-YA-LFPHLN 92
Cdd:PRK11308  31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEaqkllRQKIQIVFQNpYGsLNPRKK 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  93 VYENIAFGLRLK-KFSKQEIDKEVKEALKLVKL-TGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDESLSALDLKLR 170
Cdd:PRK11308 111 VGQILEEPLLINtSLSAAERREKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQ 190

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 488386109 171 TEMQYELRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIYDEP 226
Cdd:PRK11308 191 AQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNP 246
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
2-227 3.47e-25

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 102.56  E-value: 3.47e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   2 ESLLSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKL--PANKRRVN 79
Cdd:PRK10575   9 DTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWssKAFARKVA 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  80 TVFQDYALFPHLNVYENIAFGL-----RLKKFSKQEIDKeVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPE 154
Cdd:PRK10575  89 YLPQQLPAAEGMTVRELVAIGRypwhgALGRFGAADREK-VEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSR 167

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488386109 155 ILLLDESLSALDLKLRTEMQYELRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIYDEPV 227
Cdd:PRK10575 168 CLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGET 240
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
 20-225 3.55e-25

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: 106.43  E-value: 3.55e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   20 LNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYK-----NQSIEKLPANKRRVNT----VFQDYALFPH 90
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvgdewVDMTKPGPDGRGRAKRyigiLHQEYDLYPH 379

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   91 LNVYENI--AFGLRLKKfskqeiDKEVKEALKLVKLTGYEQ--------RHIDEMSGGQKQRVAIARAIVNKPEILLLDE 160
Cdd:TIGR03269 380 RTVLDNLteAIGLELPD------ELARMKAVITLKMVGFDEekaeeildKYPDELSEGERHRVALAQVLIKEPRIVILDE 453

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488386109  161 SLSALDLKLRTEMQYELRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIYDE 225
Cdd:TIGR03269 454 PTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIVEE 518
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
 1-213 7.08e-25

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: 101.01  E-value: 7.08e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   1 MESLLSFKKVTKKF---DDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPAN--K 75
Cdd:cd03248    8 LKGIVKFQNVTFAYptrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKylH 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  76 RRVNTVFQDYALFPHlNVYENIAFGLRLKKFskqeidKEVKEALK-------LVKLTGYEQRHIDE----MSGGQKQRVA 144
Cdd:cd03248   88 SKVSLVGQEPVLFAR-SLQDNIAYGLQSCSF------ECVKEAAQkahahsfISELASGYDTEVGEkgsqLSGGQKQRVA 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488386109 145 IARAIVNKPEILLLDESLSALDLKLRTEMQYELRELQKRLgiTFIFVTHdQEEALALSDYIFVMKDGEI 213
Cdd:cd03248  161 IARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERR--TVLVIAH-RLSTVERADQILVLDGGRI 226
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
 7-194 7.60e-25

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 105.15  E-value: 7.60e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   7 FKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIY-KNQSIEKLPankrrvntvfQDY 85
Cdd:COG0488    1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIpKGLRIGYLP----------QEP 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  86 ALFPHLNVYENIAFGLR-----LKKFSK--QEIDKEVKEALKLVKLT-------GYE-------------------QRHI 132
Cdd:COG0488   71 PLDDDLTVLDTVLDGDAelralEAELEEleAKLAEPDEDLERLAELQeefealgGWEaearaeeilsglgfpeedlDRPV 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488386109 133 DEMSGGQKQRVAIARAIVNKPEILLLDESLSALDLklrtEMQYELRELQKRLGITFIFVTHD 194
Cdd:COG0488  151 SELSGGWRRRVALARALLSEPDLLLLDEPTNHLDL----ESIEWLEEFLKNYPGTVLVVSHD 208
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
 5-217 1.04e-24

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


Pssm-ID: 213180 [Multi-domain]  Cd Length: 194  Bit Score: 99.55  E-value: 1.04e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   5 LSFKKVTKKFD------DTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAG--FEQPNEGQIIYKNQSIEKlPANKR 76
Cdd:cd03213    4 LSFRNLTVTVKsspsksGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRPLDK-RSFRK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  77 RVNTVFQDYALFPHLNVYENIAFGLRLKKfskqeidkevkealklvkltgyeqrhideMSGGQKQRVAIARAIVNKPEIL 156
Cdd:cd03213   83 IIGYVPQDDILHPTLTVRETLMFAAKLRG-----------------------------LSGGERKRVSIALELVSNPSLL 133

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488386109 157 LLDESLSALD----LKLrteMQYeLRELQKrLGITFIFVTHD-QEEALALSDYIFVMKDGEIQQFG 217
Cdd:cd03213  134 FLDEPTSGLDsssaLQV---MSL-LRRLAD-TGRTIICSIHQpSSEIFELFDKLLLLSQGRVIYFG 194
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
 4-226 1.34e-24

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 102.24  E-value: 1.34e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   4 LLSFKKVTKKFDDTT-----ILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQI----IYKNQSIEKLPAN 74
Cdd:PRK13631  21 ILRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDKKNNHELI 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  75 --------------KRRVNTVFQ--DYALFPHlNVYENIAFGLRLKKFSKQEIDKEVKEALKLVKL-TGYEQRHIDEMSG 137
Cdd:PRK13631 101 tnpyskkiknfkelRRRVSMVFQfpEYQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLdDSYLERSPFGLSG 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 138 GQKQRVAIARAIVNKPEILLLDESLSALDLKLRTEMQyELRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFG 217
Cdd:PRK13631 180 GQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMM-QLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTG 258


                 ....*....
gi 488386109 218 TPTDIYDEP 226
Cdd:PRK13631 259 TPYEIFTDQ 267
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
 3-237 1.76e-24

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 100.35  E-value: 1.76e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   3 SLLSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPAN---KRRVN 79
Cdd:PRK10895   2 ATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHaraRRGIG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  80 TVFQDYALFPHLNVYENIAFGLRLKKFSKQEIDKEVKEALklvkltgYEQRHIDE--------MSGGQKQRVAIARAIVN 151
Cdd:PRK10895  82 YLPQEASIFRRLSVYDNLMAVLQIRDDLSAEQREDRANEL-------MEEFHIEHlrdsmgqsLSGGERRRVEIARALAA 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 152 KPEILLLDESLSALDLKLRTEMQYELRELQKRlGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIY-DEPVNRF 230
Cdd:PRK10895 155 NPKFILLDEPFAGVDPISVIDIKRIIEHLRDS-GLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILqDEHVKRV 233


                 ....*..
gi 488386109 231 vadFIGE 237
Cdd:PRK10895 234 ---YLGE 237
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
 5-212 2.97e-24

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: 98.31  E-value: 2.97e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   5 LSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIiyknqsieklpankrRVNTVFQD 84
Cdd:cd03250    6 ASFTWDSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSV---------------SVPGSIAY 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  85 YALFP-HLN--VYENIAFGlrlKKFSKQEIDKEVKE-ALK--LVKLTGYEQRHIDE----MSGGQKQRVAIARAIVNKPE 154
Cdd:cd03250   71 VSQEPwIQNgtIRENILFG---KPFDEERYEKVIKAcALEpdLEILPDGDLTEIGEkginLSGGQKQRISLARAVYSDAD 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 488386109 155 ILLLDESLSALDLKL-RTEMQYELRELqKRLGITFIFVTHdQEEALALSDYIFVMKDGE 212
Cdd:cd03250  148 IYLLDDPLSAVDAHVgRHIFENCILGL-LLNNKTRILVTH-QLQLLPHADQIVVLDNGR 204
SufC COG0396
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ...
 15-219 3.37e-24

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


Pssm-ID: 440165 [Multi-domain]  Cd Length: 245  Bit Score: 99.37  E-value: 3.37e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  15 DDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFE--QPNEGQIIYKNQSIEKLPANKR---RVNTVFQDYALFP 89
Cdd:COG0396   11 EGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDILELSPDERaraGIFLAFQYPVEIP 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  90 HLNVYE--NIAFG-LRLKKFSKQEIDKEVKEALKLVKL-TGYEQRHIDE-MSGGQKQRVAIARAIVNKPEILLLDESLSA 164
Cdd:COG0396   91 GVSVSNflRTALNaRRGEELSAREFLKLLKEKMKELGLdEDFLDRYVNEgFSGGEKKRNEILQMLLLEPKLAILDETDSG 170

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 165 LD---LKLRTEMQYELRELQKrlgiTFIFVTHdQEEALAL--SDYIFVMKDGEIQQFGTP 219
Cdd:COG0396  171 LDidaLRIVAEGVNKLRSPDR----GILIITH-YQRILDYikPDFVHVLVDGRIVKSGGK 225
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
1-213 6.13e-24

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 103.27  E-value: 6.13e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   1 MESLLSFKKVTKKF----DDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLP---- 72
Cdd:PRK10535   1 MTALLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDadal 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  73 ANKRR--VNTVFQDYALFPHLNVYENIAFGlrlKKFSKQEIDKEVKEALKLVKLTGYEQR---HIDEMSGGQKQRVAIAR 147
Cdd:PRK10535  81 AQLRRehFGFIFQRYHLLSHLTAAQNVEVP---AVYAGLERKQRLLRAQELLQRLGLEDRveyQPSQLSGGQQQRVSIAR 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488386109 148 AIVNKPEILLLDESLSALDLKLRTEMQYELRELQKRlGITFIFVTHDQEEAlALSDYIFVMKDGEI 213
Cdd:PRK10535 158 ALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHDPQVA-AQAERVIEIRDGEI 221
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
 15-194 7.96e-24

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: 102.44  E-value: 7.96e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   15 DDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPAN--KRRVNTVFQDYALFpHLN 92
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDevRRRVSVCAQDAHLF-DTT 424

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   93 VYENIAFGlrlkkfSKQEIDKEVKEALKLVKLTGYEQRHIDEM-----------SGGQKQRVAIARAIVNKPEILLLDES 161
Cdd:TIGR02868 425 VRENLRLA------RPDATDEELWAALERVGLADWLRALPDGLdtvlgeggarlSGGERQRLALARALLADAPILLLDEP 498

                         170       180       190
                  ....*....|....*....|....*....|....
gi 488386109  162 LSALDLKLRTEMqyeLRELQKRL-GITFIFVTHD 194
Cdd:TIGR02868 499 TEHLDAETADEL---LEDLLAALsGRTVVLITHH 529
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
 1-227 9.99e-24

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 102.05  E-value: 9.99e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   1 MESLLSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANKRR--- 77
Cdd:PRK15439   8 APPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHqlg 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  78 VNTVFQDYALFPHLNVYENIAFGLrlkkfSKQEIDKEVKEALkLVKLtgyeQRHID-EMSGG-----QKQRVAIARAIVN 151
Cdd:PRK15439  88 IYLVPQEPLLFPNLSVKENILFGL-----PKRQASMQKMKQL-LAAL----GCQLDlDSSAGslevaDRQIVEILRGLMR 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488386109 152 KPEILLLDESLSALDlKLRTEMQY-ELRELQKrLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIYDEPV 227
Cdd:PRK15439 158 DSRILILDEPTASLT-PAETERLFsRIRELLA-QGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDDI 232
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
 5-212 2.21e-23

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: 94.44  E-value: 2.21e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   5 LSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKnqsieklpankrrvntvfqd 84
Cdd:cd03221    1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG-------------------- 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  85 yalfPHLNVYeniafglrlkkfskqeidkevkealklvkltgyeqrHIDEMSGGQKQRVAIARAIVNKPEILLLDESLSA 164
Cdd:cd03221   61 ----STVKIG------------------------------------YFEQLSGGEKMRLALAKLLLENPNLLLLDEPTNH 100

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 488386109 165 LDLKLRTEMQYELRELQKrlgiTFIFVTHDQEEALALSDYIFVMKDGE 212
Cdd:cd03221  101 LDLESIEALEEALKEYPG----TVILVSHDRYFLDQVATKIIELEDGK 144
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
16-218 2.95e-23

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


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 100.94  E-value: 2.95e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  16 DTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIE--KLPANKRRVNTVFQDYALFPHlNV 93
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTklQLDSWRSRLAVVSQTPFLFSD-TV 405

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  94 YENIAFGLrlKKFSKQEIDKEVKEA------LKLVKltGYeQRHIDE----MSGGQKQRVAIARAIVNKPEILLLDESLS 163
Cdd:PRK10789 406 ANNIALGR--PDATQQEIEHVARLAsvhddiLRLPQ--GY-DTEVGErgvmLSGGQKQRISIARALLLNAEILILDDALS 480

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 488386109 164 ALDlkLRTEMQ--YELRelQKRLGITFIFVTHdQEEALALSDYIFVMKDGEIQQFGT 218
Cdd:PRK10789 481 AVD--GRTEHQilHNLR--QWGEGRTVIISAH-RLSALTEASEILVMQHGHIAQRGN 532
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
 1-226 3.64e-23

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 98.26  E-value: 3.64e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   1 MESLLSFKKVTKKFD----DTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPN---EGQIIYKNQSIEKLPA 73
Cdd:PRK09473   9 ADALLDVKDLRVTFStpdgDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNLPE 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  74 ---NKRR---VNTVFQD--YALFPHLNVYENIAFGLRL-KKFSKQEIDKEVKEALKLVKLTGYEQR-----HidEMSGGQ 139
Cdd:PRK09473  89 kelNKLRaeqISMIFQDpmTSLNPYMRVGEQLMEVLMLhKGMSKAEAFEESVRMLDAVKMPEARKRmkmypH--EFSGGM 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 140 KQRVAIARAIVNKPEILLLDESLSALDLKLRTEMQYELRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTP 219
Cdd:PRK09473 167 RQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNA 246


                 ....*..
gi 488386109 220 TDIYDEP 226
Cdd:PRK09473 247 RDVFYQP 253
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
 1-234 4.12e-23

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 96.72  E-value: 4.12e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   1 MESLLSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQsieklpankRRVNT 80
Cdd:PRK09544   1 MTSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK---------LRIGY 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  81 VFQDYALFPHLNVyeNIAFGLRLKKFSKqeiDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDE 160
Cdd:PRK09544  72 VPQKLYLDTTLPL--TVNRFLRLRPGTK---KEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDE 146

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488386109 161 SLSALDLKLRTEMQYELRELQKRLGITFIFVTHDQEEALALSDYIFVMkDGEIQQFGTPTDIYDEPvnRFVADF 234
Cdd:PRK09544 147 PTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCL-NHHICCSGTPEVVSLHP--EFISMF 217
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
 19-225 6.03e-23

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: 100.20  E-value: 6.03e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   19 ILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANKRR--VNTVFQDYALFPHlNVYEN 96
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRqfINYLPQEPYIFSG-SILEN 567

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   97 IAFGLRlKKFSKQEIDK-----EVKEALKLVKLtGYEQR---HIDEMSGGQKQRVAIARAIVNKPEILLLDESLSALDLK 168
Cdd:TIGR01193 568 LLLGAK-ENVSQDEIWAaceiaEIKDDIENMPL-GYQTElseEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTI 645

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 488386109  169 LRTEMQYELRELQKRlgiTFIFVTHDQEEAlALSDYIFVMKDGEIQQFGTPTDIYDE 225
Cdd:TIGR01193 646 TEKKIVNNLLNLQDK---TIIFVAHRLSVA-KQSDKIIVLDHGKIIEQGSHDELLDR 698
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
1-213 1.19e-22

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


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 94.95  E-value: 1.19e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   1 MESLLSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANK---RR 77
Cdd:PRK11614   2 EKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKimrEA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  78 VNTVFQDYALFPHLNVYENIAFGLRLKkfSKQEIDKEVKEALKLVKLTgYEQRH--IDEMSGGQKQRVAIARAIVNKPEI 155
Cdd:PRK11614  82 VAIVPEGRRVFSRMTVEENLAMGGFFA--ERDQFQERIKWVYELFPRL-HERRIqrAGTMSGGEQQMLAIGRALMSQPRL 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 488386109 156 LLLDESLSALDLKLRTEMQYELRELQKRlGITFIFVTHDQEEALALSDYIFVMKDGEI 213
Cdd:PRK11614 159 LLLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHV 215
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
1-261 1.51e-22

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 98.70  E-value: 1.51e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   1 MESLLSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLP---ANKRR 77
Cdd:PRK09700   2 ATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDhklAAQLG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  78 VNTVFQDYALFPHLNVYENIAFG-LRLKKF------SKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIV 150
Cdd:PRK09700  82 IGIIYQELSVIDELTVLENLYIGrHLTKKVcgvniiDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLM 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 151 NKPEILLLDESLSALDLKLRTEMQYELRELQKRlGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIYDEPV--- 227
Cdd:PRK09700 162 LDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIvrl 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 488386109 228 -------NRFVADFIGESNIVDGTMVKdfVVNIYGQDFECV 261
Cdd:PRK09700 241 mvgrelqNRFNAMKENVSNLAHETVFE--VRNVTSRDRKKV 279
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
 1-212 2.04e-22

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 98.08  E-value: 2.04e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   1 MESLLSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFeQPN---EGQIIYKNqsiEKLPANKRR 77
Cdd:PRK13549   2 MEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHgtyEGEIIFEG---EELQASNIR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  78 ------VNTVFQDYALFPHLNVYENIAFGLRLKKFSKQEIDKEVKEALKL---VKLTGYEQRHIDEMSGGQKQRVAIARA 148
Cdd:PRK13549  78 dteragIAIIHQELALVKELSVLENIFLGNEITPGGIMDYDAMYLRAQKLlaqLKLDINPATPVGNLGLGQQQLVEIAKA 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488386109 149 IVNKPEILLLDESLSALdlklrTEMQYE-----LRELQKRlGITFIFVTHDQEEALALSDYIFVMKDGE 212
Cdd:PRK13549 158 LNKQARLLILDEPTASL-----TESETAvlldiIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDGR 220
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
 4-212 2.75e-22

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: 97.97  E-value: 2.75e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109    4 LLSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFeQPN---EGQIIYKNQSIEK---LPANKRR 77
Cdd:TIGR02633   1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGV-YPHgtwDGEIYWSGSPLKAsniRDTERAG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   78 VNTVFQDYALFPHLNVYENIAFG----LRLKKFSKQEIDKEVKEALKLVKLTGY-EQRHIDEMSGGQKQRVAIARAIVNK 152
Cdd:TIGR02633  80 IVIIHQELTLVPELSVAENIFLGneitLPGGRMAYNAMYLRAKNLLRELQLDADnVTRPVGDYGGGQQQLVEIAKALNKQ 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488386109  153 PEILLLDESLSALDLKlRTEMQYEL-RELQKRlGITFIFVTHDQEEALALSDYIFVMKDGE 212
Cdd:TIGR02633 160 ARLLILDEPSSSLTEK-ETEILLDIiRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQ 218
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
 5-213 8.85e-22

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


Pssm-ID: 213214 [Multi-domain]  Cd Length: 178  Bit Score: 91.22  E-value: 8.85e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   5 LSFKKVTKKFD--DTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANKRRVNTVF 82
Cdd:cd03247    1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  83 QDYalfPHL---NVYENIafGLRLkkfskqeidkevkealklvkltgyeqrhidemSGGQKQRVAIARAIVNKPEILLLD 159
Cdd:cd03247   81 NQR---PYLfdtTLRNNL--GRRF--------------------------------SGGERQRLALARILLQDAPIVLLD 123

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 488386109 160 ESLSALDLKlrTEMQYeLRELQKRL-GITFIFVTHdQEEALALSDYIFVMKDGEI 213
Cdd:cd03247  124 EPTVGLDPI--TERQL-LSLIFEVLkDKTLIWITH-HLTGIEHMDKILFLENGKI 174
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
 5-213 1.27e-21

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: 91.05  E-value: 1.27e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   5 LSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFE--QPNEGQIIYKNQSIEKLPANKRRVNTV- 81
Cdd:cd03217    1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERARLGIf 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  82 --FQDYALFPhlnvyeniafGLRLKKFskqeidkevkealklvkltgyeQRHIDE-MSGGQKQRVAIARAIVNKPEILLL 158
Cdd:cd03217   81 laFQYPPEIP----------GVKNADF----------------------LRYVNEgFSGGEKKRNEILQLLLLEPDLAIL 128

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 488386109 159 DESLSALD---LKLRTEMQYELRElqkrLGITFIFVTHDQEEALAL-SDYIFVMKDGEI 213
Cdd:cd03217  129 DEPDSGLDidaLRLVAEVINKLRE----EGKSVLIITHYQRLLDYIkPDRVHVLYDGRI 183
cbiO PRK13646
energy-coupling factor transporter ATPase;
20-223 1.75e-21

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 92.92  E-value: 1.75e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  20 LNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANK------RRVNTVFQdyalFPHLNV 93
Cdd:PRK13646  23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKyirpvrKRIGMVFQ----FPESQL 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  94 YEN-----IAFGLrlKKFsKQEIDKEVKEALKLVKLTGYEQRHID----EMSGGQKQRVAIARAIVNKPEILLLDESLSA 164
Cdd:PRK13646  99 FEDtvereIIFGP--KNF-KMNLDEVKNYAHRLLMDLGFSRDVMSqspfQMSGGQMRKIAIVSILAMNPDIIVLDEPTAG 175

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 488386109 165 LDLKLRTEMQYELRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIY 223
Cdd:PRK13646 176 LDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELF 234
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
 4-225 1.79e-21

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 95.52  E-value: 1.79e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   4 LLSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIiyknqsieklpanKRRVNTVF- 82
Cdd:COG0488  315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV-------------KLGETVKIg 381

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  83 ---QDYALF-PHLNVYENIAfglrlkKFSKQEIDKEVKEALKLVKLTGYEQR-HIDEMSGGQKQRVAIARAIVNKPEILL 157
Cdd:COG0488  382 yfdQHQEELdPDKTVLDELR------DGAPGGTEQEVRGYLGRFLFSGDDAFkPVGVLSGGEKARLALAKLLLSPPNVLL 455

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488386109 158 LDE--------SLSALDLKLrteMQYElrelqkrlGiTFIFVTHDQE--EALAlsDYIFVMKDGEIQQF-GTptdiYDE 225
Cdd:COG0488  456 LDEptnhldieTLEALEEAL---DDFP--------G-TVLLVSHDRYflDRVA--TRILEFEDGGVREYpGG----YDD 516
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
 1-211 2.34e-21

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: 91.34  E-value: 2.34e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   1 MESLLSFKKVTKKF-----DDTTI--LNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYK--NQSIEKL 71
Cdd:COG4778    1 MTTLLEVENLSKTFtlhlqGGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdGGWVDLA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  72 PANKRRV-----NT---VFQdyalfpHLNV------YENIAFGLRLKKFSKQEIDKEVKEALklvkltgyEQRHIDE--- 134
Cdd:COG4778   81 QASPREIlalrrRTigyVSQ------FLRViprvsaLDVVAEPLLERGVDREEARARARELL--------ARLNLPErlw 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 135 ------MSGGQKQRVAIARAIVNKPEILLLDESLSALDLKLRT---EMqyeLRELQKRlGITFIFVTHDQEEALALSDYI 205
Cdd:COG4778  147 dlppatFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAvvvEL---IEEAKAR-GTAIIGIFHDEEVREAVADRV 222


                 ....*.
gi 488386109 206 FVMKDG 211
Cdd:COG4778  223 VDVTPF 228
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
 14-204 7.48e-21

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127 [Multi-domain]  Cd Length: 200  Bit Score: 89.24  E-value: 7.48e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  14 FDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEK-LPANKRRVNTVFQDYALFPHLN 92
Cdd:PRK13540  11 YHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKdLCTYQKQLCFVGHRSGINPYLT 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  93 VYENIAFGLRlkkFSKQEIdkEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDESLSALDLKLRTE 172
Cdd:PRK13540  91 LRENCLYDIH---FSPGAV--GITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLT 165

                        170       180       190
                 ....*....|....*....|....*....|..
gi 488386109 173 MQYELRELQKRLGItfIFVTHDQEEALALSDY 204
Cdd:PRK13540 166 IITKIQEHRAKGGA--VLLTSHQDLPLNKADY 195
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
 5-193 8.20e-21

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: 8.20e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109    5 LSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANKRRVNTvfqd 84
Cdd:TIGR01189   1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENIL---- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   85 Y-----ALFPHLNVYENIAFglrLKKFSKQEiDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLD 159
Cdd:TIGR01189  77 YlghlpGLKPELSALENLHF---WAAIHGGA-QRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILD 152

                         170       180       190
                  ....*....|....*....|....*....|....
gi 488386109  160 ESLSALDLKLRTEMQYELRELQKRLGITfIFVTH 193
Cdd:TIGR01189 153 EPTTALDKAGVALLAGLLRAHLARGGIV-LLTTH 185
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
 2-214 9.47e-21

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: 89.70  E-value: 9.47e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   2 ESLLSFKKvtKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQI-IYKNQSIEKLPANKRRVNT 80
Cdd:cd03267   21 GSLKSLFK--RKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVrVAGLVPWKRRKKFLRRIGV 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  81 VF-QDYALFPHLNVYENIAFGLRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLD 159
Cdd:cd03267   99 VFgQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLD 178

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 488386109 160 ESLSALDLKLRTEMQYELRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQ 214
Cdd:cd03267  179 EPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
 4-218 1.55e-20

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 92.97  E-value: 1.55e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   4 LLSFKKVTKKFDDTT--ILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLP--ANKRRVN 79
Cdd:PRK11160 338 SLTLNNVSFTYPDQPqpVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSeaALRQAIS 417

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  80 TVFQDYALFPHlNVYENIAFGlrlkkfSKQEIDKEVKEALKLVKLtgyeQRHIDE--------------MSGGQKQRVAI 145
Cdd:PRK11160 418 VVSQRVHLFSA-TLRDNLLLA------APNASDEALIEVLQQVGL----EKLLEDdkglnawlgeggrqLSGGEQRRLGI 486

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488386109 146 ARAIVNKPEILLLDESLSALDlkLRTEMQY--ELRELQKrlGITFIFVTHdQEEALALSDYIFVMKDGEIQQFGT 218
Cdd:PRK11160 487 ARALLHDAPLLLLDEPTEGLD--AETERQIleLLAEHAQ--NKTVLMITH-RLTGLEQFDRICVMDNGQIIEQGT 556
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
15-166 1.73e-20

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 88.32  E-value: 1.73e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  15 DDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIeklpankRRVNTVFQDYALF------ 88
Cdd:PRK13538  12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPI-------RRQRDEYHQDLLYlghqpg 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  89 --PHLNVYENIAFGLRLkkfsKQEIDKE-VKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDESLSAL 165
Cdd:PRK13538  85 ikTELTALENLRFYQRL----HGPGDDEaLWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAI 160


                 .
gi 488386109 166 D 166
Cdd:PRK13538 161 D 161
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
 10-237 2.45e-20

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 89.38  E-value: 2.45e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  10 VTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKL-------IAGFEQPNE----GQIIYKNQSIEKLpanKRRV 78
Cdd:PRK14271  27 LTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTlnrmndkVSGYRYSGDvllgGRSIFNYRDVLEF---RRRV 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  79 NTVFQDYALFPhLNVYENIAFGLRLKKFSKQEIDKEVKEA-LKLVKLTGYEQRHIDE----MSGGQKQRVAIARAIVNKP 153
Cdd:PRK14271 104 GMLFQRPNPFP-MSIMDNVLAGVRAHKLVPRKEFRGVAQArLTEVGLWDAVKDRLSDspfrLSGGQQQLLCLARTLAVNP 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 154 EILLLDESLSALDLKLRTEMQYELRELQKRLgiTFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIYDEP----VNR 229
Cdd:PRK14271 183 EVLLLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPkhaeTAR 260


                 ....*...
gi 488386109 230 FVADFIGE 237
Cdd:PRK14271 261 YVAGLSGD 268
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
 16-211 2.58e-20

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: 88.16  E-value: 2.58e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  16 DTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANKRRVNTVFQ-DYA----LFPH 90
Cdd:cd03290   13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSvAYAaqkpWLLN 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  91 LNVYENIAFGlrlKKFSKQEIdKEVKEALKL---VKLTGY-EQRHIDE----MSGGQKQRVAIARAIVNKPEILLLDESL 162
Cdd:cd03290   93 ATVEENITFG---SPFNKQRY-KAVTDACSLqpdIDLLPFgDQTEIGErginLSGGQRQRICVARALYQNTNIVFLDDPF 168

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 488386109 163 SALDLKLRTEMQYE--LRELQ--KRlgiTFIFVTHdQEEALALSDYIFVMKDG 211
Cdd:cd03290  169 SALDIHLSDHLMQEgiLKFLQddKR---TLVLVTH-KLQYLPHADWIIAMKDG 217
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
 15-218 7.46e-20

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 90.67  E-value: 7.46e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  15 DDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFeQPNEGQIIYKNQSIEKLPAN--KRRVNTVFQDYALFpHLN 92
Cdd:PRK11174 361 DGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELRELDPEswRKHLSWVGQNPQLP-HGT 438

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  93 VYENIAFGlrlkkfsKQEI-DKEVKEALKLVKLTGYEQRH-------IDE----MSGGQKQRVAIARAIVNKPEILLLDE 160
Cdd:PRK11174 439 LRDNVLLG-------NPDAsDEQLQQALENAWVSEFLPLLpqgldtpIGDqaagLSVGQAQRLALARALLQPCQLLLLDE 511

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 488386109 161 SLSALDlkLRTEmQYELRELQK-RLGITFIFVTHdQEEALALSDYIFVMKDGEIQQFGT 218
Cdd:PRK11174 512 PTASLD--AHSE-QLVMQALNAaSRRQTTLMVTH-QLEDLAQWDQIWVMQDGQIVQQGD 566
ycf16 CHL00131
sulfate ABC transporter protein; Validated
 3-220 1.00e-19

sulfate ABC transporter protein; Validated


Pssm-ID: 214372 [Multi-domain]  Cd Length: 252  Bit Score: 87.39  E-value: 1.00e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   3 SLLSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFE--QPNEGQIIYKNQSIEKLPANKRRVNT 80
Cdd:CHL00131   6 PILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPayKILEGDILFKGESILDLEPEERAHLG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  81 VFQDYALFPHLNVYENIAFgLRL------KKFSKQEID-----KEVKEALKLVKLTG-YEQRHIDE-MSGGQKQRVAIAR 147
Cdd:CHL00131  86 IFLAFQYPIEIPGVSNADF-LRLaynskrKFQGLPELDpleflEIINEKLKLVGMDPsFLSRNVNEgFSGGEKKRNEILQ 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 148 AIVNKPEILLLDESLSALD---LKLRTEMQYELRELQKrlgiTFIFVTHDQEealaLSDYI-----FVMKDGEIQQFGTP 219
Cdd:CHL00131 165 MALLDSELAILDETDSGLDidaLKIIAEGINKLMTSEN----SIILITHYQR----LLDYIkpdyvHVMQNGKIIKTGDA 236


                 .
gi 488386109 220 T 220
Cdd:CHL00131 237 E 237
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
4-229 1.05e-19

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 90.41  E-value: 1.05e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   4 LLSFKKVTKKFDDTT-ILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANKRRVN--T 80
Cdd:PRK13657 334 AVEFDDVSFSYDNSRqGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNiaV 413

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  81 VFQDYALFpHLNVYENIAFGlrlkkfSKQEIDKEVKEALK--------LVKLTGYEQrHIDE----MSGGQKQRVAIARA 148
Cdd:PRK13657 414 VFQDAGLF-NRSIEDNIRVG------RPDATDEEMRAAAEraqahdfiERKPDGYDT-VVGErgrqLSGGERQRLAIARA 485

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 149 IVNKPEILLLDESLSALDLKLRTEMQYELRELQK-RlgITFIFvthdqeeALALS-----DYIFVMKDGEIQQFGTptdi 222
Cdd:PRK13657 486 LLKDPPILILDEATSALDVETEAKVKAALDELMKgR--TTFII-------AHRLStvrnaDRILVFDNGRVVESGS---- 552


                 ....*..
gi 488386109 223 YDEPVNR 229
Cdd:PRK13657 553 FDELVAR 559
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
 37-213 1.20e-19

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: 85.18  E-value: 1.20e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  37 GPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANKRRVNTVF------QDYALFPHLNVYENIAFGLRLkkfskqe 110
Cdd:cd03215   33 GLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAyvpedrKREGLVLDLSVAENIALSSLL------- 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 111 idkevkealklvkltgyeqrhidemSGGQKQRVAIARAIVNKPEILLLDESLSALDLKLRTEMQYELRELQKRlGITFIF 190
Cdd:cd03215  106 -------------------------SGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADA-GKAVLL 159

                        170       180
                 ....*....|....*....|...
gi 488386109 191 VTHDQEEALALSDYIFVMKDGEI 213
Cdd:cd03215  160 ISSELDELLGLCDRILVMYEGRI 182
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
 19-219 1.28e-19

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: 85.93  E-value: 1.28e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  19 ILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANK--RRVNTVFQDYALFphlnvyen 96
Cdd:cd03369   23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDlrSSLTIIPQDPTLF-------- 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  97 iAFGLR--LKKFSKQEiDKEVKEALKlVKLTGyeqrhiDEMSGGQKQRVAIARAIVNKPEILLLDESLSALDLKLRTEMQ 174
Cdd:cd03369   95 -SGTIRsnLDPFDEYS-DEEIYGALR-VSEGG------LNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQ 165

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 488386109 175 YELRELQKrlGITFIFVTHdQEEALALSDYIFVMKDGEIQQFGTP 219
Cdd:cd03369  166 KTIREEFT--NSTILTIAH-RLRTIIDYDKILVMDAGEVKEYDHP 207
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
 18-220 1.88e-19

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


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 89.72  E-value: 1.88e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   18 TILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPN---EGQIIYKNQSIEKlPANKRRVNTVFQDYALFPHLNVY 94
Cdd:TIGR00955  39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDA-KEMRAISAYVQQDDLFIPTLTVR 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   95 ENIAFGLRLK------KFSKQEIDKEVKEALKLVK----LTGYEQRHiDEMSGGQKQRVAIARAIVNKPEILLLDESLSA 164
Cdd:TIGR00955 118 EHLMFQAHLRmprrvtKKEKRERVDEVLQALGLRKcantRIGVPGRV-KGLSGGERKRLAFASELLTDPPLLFCDEPTSG 196

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  165 LDlklrTEMQYELRELQKRL---GITFIFVTHD-QEEALALSDYIFVMKDGEIQQFGTPT 220
Cdd:TIGR00955 197 LD----SFMAYSVVQVLKGLaqkGKTIICTIHQpSSELFELFDKIILMAEGRVAYLGSPD 252
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
 15-166 1.98e-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: 85.24  E-value: 1.98e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  15 DDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSI-EKLPANKRRVNTVFQDYALFPHLNV 93
Cdd:cd03231   11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLdFQRDSIARGLLYLGHAPGIKTTLSV 90

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488386109  94 YENIAFglrlkkFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDESLSALD 166
Cdd:cd03231   91 LENLRF------WHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
 20-219 2.51e-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: 90.07  E-value: 2.51e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109    20 LNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIE-KLPANKRRVNTVFQDYALFPHLNVYENIA 98
Cdd:TIGR01257  946 VDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIEtNLDAVRQSLGMCPQHNILFHHLTVAEHIL 1025

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109    99 FGLRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDESLSALDLKLRTEMQYELr 178
Cdd:TIGR01257 1026 FYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL- 1104

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 488386109   179 eLQKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTP 219
Cdd:TIGR01257 1105 -LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
18-221 2.62e-19

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 86.48  E-value: 2.62e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  18 TILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKlPANKRRVNTVFQ----DYAlFPHLnV 93
Cdd:PRK15056  21 TALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ-ALQKNLVAYVPQseevDWS-FPVL-V 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  94 YENIAFG-------LRLKKFSKQEIdkeVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDESLSALD 166
Cdd:PRK15056  98 EDVVMMGryghmgwLRRAKKRDRQI---VTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVD 174

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 488386109 167 LKLRTEMQYELRELQKRlGITFIFVTHDQEEALALSDYIfVMKDGEIQQFGtPTD 221
Cdd:PRK15056 175 VKTEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCDYT-VMVKGTVLASG-PTE 226
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
 1-226 5.15e-19

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 85.36  E-value: 5.15e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   1 MESLLSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQS-----IEKLPANK 75
Cdd:PRK11701   3 DQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDgqlrdLYALSEAE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  76 RR--VNT----VFQDYA--LFPHLNVYENI-----AFGLR---------LKKFSKQEIDKEvkealklvkltgyeqrHID 133
Cdd:PRK11701  83 RRrlLRTewgfVHQHPRdgLRMQVSAGGNIgerlmAVGARhygdirataGDWLERVEIDAA----------------RID 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 134 EM----SGGQKQRVAIARAIVNKPEILLLDESLSALDLKLRTEMQYELRELQKRLGITFIFVTHDQEEALALSDYIFVMK 209
Cdd:PRK11701 147 DLpttfSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMK 226

                        250
                 ....*....|....*..
gi 488386109 210 DGEIQQFGTPTDIYDEP 226
Cdd:PRK11701 227 QGRVVESGLTDQVLDDP 243
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
 17-214 5.54e-19

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


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 84.62  E-value: 5.54e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  17 TTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFE--QPNEGQIiyknqsieklpankrrvntVFQDYALFPHLNVY 94
Cdd:COG2401   43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCV-------------------DVPDNQFGREASLI 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  95 ENIAfglrlkkfskqeIDKEVKEALKLVKLTGYEQ-----RHIDEMSGGQKQRVAIARAIVNKPEILLLDESLSALDLKL 169
Cdd:COG2401  104 DAIG------------RKGDFKDAVELLNAVGLSDavlwlRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQT 171

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 488386109 170 RTEMQYELRELQKRLGITFIFVTHDQEEALALSD--YIFVMKDGEIQ 214
Cdd:COG2401  172 AKRVARNLQKLARRAGITLVVATHHYDVIDDLQPdlLIFVGYGGVPE 218
PLN03211 PLN03211
ABC transporter G-25; Provisional
 11-166 8.69e-19

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 87.63  E-value: 8.69e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  11 TKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPN--EGQIIYKNQSIEKlpANKRRVNTVFQDYALF 88
Cdd:PLN03211  75 TRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTK--QILKRTGFVTQDDILY 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  89 PHLNVYENIAFG--LRL-KKFSKQE---IDKEVKEALKLVKL--TGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDE 160
Cdd:PLN03211 153 PHLTVRETLVFCslLRLpKSLTKQEkilVAESVISELGLTKCenTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDE 232


                 ....*.
gi 488386109 161 SLSALD 166
Cdd:PLN03211 233 PTSGLD 238
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
1-236 1.04e-18

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 87.27  E-value: 1.04e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   1 MESLLSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSI------EKLPAN 74
Cdd:PRK11288   1 SSPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfasttAALAAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  75 krrVNTVFQDYALFPHLNVYENIAFGLRLKKF---SKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVN 151
Cdd:PRK11288  81 ---VAIIYQELHLVPEMTVAENLYLGQLPHKGgivNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALAR 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 152 KPEILLLDE---SLSALDlklrTEMQYEL-RELQKRlGITFIFVTHDQEEALALSDYIFVMKDGeiQQFGTPTDIYDEPV 227
Cdd:PRK11288 158 NARVIAFDEptsSLSARE----IEQLFRViRELRAE-GRVILYVSHRMEEIFALCDAITVFKDG--RYVATFDDMAQVDR 230


                 ....*....
gi 488386109 228 NRFVADFIG 236
Cdd:PRK11288 231 DQLVQAMVG 239
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
 5-219 1.44e-18

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: 83.31  E-value: 1.44e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   5 LSFKKVTKKFDDT--TILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANK--RRVNT 80
Cdd:cd03244    3 IEFKNVSLRYRPNlpPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDlrSRISI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  81 VFQDYALFPHlNVYENIAFglrLKKFSkqeiDKEVKEALKLVKLTGyeqrHIDEMSG---------------GQKQRVAI 145
Cdd:cd03244   83 IPQDPVLFSG-TIRSNLDP---FGEYS----DEELWQALERVGLKE----FVESLPGgldtvveeggenlsvGQRQLLCL 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488386109 146 ARAIVNKPEILLLDESLSALDLKLRTEMQYELRElqKRLGITFIFVTHdQEEALALSDYIFVMKDGEIQQFGTP 219
Cdd:cd03244  151 ARALLRKSKILVLDEATASVDPETDALIQKTIRE--AFKDCTVLTIAH-RLDTIIDSDRILVLDKGRVVEFDSP 221
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
 22-226 1.49e-18

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 86.83  E-value: 1.49e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  22 NMNLDIESGYFYTLLGPSGCGKT----TILKLI--AGFEQPNEGQIIYK-NQSI----EKLPANKRRVN-----TVFQD- 84
Cdd:PRK10261  34 NLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqAGGLVQCDKMLLRRrSRQVielsEQSAAQMRHVRgadmaMIFQEp 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  85 -YALFPHLNVYENIAFGLRLKK-FSKQEIDKEVKEALKLVKLTGYEQ---RHIDEMSGGQKQRVAIARAIVNKPEILLLD 159
Cdd:PRK10261 114 mTSLNPVFTVGEQIAESIRLHQgASREEAMVEAKRMLDQVRIPEAQTilsRYPHQLSGGMRQRVMIAMALSCRPAVLIAD 193

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488386109 160 ESLSALDLKLRTEMQYELRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIYDEP 226
Cdd:PRK10261 194 EPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAP 260
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
 18-166 7.84e-18

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 81.07  E-value: 7.84e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  18 TILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEkLPANKRRVNTVFQDYALFPHLNVYENI 97
Cdd:PRK13539  16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDID-DPDVAEACHYLGHRNAMKPALTVAENL 94

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488386109  98 AFGLRLKKFSKQEIDkevkEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDESLSALD 166
Cdd:PRK13539  95 EFWAAFLGGEELDIA----AALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALD 159
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
 15-193 7.87e-18

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


Pssm-ID: 213190 [Multi-domain]  Cd Length: 166  Bit Score: 79.89  E-value: 7.87e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  15 DDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYknqsieklPANKrrvNTVF---QDYalFPHL 91
Cdd:cd03223   12 DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM--------PEGE---DLLFlpqRPY--LPLG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  92 NVYENIAFGLRlkkfskqeidkevkealklvkltgyeqrhiDEMSGGQKQRVAIARAIVNKPEILLLDESLSALDlklrT 171
Cdd:cd03223   79 TLREQLIYPWD------------------------------DVLSGGEQQRLAFARLLLHKPKFVFLDEATSALD----E 124

                        170       180
                 ....*....|....*....|..
gi 488386109 172 EMQYELRELQKRLGITFIFVTH 193
Cdd:cd03223  125 ESEDRLYQLLKELGITVISVGH 146
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 3-241 1.08e-17

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


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 82.83  E-value: 1.08e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   3 SLLSFKKVTKKfddttILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQI------IYKNQsieklPANKR 76
Cdd:COG4586   26 GLFRREYREVE-----AVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVrvlgyvPFKRR-----KEFAR 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  77 RVNTVF-QDYALFPHLNVYENiafgLRLKK----FSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVN 151
Cdd:COG4586   96 RIGVVFgQRSQLWWDLPAIDS----FRLLKaiyrIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLH 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 152 KPEILLLDESLSALDLKLRTEMQYELRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEIqqfgtptdIYDEPVNRFV 231
Cdd:COG4586  172 RPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRI--------IYDGSLEELK 243

                        250
                 ....*....|
gi 488386109 232 ADFIGESNIV 241
Cdd:COG4586  244 ERFGPYKTIV 253
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
40-213 1.54e-17

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 83.53  E-value: 1.54e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  40 GCGKTTILKLIAGFEQPNEGQIIYKNQSIEK-------------LPANKRRvntvfqdYALFPHLNVYENIAFGlRLKKF 106
Cdd:COG1129  288 GAGRTELARALFGADPADSGEIRLDGKPVRIrsprdairagiayVPEDRKG-------EGLVLDLSIRENITLA-SLDRL 359

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 107 SK------QEIDKEVKEALKL--VKLTGYEQRhIDEMSGGQKQRVAIARAIVNKPEILLLDESLSALDLKLRTEMqYEL- 177
Cdd:COG1129  360 SRgglldrRRERALAEEYIKRlrIKTPSPEQP-VGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEI-YRLi 437

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 488386109 178 RELQKRlGITFIFVTHDQEEALALSDYIFVMKDGEI 213
Cdd:COG1129  438 RELAAE-GKAVIVISSELPELLGLSDRILVMREGRI 472
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
 3-226 1.76e-16

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 79.40  E-value: 1.76e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   3 SLLSFKKVTKKFDDTTI----LNNMNLDIESGYFYTLLGPSGCGKT----TILKLIAGFEQPNEGQIIYKNQSIEKLPAN 74
Cdd:PRK11022   2 ALLNVDKLSVHFGDESApfraVDRISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISEK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  75 KRR------VNTVFQD--YALFPHLNVYENIAFGLRLKKF-SKQEIDKEVKEALKLVKLTGYEQR---HIDEMSGGQKQR 142
Cdd:PRK11022  82 ERRnlvgaeVAMIFQDpmTSLNPCYTVGFQIMEAIKVHQGgNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQR 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 143 VAIARAIVNKPEILLLDESLSALDLKLRTEMQYELRELQKRLGITFIFVTHDqeeaLAL----SDYIFVMKDGEIQQFGT 218
Cdd:PRK11022 162 VMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHD----LALvaeaAHKIIVMYAGQVVETGK 237


                 ....*...
gi 488386109 219 PTDIYDEP 226
Cdd:PRK11022 238 AHDIFRAP 245
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
 5-212 1.91e-16

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 81.23  E-value: 1.91e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109    5 LSFKKVTKKFD---DTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEK---LPANKRRV 78
Cdd:PTZ00265  383 IQFKNVRFHYDtrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKdinLKWWRSKI 462

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   79 NTVFQDYALFPHlNVYENIAFGLRLKK-------------FSKQE----------------------------------- 110
Cdd:PTZ00265  463 GVVSQDPLLFSN-SIKNNIKYSLYSLKdlealsnyynedgNDSQEnknkrnscrakcagdlndmsnttdsneliemrkny 541

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  111 ---IDKEVKEALKLVKLTGYEQRHIDE-----------MSGGQKQRVAIARAIVNKPEILLLDESLSALDLKLRTEMQYE 176
Cdd:PTZ00265  542 qtiKDSEVVDVSKKVLIHDFVSALPDKyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKT 621

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 488386109  177 LRELQKRLGITFIFVTHdQEEALALSDYIFVMKDGE 212
Cdd:PTZ00265  622 INNLKGNENRITIIIAH-RLSTIRYANTIFVLSNRE 656
3a01203 TIGR00954
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...
 19-193 2.28e-16

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: 80.56  E-value: 2.28e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   19 ILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGF--------EQPNEGQIIYknqsiekLPANKRRVNTVFQDYALFPh 90
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELwpvyggrlTKPAKGKLFY-------VPQRPYMTLGTLRDQIIYP- 538

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   91 lnvyeNIAFGLRLKKFSkqeiDKEVKEALKLVKLTGYEQRHI---------DEMSGGQKQRVAIARAIVNKPEILLLDES 161
Cdd:TIGR00954 539 -----DSSEDMKRRGLS----DKDLEQILDNVQLTHILEREGgwsavqdwmDVLSGGEKQRIAMARLFYHKPQFAILDEC 609

                         170       180       190
                  ....*....|....*....|....*....|..
gi 488386109  162 LSALDLklrtEMQYELRELQKRLGITFIFVTH 193
Cdd:TIGR00954 610 TSAVSV----DVEGYMYRLCREFGITLFSVSH 637
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
 18-211 2.57e-16

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 80.13  E-value: 2.57e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  18 TILNNMNLDIESGYFYTLLGPSGCGKT----TILKLIAG--FEQPnEGQIIYKNQSIekLPANKR--------RVNTVFQ 83
Cdd:PRK15134  23 TVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSppVVYP-SGDIRFHGESL--LHASEQtlrgvrgnKIAMIFQ 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  84 D--YALFPHLNVYENIAFGLRLKKFSKQEIDK-EVKEALKLVKLTGYEQRHID---EMSGGQKQRVAIARAIVNKPEILL 157
Cdd:PRK15134 100 EpmVSLNPLHTLEKQLYEVLSLHRGMRREAARgEILNCLDRVGIRQAAKRLTDyphQLSGGERQRVMIAMALLTRPELLI 179

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488386109 158 LDESLSALDLKLRTEMQYELRELQKRLGITFIFVTHDQEEALALSDYIFVMKDG 211
Cdd:PRK15134 180 ADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNG 233
PRK13543 PRK13543
heme ABC exporter ATP-binding protein CcmA;
4-167 3.78e-16

heme ABC exporter ATP-binding protein CcmA;


Pssm-ID: 184129 [Multi-domain]  Cd Length: 214  Bit Score: 76.43  E-value: 3.78e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   4 LLSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIiyknqSIEKLPaNKRRVNTVFQ 83
Cdd:PRK13543  11 LLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQI-----QIDGKT-ATRGDRSRFM 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  84 DY-----ALFPHLNVYENIAFGLRLKKFSKQEIDKEvkeALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLL 158
Cdd:PRK13543  85 AYlghlpGLKADLSTLENLHFLCGLHGRRAKQMPGS---ALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLL 161


                 ....*....
gi 488386109 159 DESLSALDL 167
Cdd:PRK13543 162 DEPYANLDL 170
PRK10522 PRK10522
multidrug transporter membrane component/ATP-binding component; Provisional
 5-215 3.82e-16

multidrug transporter membrane component/ATP-binding component; Provisional


Pssm-ID: 236707 [Multi-domain]  Cd Length: 547  Bit Score: 79.63  E-value: 3.82e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   5 LSFKKVTKKFDDTTI-LNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQ--SIEKLPANKRRVNTV 81
Cdd:PRK10522 323 LELRNVTFAYQDNGFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKpvTAEQPEDYRKLFSAV 402

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  82 FQDYALFPHLnvyeniafglrLKKFSKQEIDKEVK---EALKLV-KLTGYEQRHID-EMSGGQKQRVAIARAIVNKPEIL 156
Cdd:PRK10522 403 FTDFHLFDQL-----------LGPEGKPANPALVEkwlERLKMAhKLELEDGRISNlKLSKGQKKRLALLLALAEERDIL 471

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 488386109 157 LLDESLSALDLKLRTEMQYELRELQKRLGITFIFVTHDqEEALALSDYIFVMKDGEIQQ 215
Cdd:PRK10522 472 LLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQLSE 529
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
11-222 4.03e-16

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 79.78  E-value: 4.03e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  11 TKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEklpAN----KRRVNTVFQDYA 86
Cdd:NF033858 273 TMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVD---AGdiatRRRVGYMSQAFS 349

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  87 LFPHLNVYENIAFGLRLKKFSKQEIDKEVKEALKLVKLTGYeqrhIDEMSG----GQKQRVAIARAIVNKPEILLLDESL 162
Cdd:NF033858 350 LYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADV----ADALPDslplGIRQRLSLAVAVIHKPELLILDEPT 425

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488386109 163 SALDLKLRTEMQYELRELQKRLGITfIFV-THDQEEAlALSDYIFVMKDGEIQQFGTPTDI 222
Cdd:NF033858 426 SGVDPVARDMFWRLLIELSREDGVT-IFIsTHFMNEA-ERCDRISLMHAGRVLASDTPAAL 484
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
 15-218 4.42e-16

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: 79.99  E-value: 4.42e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109    15 DDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNqSIEKLPANKRRVNTVFQdyalfphlnvy 94
Cdd:TIGR00957  649 DLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-SVAYVPQQAWIQNDSLR----------- 716

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109    95 ENIAFGLRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDE----MSGGQKQRVAIARAIVNKPEILLLDESLSALDLKLR 170
Cdd:TIGR00957  717 ENILFGKALNEKYYQQVLEACALLPDLEILPSGDRTEIGEkgvnLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVG 796

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 488386109   171 TEMQYELRELQKRL-GITFIFVTHDQeEALALSDYIFVMKDGEIQQFGT 218
Cdd:TIGR00957  797 KHIFEHVIGPEGVLkNKTRILVTHGI-SYLPQVDVIIVMSGGKISEMGS 844
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
 12-217 5.21e-16

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: 75.76  E-value: 5.21e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  12 KKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPN---EGQIIYKNQSIEKLpANKRRVNTVF--QDYA 86
Cdd:cd03233   15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEF-AEKYPGEIIYvsEEDV 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  87 LFPHLNVYENIAFGLRLKKfskqeidkevkealklvkltgyeqrhiDEM----SGGQKQRVAIARAIVNKPEILLLDESL 162
Cdd:cd03233   94 HFPTLTVRETLDFALRCKG---------------------------NEFvrgiSGGERKRVSIAEALVSRASVLCWDNST 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 488386109 163 SALDLKLRTEMQYELRELQKRLGITfIFVTHDQ--EEALALSDYIFVMKDGEIQQFG 217
Cdd:cd03233  147 RGLDSSTALEILKCIRTMADVLKTT-TFVSLYQasDEIYDLFDKVLVLYEGRQIYYG 202
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
15-218 7.68e-16

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


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 78.61  E-value: 7.68e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  15 DDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLP--ANKRRVNTVFQDYALFPHlN 92
Cdd:PRK10790 352 DDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLShsVLRQGVAMVQQDPVVLAD-T 430

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  93 VYENIAFGlrlkkfskQEIDKE-VKEALKLVKLT--------GYEQRhIDE----MSGGQKQRVAIARAIVNKPEILLLD 159
Cdd:PRK10790 431 FLANVTLG--------RDISEEqVWQALETVQLAelarslpdGLYTP-LGEqgnnLSVGQKQLLALARVLVQTPQILILD 501

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 488386109 160 ESLSALDLKLRTEMQYELRELQKRlgITFIFVTHdQEEALALSDYIFVMKDGEIQQFGT 218
Cdd:PRK10790 502 EATANIDSGTEQAIQQALAAVREH--TTLVVIAH-RLSTIVEADTILVLHRGQAVEQGT 557
BtuD COG4138
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ...
 35-225 8.82e-16

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


Pssm-ID: 443313 [Multi-domain]  Cd Length: 248  Bit Score: 76.03  E-value: 8.82e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  35 LLGPSGCGKTTILKLIAGFeQPNEGQIIYKNQSIEKLPAN---KRRVNTVFQDYALFPhLNVYENIAFGLRlKKFSKQEI 111
Cdd:COG4138   27 LIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSAAelaRHRAYLSQQQSPPFA-MPVFQYLALHQP-AGASSEAV 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 112 DK---EVKEALKLV-KLTgyeqRHIDEMSGGQKQRVAIARAI------VNkPE--ILLLDESLSALD-------LKLrte 172
Cdd:COG4138  104 EQllaQLAEALGLEdKLS----RPLTQLSGGEWQRVRLAAVLlqvwptIN-PEgqLLLLDEPMNSLDvaqqaalDRL--- 175

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 488386109 173 mqyeLRELqKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIYDE 225
Cdd:COG4138  176 ----LREL-CQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMTP 223
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
 7-217 1.53e-15

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


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 78.23  E-value: 1.53e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109     7 FKKVTKKFDDTT--ILNNMNLDIESGYFYTLLGPSGCGKTTILKLIA----GFEQPNEGQIIYKNQSIEKLPANKR-RVN 79
Cdd:TIGR00956   62 FRKLKKFRDTKTfdILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEEIKKHYRgDVV 141

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109    80 TVFQDYALFPHLNVYENIAF-------GLRLKKFSKQEIDKEVKEalklVKLTGYEQRHI------DEM----SGGQKQR 142
Cdd:TIGR00956  142 YNAETDVHFPHLTVGETLDFaarcktpQNRPDGVSREEYAKHIAD----VYMATYGLSHTrntkvgNDFvrgvSGGERKR 217

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488386109   143 VAIARAIVNKPEILLLDESLSALDLKLRTEMQYELRElQKRLGITFIFVTHDQ--EEALALSDYIFVMKDGEIQQFG 217
Cdd:TIGR00956  218 VSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKT-SANILDTTPLVAIYQcsQDAYELFDKVIVLYEGYQIYFG 293
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 2-205 2.27e-15

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: 77.13  E-value: 2.27e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   2 ESLLSFKKVTKKFDDTTilnnmnLDIESGYFY-----TLLGPSGCGKTTILKLIAGFEQPNEGQII------YKNQSIEk 70
Cdd:COG1245  339 ETLVEYPDLTKSYGGFS------LEVEGGEIRegevlGIVGPNGIGKTTFAKILAGVLKPDEGEVDedlkisYKPQYIS- 411

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  71 lpankrrvntvfQDYalfpHLNVYENiafglrLKKFSKQEID-----KEVKEALKLVKLtgYEQRhIDEMSGGQKQRVAI 145
Cdd:COG1245  412 ------------PDY----DGTVEEF------LRSANTDDFGssyykTEIIKPLGLEKL--LDKN-VKDLSGGELQRVAI 466

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 146 ARAIVNKPEILLLDESLSALDLKLRTEMQYELRELQKRLGITFIFVTHDqeeaLALSDYI 205
Cdd:COG1245  467 AACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHD----IYLIDYI 522
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
 10-212 3.56e-15

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 76.31  E-value: 3.56e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  10 VTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIE---KLPANKRRVNTVFQDYA 86
Cdd:PRK10982   4 ISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfksSKEALENGISMVHQELN 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  87 LFPHLNVYENIAFGLRLKKFSKQEIDKEVKEALKLVKLTGYE---QRHIDEMSGGQKQRVAIARAIVNKPEILLLDESLS 163
Cdd:PRK10982  84 LVLQRSVMDNMWLGRYPTKGMFVDQDKMYRDTKAIFDELDIDidpRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTS 163

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 488386109 164 ALDLKLRTEMQYELRELQKRlGITFIFVTHDQEEALALSDYIFVMKDGE 212
Cdd:PRK10982 164 SLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDGQ 211
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
 35-240 6.69e-15

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: 73.55  E-value: 6.69e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  35 LLGPSGCGKTTILKLIAGFEQPNEGQ---------II--YKNQSI----EKLPANKRRVNTVFQDYALFPHlNVYENIaf 99
Cdd:cd03236   31 LVGPNGIGKSTALKILAGKLKPNLGKfddppdwdeILdeFRGSELqnyfTKLLEGDVKVIVKPQYVDLIPK-AVKGKV-- 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 100 GLRLKKFSKQEIDKEVKEALKLVKLTgyeQRHIDEMSGGQKQRVAIARAIVNKPEILLLDESLSALDLKLRTEMQYELRE 179
Cdd:cd03236  108 GELLKKKDERGKLDELVDQLELRHVL---DRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRE 184

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488386109 180 LQKRlGITFIFVTHDQEEALALSDYIFVMKdGEIQQFG--TPTDIYDEPVNRFVADFIGESNI 240
Cdd:cd03236  185 LAED-DNYVLVVEHDLAVLDYLSDYIHCLY-GEPGAYGvvTLPKSVREGINEFLDGYLPTENM 245
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 35-208 7.02e-15

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: 75.59  E-value: 7.02e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  35 LLGPSGCGKTTILKLIAGFEQPNEGqiIYKNqsieklPANKRRVNTVFQDYALFPHL-NVYENiafglRLKKFSK-QEID 112
Cdd:COG1245  104 ILGPNGIGKSTALKILSGELKPNLG--DYDE------EPSWDEVLKRFRGTELQDYFkKLANG-----EIKVAHKpQYVD 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 113 K-------EVKEALK----------LVKLTGYEQ---RHIDEMSGGQKQRVAIARAIVNKPEILLLDESLSALDLKLRTE 172
Cdd:COG1245  171 LipkvfkgTVRELLEkvdergkldeLAEKLGLENildRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLN 250

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 488386109 173 MQYELRELQKRlGITFIFVTHDqeeaLA----LSDYIFVM 208
Cdd:COG1245  251 VARLIRELAEE-GKYVLVVEHD----LAildyLADYVHIL 285
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
 5-166 1.11e-14

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


Pssm-ID: 274744 [Multi-domain]  Cd Length: 552  Bit Score: 74.97  E-value: 1.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109    5 LSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEG--------QIIYKNQSIEKLPANKr 76
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGtieigetvKLAYVDQSRDALDPNK- 401

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   77 rvntvfqdyalfphlNVYENIAFGLRLKKFSKQEIDKevKEALKLVKLTGYEQ-RHIDEMSGGQKQRVAIARAIVNKPEI 155
Cdd:TIGR03719 402 ---------------TVWEEISGGLDIIKLGKREIPS--RAYVGRFNFKGSDQqKKVGQLSGGERNRVHLAKTLKSGGNV 464

                         170
                  ....*....|.
gi 488386109  156 LLLDESLSALD 166
Cdd:TIGR03719 465 LLLDEPTNDLD 475
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
 5-225 1.46e-14

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 74.54  E-value: 1.46e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   5 LSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIY-KNQSIEKLPankrrvntvfQ 83
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWsENANIGYYA----------Q 389

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  84 DYAL-FPH-LNVYENIA---------------FGLRLkkFSKQEIDKEVKealklvkltgyeqrhidEMSGGQKQRVAIA 146
Cdd:PRK15064 390 DHAYdFENdLTLFDWMSqwrqegddeqavrgtLGRLL--FSQDDIKKSVK-----------------VLSGGEKGRMLFG 450

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 147 RAIVNKPEILLLD--------ESLSALDLKLRtemQYElrelqkrlGiTFIFVTHDQEEALALSDYIFVMKDGEIQQF-G 217
Cdd:PRK15064 451 KLMMQKPNVLVMDeptnhmdmESIESLNMALE---KYE--------G-TLIFVSHDREFVSSLATRIIEITPDGVVDFsG 518


                 ....*...
gi 488386109 218 TptdiYDE 225
Cdd:PRK15064 519 T----YEE 522
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
 1-242 1.73e-14

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 74.27  E-value: 1.73e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   1 MESLLSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIE-KLPANKRR-- 77
Cdd:PRK10762   1 MQALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfNGPKSSQEag 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  78 VNTVFQDYALFPHLNVYENIAFGLRLK-KFSKQEIDKEVKEALKLVK---LTGYEQRHIDEMSGGQKQRVAIARAIVNKP 153
Cdd:PRK10762  81 IGIIHQELNLIPQLTIAENIFLGREFVnRFGRIDWKKMYAEADKLLArlnLRFSSDKLVGELSIGEQQMVEIAKVLSFES 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 154 EILLLDESLSALDlklRTEMQ------YELRElQKRlGITFIfvTHDQEEALALSDYIFVMKDGEiqqfgtptdiydepv 227
Cdd:PRK10762 161 KVIIMDEPTDALT---DTETEslfrviRELKS-QGR-GIVYI--SHRLKEIFEICDDVTVFRDGQ--------------- 218

                        250
                 ....*....|....*
gi 488386109 228 nrfvadFIGESNIVD 242
Cdd:PRK10762 219 ------FIAEREVAD 227
PLN03130 PLN03130
ABC transporter C family member; Provisional
 20-218 1.86e-14

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 75.16  E-value: 1.86e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   20 LNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPankrRVNTVFqdyalfpHLNVYENIAF 99
Cdd:PLN03130  633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVVIRGTVAYVP----QVSWIF-------NATVRDNILF 701

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  100 GLrlkKFSKQEIDKEVK-EALK--LVKLTGYEQRHIDE----MSGGQKQRVAIARAIVNKPEILLLDESLSALDLKL-RT 171
Cdd:PLN03130  702 GS---PFDPERYERAIDvTALQhdLDLLPGGDLTEIGErgvnISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVgRQ 778

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 488386109  172 EMQYELR-ELQKRlgiTFIFVThDQEEALALSDYIFVMKDGEIQQFGT 218
Cdd:PLN03130  779 VFDKCIKdELRGK---TRVLVT-NQLHFLSQVDRIILVHEGMIKEEGT 822
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
2-233 1.88e-14

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 74.46  E-value: 1.88e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   2 ESLLSFKKVTKKFDDTTilnnmnLDIESGYFY-----TLLGPSGCGKTTILKLIAGFEQPNEGQII------YKNQSIEk 70
Cdd:PRK13409 338 ETLVEYPDLTKKLGDFS------LEVEGGEIYegeviGIVGPNGIGKTTFAKLLAGVLKPDEGEVDpelkisYKPQYIK- 410

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  71 lPANKRRVntvfqdYALFphlnvyENIAfglrlKKFSKQEIDKEVKEALKLVKLtgYEQRhIDEMSGGQKQRVAIARAIV 150
Cdd:PRK13409 411 -PDYDGTV------EDLL------RSIT-----DDLGSSYYKSEIIKPLQLERL--LDKN-VKDLSGGELQRVAIAACLS 469

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 151 NKPEILLLDESLSALDLKLRTEMQYELRELQKRLGITFIFVTHDqeeaLALSDYI---FVMKDGEIQQFGT---PTDIyD 224
Cdd:PRK13409 470 RDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHD----IYMIDYIsdrLMVFEGEPGKHGHasgPMDM-R 544


                 ....*....
gi 488386109 225 EPVNRFVAD 233
Cdd:PRK13409 545 EGMNRFLKE 553
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
35-208 2.88e-14

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 74.07  E-value: 2.88e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  35 LLGPSGCGKTTILKLIAGFEQPN------------------------------EGQI--IYKNQSIEKLP-ANKRRVNTV 81
Cdd:PRK13409 104 ILGPNGIGKTTAVKILSGELIPNlgdyeeepswdevlkrfrgtelqnyfkklyNGEIkvVHKPQYVDLIPkVFKGKVREL 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  82 fqdyalfphlnvyeniafglrLKKFSKQEIDKEVKEALKLVKLTGyeqRHIDEMSGGQKQRVAIARAIVNKPEILLLDES 161
Cdd:PRK13409 184 ---------------------LKKVDERGKLDEVVERLGLENILD---RDISELSGGELQRVAIAAALLRDADFYFFDEP 239

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 488386109 162 LSALDLKLRTEMQYELRELQKrlGITFIFVTHDqeeaLA----LSDYIFVM 208
Cdd:PRK13409 240 TSYLDIRQRLNVARLIRELAE--GKYVLVVEHD----LAvldyLADNVHIA 284
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
 4-216 3.77e-14

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 73.67  E-value: 3.77e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   4 LLSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQI---------IYKNQSIEKLPAn 74
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIglakgiklgYFAQHQLEFLRA- 390

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  75 krrvntvfqDYALFPHLNvyeniafglrlkKFSKQEIDKEVKEALKLVKLTGYEQRHIDE-MSGGQKQRVAIARAIVNKP 153
Cdd:PRK10636 391 ---------DESPLQHLA------------RLAPQELEQKLRDYLGGFGFQGDKVTEETRrFSGGEKARLVLALIVWQRP 449

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488386109 154 EILLLDESLSALDLKLRTEMQYELRELQKRLgitfIFVTHDQEEALALSDYIFVMKDGEIQQF 216
Cdd:PRK10636 450 NLLLLDEPTNHLDLDMRQALTEALIDFEGAL----VVVSHDRHLLRSTTDDLYLVHDGKVEPF 508
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
 20-232 6.56e-14

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: 70.51  E-value: 6.56e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  20 LNNMNLDIESGYFY-----TLLGPSGCGKTTILKLIAGFEQPNEGQII-------YKNQSIEklPANKRRVntvfqDYAL 87
Cdd:cd03237   10 LGEFTLEVEGGSISeseviGILGPNGIGKTTFIKMLAGVLKPDEGDIEieldtvsYKPQYIK--ADYEGTV-----RDLL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  88 FPHLNvyeniafglrlKKFSKQEIDKEVKEALKLVKLtgYEQRhIDEMSGGQKQRVAIARAIVNKPEILLLDESLSALDL 167
Cdd:cd03237   83 SSITK-----------DFYTHPYFKTEIAKPLQIEQI--LDRE-VPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDV 148

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488386109 168 KLRTEMQYELRELQKRLGITFIFVTHDQEEALALSDYIFVMkDGEIQQFGT--PTDIYDEPVNRFVA 232
Cdd:cd03237  149 EQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIVF-EGEPSVNGVanPPQSLRSGMNRFLK 214
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
 4-218 9.49e-14

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: 72.74  E-value: 9.49e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109     4 LLSFKKVTKKFDDTT--ILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKlpankrRVNTV 81
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT------NISDV 2010

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109    82 FQDYALFPHLNVYENIAFG-------LRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPE 154
Cdd:TIGR01257 2011 HQNMGYCPQFDAIDDLLTGrehlylyARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPP 2090

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488386109   155 ILLLDESLSALDLKLRtEMQYELRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGT 218
Cdd:TIGR01257 2091 LVLLDEPTTGMDPQAR-RMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGT 2153
GguA NF040905
sugar ABC transporter ATP-binding protein;
4-211 9.81e-14

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 72.13  E-value: 9.81e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   4 LLSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFeQPN---EGQIIYKNQSIE--KLPANKRR- 77
Cdd:NF040905   1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGV-YPHgsyEGEILFDGEVCRfkDIRDSEALg 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  78 VNTVFQDYALFPHLNVYENIAFGLRLKKF---SKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPE 154
Cdd:NF040905  80 IVIIHQELALIPYLSIAENIFLGNERAKRgviDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVK 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488386109 155 ILLLDESLSALD-------LKLrtemqyeLRELQKRlGITFIFVTHDQEEALALSDYIFVMKDG 211
Cdd:NF040905 160 LLILDEPTAALNeedsaalLDL-------LLELKAQ-GITSIIISHKLNEIRRVADSITVLRDG 215
hmuV PRK13547
heme ABC transporter ATP-binding protein;
18-222 1.18e-13

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 70.24  E-value: 1.18e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  18 TILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAG----FEQPN----EGQIIYKNQSIEKLPANK-RRVNTVFQDYA-- 86
Cdd:PRK13547  15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdltgGGAPRgarvTGDVTLNGEPLAAIDAPRlARLRAVLPQAAqp 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  87 LFPhLNVYENIAFG-----LRLKKFSKQeiDKEVK-EALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVN--------- 151
Cdd:PRK13547  95 AFA-FSAREIVLLGryphaRRAGALTHR--DGEIAwQALALAGATALVGRDVTTLSGGELARVQFARVLAQlwpphdaaq 171

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488386109 152 KPEILLLDESLSALDLKLRTEMQYELRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDI 222
Cdd:PRK13547 172 PPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADV 242
PLN03232 PLN03232
ABC transporter C family member; Provisional
 20-218 2.19e-13

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 71.55  E-value: 2.19e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   20 LNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPankrRVNTVFqdyalfpHLNVYENIAF 99
Cdd:PLN03232  633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVVIRGSVAYVP----QVSWIF-------NATVRENILF 701

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  100 GlrlKKFSKQEIDKEVK-EALK--LVKLTGYEQRHIDE----MSGGQKQRVAIARAIVNKPEILLLDESLSALDLKLRTE 172
Cdd:PLN03232  702 G---SDFESERYWRAIDvTALQhdLDLLPGRDLTEIGErgvnISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQ 778

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 488386109  173 -----MQYELRelqkrlGITFIFVThDQEEALALSDYIFVMKDGEIQQFGT 218
Cdd:PLN03232  779 vfdscMKDELK------GKTRVLVT-NQLHFLPLMDRIILVSEGMIKEEGT 822
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
 6-194 2.84e-13

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


Pssm-ID: 274744 [Multi-domain]  Cd Length: 552  Bit Score: 70.73  E-value: 2.84e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109    6 SFKKVTKKFD-DTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGqiiyknqsiEKLPANKRRVNTVFQD 84
Cdd:TIGR03719   6 TMNRVSKVVPpKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNG---------EARPQPGIKVGYLPQE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   85 YALFPHLNVYENIAFGLRLKKFSKQEIDkEVKEAL--------KLVKLTGYEQRHID----------------------- 133
Cdd:TIGR03719  77 PQLDPTKTVRENVEEGVAEIKDALDRFN-EISAKYaepdadfdKLAAEQAELQEIIDaadawdldsqleiamdalrcppw 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488386109  134 -----EMSGGQKQRVAIARAIVNKPEILLLDESLSALDLKLRTEMQYELRELQKrlgiTFIFVTHD 194
Cdd:TIGR03719 156 dadvtKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPG----TVVAVTHD 217
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
 3-194 1.02e-12

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 69.21  E-value: 1.02e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   3 SLLSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGfEQP-NEGQIIY-KNQSIEKLPANKRR--V 78
Cdd:PRK11147   2 SLISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNG-EVLlDDGRIIYeQDLIVARLQQDPPRnvE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  79 NTVFqDY------ALFPHLNVYENIAFGLR-------LKKFSK-QEI---------DKEVKEALKLVKLTGYEQrhIDEM 135
Cdd:PRK11147  81 GTVY-DFvaegieEQAEYLKRYHDISHLVEtdpseknLNELAKlQEQldhhnlwqlENRINEVLAQLGLDPDAA--LSSL 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 488386109 136 SGGQKQRVAIARAIVNKPEILLLDESLSALDLklrTEMQYeLRELQKRLGITFIFVTHD 194
Cdd:PRK11147 158 SGGWLRKAALGRALVSNPDVLLLDEPTNHLDI---ETIEW-LEGFLKTFQGSIIFISHD 212
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
 19-222 1.23e-12

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: 69.20  E-value: 1.23e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109    19 ILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANKRR--VNTVFQDYALFPHlnvyen 96
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRfkITIIPQDPVLFSG------ 1374

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109    97 iAFGLRLKKFSkQEIDKEVKEALKLVKLTGYEQRHIDEM-----------SGGQKQRVAIARAIVNKPEILLLDESLSAL 165
Cdd:TIGR00957 1375 -SLRMNLDPFS-QYSDEEVWWALELAHLKTFVSALPDKLdhecaeggenlSVGQRQLVCLARALLRKTKILVLDEATAAV 1452

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 488386109   166 DLKLRTEMQYELRelQKRLGITFIFVTHDQEealALSDY--IFVMKDGEIQQFGTPTDI 222
Cdd:TIGR00957 1453 DLETDNLIQSTIR--TQFEDCTVLTIAHRLN---TIMDYtrVIVLDKGEVAEFGAPSNL 1506
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
2-221 1.38e-12

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 68.66  E-value: 1.38e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   2 ESLLSFKKVTKKfdDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIE---KLPANKRRV 78
Cdd:PRK09700 263 ETVFEVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISprsPLDAVKKGM 340

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  79 NTVFQ---DYALFPHLNVYENIAFGLRLKK---------FSKQEIDKEVKEALKL--VKLTGYEQrHIDEMSGGQKQRVA 144
Cdd:PRK09700 341 AYITEsrrDNGFFPNFSIAQNMAISRSLKDggykgamglFHEVDEQRTAENQRELlaLKCHSVNQ-NITELSGGNQQKVL 419

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488386109 145 IARAIVNKPEILLLDESLSALDLKLRTEMQYELRELQKRlGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTD 221
Cdd:PRK09700 420 ISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRD 495
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
10-222 1.61e-12

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 68.61  E-value: 1.61e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  10 VTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIeklpANKRRVNTVFQDYA--- 86
Cdd:NF033858   7 VSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDM----ADARHRRAVCPRIAymp 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  87 ------LFPHLNVYENIAFGLRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDE 160
Cdd:NF033858  83 qglgknLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDE 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488386109 161 SLSALD-LKLRtemQY-----ELRelQKRLGITFIFVTHDQEEAlALSDYIFVMKDGEIQQFGTPTDI 222
Cdd:NF033858 163 PTTGVDpLSRR---QFwelidRIR--AERPGMSVLVATAYMEEA-ERFDWLVAMDAGRVLATGTPAEL 224
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
 17-225 1.84e-12

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: 66.80  E-value: 1.84e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  17 TTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNqsieklpankrRVNTVFQDYALFPHlNVYEN 96
Cdd:cd03291   50 APVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-----------RISFSSQFSWIMPG-TIKEN 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  97 IAFGLRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDE----MSGGQKQRVAIARAIVNKPEILLLDESLSALDLKLRTE 172
Cdd:cd03291  118 IIFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKE 197

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 488386109 173 MqYELRELQKRLGITFIFVTHDQEEaLALSDYIFVMKDGEIQQFGTPTDIYDE 225
Cdd:cd03291  198 I-FESCVCKLMANKTRILVTSKMEH-LKKADKILILHEGSSYFYGTFSELQSL 248
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
 22-213 2.15e-12

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 68.15  E-value: 2.15e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  22 NMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKL-PANKRRVNTVF-----QDYALF---P-HL 91
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALsTAQRLARGLVYlpedrQSSGLYldaPlAW 360

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  92 NV----YENIAFGLRLKKFSKqeIDKEVKEALKlVKLTGYEQRhIDEMSGGQKQRVAIARAIVNKPEILLLDESLSALDL 167
Cdd:PRK15439 361 NVcaltHNRRGFWIKPARENA--VLERYRRALN-IKFNHAEQA-ARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDV 436

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 488386109 168 KLRTEMQYELRELQKRlGITFIFVTHDQEEALALSDYIFVMKDGEI 213
Cdd:PRK15439 437 SARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEI 481
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
 2-213 2.24e-12

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 67.74  E-value: 2.24e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   2 ESLLSFKKVTKKFDD-TTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANKRR--- 77
Cdd:COG3845  255 EVVLEVENLSVRDDRgVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRrlg 334

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  78 VNTVFQD---YALFPHLNVYENIAFG-LRLKKFSK------QEIDKEVKEALKL--VKLTGYEQRhIDEMSGGQKQRVAI 145
Cdd:COG3845  335 VAYIPEDrlgRGLVPDMSVAENLILGrYRRPPFSRggfldrKAIRAFAEELIEEfdVRTPGPDTP-ARSLSGGNQQKVIL 413

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488386109 146 ARAIVNKPEILL-------LDesLSAldlklrTEMQYE-LRELQKRlGITFIFVTHDQEEALALSDYIFVMKDGEI 213
Cdd:COG3845  414 ARELSRDPKLLIaaqptrgLD--VGA------IEFIHQrLLELRDA-GAAVLLISEDLDEILALSDRIAVMYEGRI 480
PRK13541 PRK13541
cytochrome c biogenesis protein CcmA; Provisional
 37-166 7.13e-12

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184128 [Multi-domain]  Cd Length: 195  Bit Score: 63.74  E-value: 7.13e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  37 GPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPanKRRVNTVFQDYALFPHLNVYENIAFGLRLkkFSKQEIdkeVK 116
Cdd:PRK13541  33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIA--KPYCTYIGHNLGLKLEMTVFENLKFWSEI--YNSAET---LY 105

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 488386109 117 EALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDESLSALD 166
Cdd:PRK13541 106 AAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLS 155
sufC PRK09580
cysteine desulfurase ATPase component; Reviewed
 4-217 7.49e-12

cysteine desulfurase ATPase component; Reviewed


Pssm-ID: 181965 [Multi-domain]  Cd Length: 248  Bit Score: 64.81  E-value: 7.49e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   4 LLSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFE--QPNEGQIIYKNQSIEKLPANKRRVNTV 81
Cdd:PRK09580   1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRAGEGI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  82 FQDYALFPHLNVYENiAFGLR-----LKKFSKQE-IDK-----EVKEALKLVKL-TGYEQRHIDE-MSGGQKQRVAIARA 148
Cdd:PRK09580  81 FMAFQYPVEIPGVSN-QFFLQtalnaVRSYRGQEpLDRfdfqdLMEEKIALLKMpEDLLTRSVNVgFSGGEKKRNDILQM 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488386109 149 IVNKPEILLLDESLSALD---LKLRTEMQYELRElQKRlgiTFIFVTHDQEEALALS-DYIFVMKDGEIQQFG 217
Cdd:PRK09580 160 AVLEPELCILDESDSGLDidaLKIVADGVNSLRD-GKR---SFIIVTHYQRILDYIKpDYVHVLYQGRIVKSG 228
SapD COG4170
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
19-226 9.39e-12

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


Pssm-ID: 443330 [Multi-domain]  Cd Length: 331  Bit Score: 65.31  E-value: 9.39e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  19 ILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNegQII------YKNQSIEKLPANKRR------VNTVFQD-- 84
Cdd:COG4170   22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDN--WHVtadrfrWNGIDLLKLSPRERRkiigreIAMIFQEps 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  85 YALFPHLNVYENIAFGLRLKKFS------KQEIDKEVKEALKLVKLtgyeQRHID-------EMSGGQKQRVAIARAIVN 151
Cdd:COG4170  100 SCLDPSAKIGDQLIEAIPSWTFKgkwwqrFKWRKKRAIELLHRVGI----KDHKDimnsyphELTEGECQKVMIAMAIAN 175

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488386109 152 KPEILLLDESLSALDLKLRTEMQYELRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIYDEP 226
Cdd:COG4170  176 QPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSP 250
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
 20-213 1.00e-11

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 65.80  E-value: 1.00e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  20 LNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIE-KLPANKRRVNTVF--QDY---ALFPHLNV 93
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVtRSPQDGLANGIVYisEDRkrdGLVLGMSV 347

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  94 YENIAFgLRLKKFSK-------QEIDKEVKEALKL--VKLTGYEQRhIDEMSGGQKQRVAIARAIVNKPEILLLDESLSA 164
Cdd:PRK10762 348 KENMSL-TALRYFSRaggslkhADEQQAVSDFIRLfnIKTPSMEQA-IGLLSGGNQQKVAIARGLMTRPKVLILDEPTRG 425

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 488386109 165 LDLKLRTEMqYELRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEI 213
Cdd:PRK10762 426 VDVGAKKEI-YQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
 17-218 1.01e-11

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: 66.47  E-value: 1.01e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109    17 TTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNqsieklpankrRVNTVFQDYALFPHlNVYEN 96
Cdd:TIGR01271  439 TPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-----------RISFSPQTSWIMPG-TIKDN 506

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109    97 IAFGLRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDE----MSGGQKQRVAIARAIVNKPEILLLDESLSALDLKlrTE 172
Cdd:TIGR01271  507 IIFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFTHLDVV--TE 584

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 488386109   173 MQYELRELQKRL-GITFIFVThDQEEALALSDYIFVMKDGEIQQFGT 218
Cdd:TIGR01271  585 KEIFESCLCKLMsNKTRILVT-SKLEHLKKADKILLLHEGVCYFYGT 630
PvdE COG4615
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...
 24-213 1.16e-11

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: 65.97  E-value: 1.16e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  24 NLDIESG--YFytLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEK--LPANKRRVNTVFQDYALFPHLnvyeniaF 99
Cdd:COG4615  352 DLTIRRGelVF--IVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTAdnREAYRQLFSAVFSDFHLFDRL-------L 422

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 100 GLRlkkfsKQEIDKEVKEALKLVKL---TGYEQRHID--EMSGGQKQRVAIARAIV-NKPeILLLDEslSALDlklrtem 173
Cdd:COG4615  423 GLD-----GEADPARARELLERLELdhkVSVEDGRFSttDLSQGQRKRLALLVALLeDRP-ILVFDE--WAAD------- 487

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 488386109 174 Q--------YE--LRELqKRLGITFIFVTHDqEEALALSDYIFVMKDGEI 213
Cdd:COG4615  488 QdpefrrvfYTelLPEL-KARGKTVIAISHD-DRYFDLADRVLKMDYGKL 535
PTZ00243 PTZ00243
ABC transporter; Provisional
 19-221 1.51e-11

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 65.96  E-value: 1.51e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   19 ILNNMNLDIESGYFYTLLGPSGCGKTTILK-LIAGFEQpNEGQIiYKNQSIEKLPANKRRVNTVFQDYALFPHLNVYENI 97
Cdd:PTZ00243  675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQsLLSQFEI-SEGRV-WAERSIAYVPQQAWIMNATVRGNILFFDEEDAARL 752

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   98 AFGLRLkkfSKQEIDkevkealkLVKLTGYEQRHIDEM----SGGQKQRVAIARAIVNKPEILLLDESLSALDLKLRTEM 173
Cdd:PTZ00243  753 ADAVRV---SQLEAD--------LAQLGGGLETEIGEKgvnlSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERV 821

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 488386109  174 QYELreLQKRL-GITFIFVTHdQEEALALSDYIFVMKDGEIQQFGTPTD 221
Cdd:PTZ00243  822 VEEC--FLGALaGKTRVLATH-QVHVVPRADYVVALGDGRVEFSGSSAD 867
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
 19-218 3.40e-11

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 65.05  E-value: 3.40e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   19 ILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGF-EQPNEGQIIYKNQ-----SIEKLPANKRRVNTVF---------- 82
Cdd:PTZ00265 1183 IYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFyDLKNDHHIVFKNEhtndmTNEQDYQGDEEQNVGMknvnefsltk 1262

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   83 -----QDYALFPH----------------------------------LNVYENIAFGlrlkkfsKQEIDKE-VKEALKLV 122
Cdd:PTZ00265 1263 eggsgEDSTVFKNsgkilldgvdicdynlkdlrnlfsivsqepmlfnMSIYENIKFG-------KEDATREdVKRACKFA 1335

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  123 KLTGYEQR-----------HIDEMSGGQKQRVAIARAIVNKPEILLLDESLSALDLKLRTEMQYELRELQKRLGITFIFV 191
Cdd:PTZ00265 1336 AIDEFIESlpnkydtnvgpYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITI 1415

                         250       260       270
                  ....*....|....*....|....*....|..
gi 488386109  192 THdQEEALALSDYIFVMKDGE-----IQQFGT 218
Cdd:PTZ00265 1416 AH-RIASIKRSDKIVVFNNPDrtgsfVQAHGT 1446
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
 7-166 4.19e-11

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 63.98  E-value: 4.19e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   7 FKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEG--------QIIYKNQSIEKLPANKrrv 78
Cdd:PRK11819 327 AENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGtikigetvKLAYVDQSRDALDPNK--- 403

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  79 ntvfqdyalfphlNVYENIAFGLRLKKFSKQEIDKEvkealklvkltGY----------EQRHIDEMSGGQKQRVAIARA 148
Cdd:PRK11819 404 -------------TVWEEISGGLDIIKVGNREIPSR-----------AYvgrfnfkggdQQKKVGVLSGGERNRLHLAKT 459

                        170
                 ....*....|....*...
gi 488386109 149 IVNKPEILLLDESLSALD 166
Cdd:PRK11819 460 LKQGGNVLLLDEPTNDLD 477
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
 6-194 4.23e-11

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 63.98  E-value: 4.23e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   6 SFKKVTKKFD-DTTILNNMNLdiesGYFYT----LLGPSGCGKTTILKLIAGFEQPNEGqiiyknqsiEKLPANKRRVNT 80
Cdd:PRK11819   8 TMNRVSKVVPpKKQILKDISL----SFFPGakigVLGLNGAGKSTLLRIMAGVDKEFEG---------EARPAPGIKVGY 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  81 VFQDYALFPHLNVYENIAFGLRLKKFSKQEIDkEVKEAL--------KLVKLTGYEQRHID-----------EM------ 135
Cdd:PRK11819  75 LPQEPQLDPEKTVRENVEEGVAEVKAALDRFN-EIYAAYaepdadfdALAAEQGELQEIIDaadawdldsqlEIamdalr 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488386109 136 -----------SGGQKQRVAIARAIVNKPEILLLDESLSALD------LKlrtemqyelRELQKRLGiTFIFVTHD 194
Cdd:PRK11819 154 cppwdakvtklSGGERRRVALCRLLLEKPDMLLLDEPTNHLDaesvawLE---------QFLHDYPG-TVVAVTHD 219
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
 35-227 4.28e-11

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 62.26  E-value: 4.28e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  35 LLGPSGCGKTTILKLIAGFeQPNEGQIIYKNQSIEKLPANK---RRVNTVFQDYALFpHLNVYENIAFGLRlKKFSKQEI 111
Cdd:PRK03695  27 LVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAElarHRAYLSQQQTPPF-AMPVFQYLTLHQP-DKTRTEAV 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 112 DKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAI-----VNKPE--ILLLDESLSALDLKLRTEMQYELRELQkRL 184
Cdd:PRK03695 104 ASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqvwpDINPAgqLLLLDEPMNSLDVAQQAALDRLLSELC-QQ 182

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 488386109 185 GITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIYDEPV 227
Cdd:PRK03695 183 GIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPEN 225
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 29-212 1.04e-10

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 59.31  E-value: 1.04e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109    29 SGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANKRRVNTVFQDYALfphlnvyeniafglrlkkfsk 108
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKA--------------------- 59

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   109 qeidkevkealklvkltgyeqrhidEMSGGQKQRVAIARAIVNKPEILLLDESLSALD-----LKLRTEMQYELRELQKR 183
Cdd:smart00382  60 -------------------------SGSGELRLRLALALARKLKPDVLILDEITSLLDaeqeaLLLLLEELRLLLLLKSE 114

                          170       180       190
                   ....*....|....*....|....*....|....
gi 488386109   184 LGITFIFVTHDQE-----EALALSDYIFVMKDGE 212
Cdd:smart00382 115 KNLTVILTTNDEKdlgpaLLRRRFDRRIVLLLIL 148
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
 20-214 1.11e-10

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: 62.53  E-value: 1.11e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   20 LNNMNLDIESGYFYTLLGPSGCGKTTILKLIAG-FEQPNEGQIIYKNQSIE-KLPANKRR--VNTVFQD---YALFPHLN 92
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGaYPGKFEGNVFINGKPVDiRNPAQAIRagIAMVPEDrkrHGIVPILG 355

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   93 VYENIAFGLrLKKFSKQ-EIDKE-----VKEALKLVKL-TGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDESLSAL 165
Cdd:TIGR02633 356 VGKNITLSV-LKSFCFKmRIDAAaelqiIGSAIQRLKVkTASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGV 434

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 488386109  166 DLKLRTEMqYELRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQ 214
Cdd:TIGR02633 435 DVGAKYEI-YKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLK 482
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
 22-226 1.34e-10

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 60.87  E-value: 1.34e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  22 NMNLDIESGYFYTLLGPSGCGKT-TILKLI----AGFEQPNeGQIIYKNQSIEKLPANKRRVNTVFQDyalfPH--LNVY 94
Cdd:PRK10418  21 GVSLTLQRGRVLALVGGSGSGKSlTCAAALgilpAGVRQTA-GRVLLDGKPVAPCALRGRKIATIMQN----PRsaFNPL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  95 ENIAFGLR--LKKFSKQEIDKEVKEALKLVKLTGYE---QRHIDEMSGGQKQRVAIARAIVNKPEILLLDESLSALDLKL 169
Cdd:PRK10418  96 HTMHTHARetCLALGKPADDATLTAALEAVGLENAArvlKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVA 175

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 488386109 170 RTEMQYELRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIYDEP 226
Cdd:PRK10418 176 QARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAP 232
PLN03073 PLN03073
ABC transporter F family; Provisional
 18-221 2.50e-10

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 61.80  E-value: 2.50e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  18 TILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIiYKNQSIEKLPANKRRVNTVfqDYALFPHLnvyeni 97
Cdd:PLN03073 523 LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV-FRSAKVRMAVFSQHHVDGL--DLSSNPLL------ 593

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  98 afglRLKKFSKQEIDKEVKEALKLVKLTG-YEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDESLSALDLKLRTEMQYE 176
Cdd:PLN03073 594 ----YMMRCFPGVPEQKLRAHLGSFGVTGnLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQG 669

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 488386109 177 LRELQKrlGItfIFVTHDQEEALALSDYIFVMKDGEIQQF-GTPTD 221
Cdd:PLN03073 670 LVLFQG--GV--LMVSHDEHLISGSVDELWVVSEGKVTPFhGTFHD 711
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
8-213 2.95e-10

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 60.90  E-value: 2.95e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   8 KKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTiLKLIAGFEQPNEGQIIYKnqsIEKLPANKRRVNTVFQDY-- 85
Cdd:NF000106  17 RGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**R-GALPAHV*GPDAGRRPWR---F*TWCANRRALRRTIG*Hrp 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  86 ---ALFPHLNVYENIAFGLRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDESL 162
Cdd:NF000106  93 vr*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPT 172

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 488386109 163 SALDLKLRTEMQYELRELQkRLGITFIFVTHDQEEALALSDYIFVMKDGEI 213
Cdd:NF000106 173 TGLDPRTRNEVWDEVRSMV-RDGATVLLTTQYMEEAEQLAHELTVIDRGRV 222
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
 2-198 5.02e-10

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 60.80  E-value: 5.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   2 ESLLSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGfEQPnEGqiiYKNQ---------SIEKLP 72
Cdd:PRK10938 258 EPRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DHP-QG---YSNDltlfgrrrgSGETIW 332

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  73 ANKR-------------RVNTVFQDYAL---FPHLNVYEniAFGLRLKKFSKQEIDKevkeaLKLVKLTGYEQRHidEMS 136
Cdd:PRK10938 333 DIKKhigyvssslhldyRVSTSVRNVILsgfFDSIGIYQ--AVSDRQQKLAQQWLDI-----LGIDKRTADAPFH--SLS 403

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488386109 137 GGQKQRVAIARAIVNKPEILLLDESLSALD-LKlrtemqyelRELQKRL-------GIT-FIFVTHDQEEA 198
Cdd:PRK10938 404 WGQQRLALIVRALVKHPTLLILDEPLQGLDpLN---------RQLVRRFvdvliseGETqLLFVSHHAEDA 465
ABCG_PDR_domain2 cd03232
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...
 3-166 9.49e-10

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: 57.64  E-value: 9.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   3 SLLSFK----KVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEqpnEGQIIYKNQSIEKLPANK--- 75
Cdd:cd03232    2 SVLTWKnlnyTVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRK---TAGVITGEILINGRPLDKnfq 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  76 RRVNTVFQDYALFPHLNVYENIAFGLRLKkfskqeidkevkealklvkltgyeqrhidEMSGGQKQRVAIARAIVNKPEI 155
Cdd:cd03232   79 RSTGYVEQQDVHSPNLTVREALRFSALLR-----------------------------GLSVEQRKRLTIGVELAAKPSI 129

                        170
                 ....*....|.
gi 488386109 156 LLLDESLSALD 166
Cdd:cd03232  130 LFLDEPTSGLD 140
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
24-213 1.31e-09

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 59.54  E-value: 1.31e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  24 NLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIE-KLPANKRRVNTVF------QDyALFPHLNVYEN 96
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDiRSPRDAIRAGIMLcpedrkAE-GIIPVHSVADN 351

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  97 IAFGLRlKKFS--------KQEID--KEVKEALKlVKLTGYEQRhIDEMSGGQKQRVAIARAIVNKPEILLLDESLSALD 166
Cdd:PRK11288 352 INISAR-RHHLragclinnRWEAEnaDRFIRSLN-IKTPSREQL-IMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGID 428

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 488386109 167 LKLRTEMQYELRELQKRlGITFIFVTHDQEEALALSDYIFVMKDGEI 213
Cdd:PRK11288 429 VGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRI 474
PRK13546 PRK13546
teichoic acids export ABC transporter ATP-binding subunit TagH;
20-230 1.83e-09

teichoic acids export ABC transporter ATP-binding subunit TagH;


Pssm-ID: 184131 [Multi-domain]  Cd Length: 264  Bit Score: 57.90  E-value: 1.83e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  20 LNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQsieklpankrrVNTVFQDYALFPHLNVYENIAF 99
Cdd:PRK13546  40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE-----------VSVIAISAGLSGQLTGIENIEF 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 100 GLRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDESLSALDlklRTEMQYELRE 179
Cdd:PRK13546 109 KMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGD---QTFAQKCLDK 185

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 488386109 180 LQ--KRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDI---YDEPVNRF 230
Cdd:PRK13546 186 IYefKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVlpkYEAFLNDF 241
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
 20-213 2.16e-09

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 58.59  E-value: 2.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  20 LNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPANK------------RRVNTVFQDY-- 85
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEainhgfalvteeRRSTGIYAYLdi 343

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  86 ---ALFPHLNVYENiAFGL----RLKKFSKQEIDkevkeALKlVKLTGYeQRHIDEMSGGQKQRVAIARAIVNKPEILLL 158
Cdd:PRK10982 344 gfnSLISNIRNYKN-KVGLldnsRMKSDTQWVID-----SMR-VKTPGH-RTQIGSLSGGNQQKVIIGRWLLTQPEILML 415

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 488386109 159 DESLSALDLKLRTEMQYELRELQKR-LGItfIFVTHDQEEALALSDYIFVMKDGEI 213
Cdd:PRK10982 416 DEPTRGIDVGAKFEIYQLIAELAKKdKGI--IIISSEMPELLGITDRILVMSNGLV 469
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
 85-214 2.25e-09

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 58.79  E-value: 2.25e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  85 YALFPHLNVYENIAFGLrLKKFSK----------QEIDKEVKEaLKlVKLTGYEQRhIDEMSGGQKQRVAIARAIVNKPE 154
Cdd:PRK13549 350 DGIVPVMGVGKNITLAA-LDRFTGgsriddaaelKTILESIQR-LK-VKTASPELA-IARLSGGNQQKAVLAKCLLLNPK 425

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488386109 155 ILLLDESLSALDLKLRTEMqYEL-RELQKRlGITFIFVTHDQEEALALSDYIFVMKDGEIQ 214
Cdd:PRK13549 426 ILILDEPTRGIDVGAKYEI-YKLiNQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGKLK 484
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
 8-216 5.41e-09

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 57.65  E-value: 5.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   8 KKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIiyknqsieklpankrRVNT-----VF 82
Cdd:PRK11147 323 ENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI---------------HCGTklevaYF 387

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  83 QDY--ALFPHLNVYENIAFGlrlkkfsKQEI-----DKEV-----------KEALKLVKltgyeqrhidEMSGGQKQRVA 144
Cdd:PRK11147 388 DQHraELDPEKTVMDNLAEG-------KQEVmvngrPRHVlgylqdflfhpKRAMTPVK----------ALSGGERNRLL 450

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488386109 145 IARAIVNKPEILLLDESLSALD---LKLRTEMqyeLRELQKrlgiTFIFVTHDQE--EALALSDYIFvMKDGEIQQF 216
Cdd:PRK11147 451 LARLFLKPSNLLILDEPTNDLDvetLELLEEL---LDSYQG----TVLLVSHDRQfvDNTVTECWIF-EGNGKIGRY 519
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
 26-232 1.52e-08

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


Pssm-ID: 213189 [Multi-domain]  Cd Length: 177  Bit Score: 53.73  E-value: 1.52e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  26 DIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLPankrrvntvfqdyalfphlnvyeniafglrlkk 105
Cdd:cd03222   21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKP--------------------------------- 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 106 fskQEIDkevkealklvkltgyeqrhideMSGGQKQRVAIARAIVNKPEILLLDESLSALDLKLRTEMQYELRELQKRLG 185
Cdd:cd03222   68 ---QYID----------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGK 122

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 488386109 186 ITFIFVTHDQEEALALSDYIFVMkDGEIQQFGT--PTDIYDEPVNRFVA 232
Cdd:cd03222  123 KTALVVEHDLAVLDYLSDRIHVF-EGEPGVYGIasQPKGTREGINRFLR 170
tagH PRK13545
teichoic acids export protein ATP-binding subunit; Provisional
 20-225 2.00e-08

teichoic acids export protein ATP-binding subunit; Provisional


Pssm-ID: 184130 [Multi-domain]  Cd Length: 549  Bit Score: 55.67  E-value: 2.00e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  20 LNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSieKLPANKRRVNTvfqdyalfpHLNVYENIAF 99
Cdd:PRK13545  40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSA--ALIAISSGLNG---------QLTGIENIEL 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 100 GLRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVNKPEILLLDESLSALDLKLRTEMQYELRE 179
Cdd:PRK13545 109 KGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNE 188

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 488386109 180 LqKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIYDE 225
Cdd:PRK13545 189 F-KEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDH 233
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
 13-166 4.71e-08

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


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 55.11  E-value: 4.71e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109    13 KFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAgfEQPNEGQIIYKNQSIEKLPANK---RRVNTVFQDYALFP 89
Cdd:TIGR00956  772 KKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLA--ERVTTGVITGGDRLVNGRPLDSsfqRSIGYVQQQDLHLP 849

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109    90 HLNVYENIAFGLRL---KKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGG----QKQRVAIARAIVNKPEILL-LDES 161
Cdd:TIGR00956  850 TSTVRESLRFSAYLrqpKSVSKSEKMEYVEEVIKLLEMESYADAVVGVPGEGlnveQRKRLTIGVELVAKPKLLLfLDEP 929


                   ....*
gi 488386109   162 LSALD 166
Cdd:TIGR00956  930 TSGLD 934
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
 37-212 1.07e-07

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: 51.84  E-value: 1.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  37 GPSGCGKTTILKLI--AGF-EQPNEGQIIYKNQSIEKLPANKRRVNTVFQ-----DYALFPHLNVYENIAFglrlkkfSK 108
Cdd:cd03240   29 GQNGAGKTTIIEALkyALTgELPPNSKGGAHDPKLIREGEVRAQVKLAFEnangkKYTITRSLAILENVIF-------CH 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 109 QEidkevkEALKLVkltgyeQRHIDEMSGGQKQ------RVAIARAIVNKPEILLLDESLSALDLKLRTEMQYELRELQK 182
Cdd:cd03240  102 QG------ESNWPL------LDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEESLAEIIEERK 169

                        170       180       190
                 ....*....|....*....|....*....|.
gi 488386109 183 RLGI-TFIFVTHDQEEALALSDYIFVMKDGE 212
Cdd:cd03240  170 SQKNfQLIVITHDEELVDAADHIYRVEKDGR 200
ABCC_SUR2 cd03288
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...
 19-222 4.69e-07

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


Pssm-ID: 213255 [Multi-domain]  Cd Length: 257  Bit Score: 50.68  E-value: 4.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  19 ILNNMNLDIESGYFYTLLGPSGCGKTTILklIAGFEQPN--EGQIIYKNQSIEKLPAN--KRRVNTVFQDYALFPHlnvy 94
Cdd:cd03288   36 VLKHVKAYIKPGQKVGICGRTGSGKSSLS--LAFFRMVDifDGKIVIDGIDISKLPLHtlRSRLSIILQDPILFSG---- 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  95 eNIAFGLRLKKfskQEIDKEVKEALKLVKLTGYEQR---HIDEM--------SGGQKQRVAIARAIVNKPEILLLDESLS 163
Cdd:cd03288  110 -SIRFNLDPEC---KCTDDRLWEALEIAQLKNMVKSlpgGLDAVvteggenfSVGQRQLFCLARAFVRKSSILIMDEATA 185

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 164 ALDLKLRTEMQ-YELRELQKRLGITFIFVTHDQEEAlalsDYIFVMKDGEIQQFGTPTDI 222
Cdd:cd03288  186 SIDMATENILQkVVMTAFADRTVVTIAHRVSTILDA----DLVLVLSRGILVECDTPENL 241
PLN03232 PLN03232
ABC transporter C family member; Provisional
 35-230 8.09e-07

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 51.13  E-value: 8.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   35 LLGPSGCGKTTILKLIAGFEQPNEGQIIYKNQSIEKLP-ANKRRVntvfqdYALFPHLNVYENIAFGLRLKKFSKQEiDK 113
Cdd:PLN03232 1267 VVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGlTDLRRV------LSIIPQSPVLFSGTVRFNIDPFSEHN-DA 1339

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  114 EVKEALKLVKLTGYEQRHI-----------DEMSGGQKQRVAIARAIVNKPEILLLDESLSALDLKLRTEMQYELRELQK 182
Cdd:PLN03232 1340 DLWEALERAHIKDVIDRNPfgldaevseggENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFK 1419

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 488386109  183 rlGITFIFVTHdQEEALALSDYIFVMKDGEIQQFGTPTDIYDEPVNRF 230
Cdd:PLN03232 1420 --SCTMLVIAH-RLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAF 1464
TOBE_2 pfam08402
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the ...
 273-342 8.68e-07

TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the C-terminal strand of each domain is supplied by the partner. Probably involved in the recognition of small ligands such as molybdenum and sulphate. Found in ABC transporters immediately after the ATPase domain. In this family a strong RPE motif is found at the presumed N-terminus of the domain.


Pssm-ID: 462465 [Multi-domain]  Cd Length: 73  Bit Score: 46.07  E-value: 8.68e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488386109  273 VVIRPEDISLVEsTQGLFTATVDSMLFRGVHYEICCIDEKGYEWVIQSTKKT----TIGSQVGLFFEPEAIHIM 342
Cdd:pfam08402   1 LAIRPEKIRLAA-AANGLSGTVTDVEYLGDHTRYHVELAGGEELVVRVPNAHarppAPGDRVGLGWDPEDAHVL 73
PRK15093 PRK15093
peptide ABC transporter ATP-binding protein SapD;
23-226 8.95e-07

peptide ABC transporter ATP-binding protein SapD;


Pssm-ID: 185049 [Multi-domain]  Cd Length: 330  Bit Score: 50.19  E-value: 8.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  23 MNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPN----EGQIIYKNQSIEKLPANKRR------VNTVFQDyalfPH-- 90
Cdd:PRK15093  26 VSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNwrvtADRMRFDDIDLLRLSPRERRklvghnVSMIFQE----PQsc 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  91 LNVYENIAF-------GLRLKKFSKQEIDKEVKEALKLVKLTGYEQrHID-------EMSGGQKQRVAIARAIVNKPEIL 156
Cdd:PRK15093 102 LDPSERVGRqlmqnipGWTYKGRWWQRFGWRKRRAIELLHRVGIKD-HKDamrsfpyELTEGECQKVMIAIALANQPRLL 180

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109 157 LLDESLSALDLKLRTEMQYELRELQKRLGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDIYDEP 226
Cdd:PRK15093 181 IADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTTP 250
PLN03140 PLN03140
ABC transporter G family member; Provisional
 30-166 2.48e-06

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 49.46  E-value: 2.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   30 GYFYTLLGPSGCGKTTILKLIAGFEQpneGQIIYKNQSIEKLPANK----RRVNTVFQDYALFPHLNVYENIAFG--LRL 103
Cdd:PLN03140  906 GVLTALMGVSGAGKTTLMDVLAGRKT---GGYIEGDIRISGFPKKQetfaRISGYCEQNDIHSPQVTVRESLIYSafLRL 982

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488386109  104 -KKFSKQEIDKEVKEALKLVKLTGYEQR-----HIDEMSGGQKQRVAIARAIVNKPEILLLDESLSALD 166
Cdd:PLN03140  983 pKEVSKEEKMMFVDEVMELVELDNLKDAivglpGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 1051
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
 3-222 7.93e-06

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 47.70  E-value: 7.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   3 SLLSFKKVTKKFDDTTILNNMNLDIESGYFYTLLGPSGCGKTTILKLIAGFEQPNEGQiiYKNQ-------SIEKLpanK 75
Cdd:PRK10938   2 SSLQISQGTFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGE--RQSQfshitrlSFEQL---Q 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  76 RRVNTVFQDyalfphlNVYENIA-----FGlrlkKFSKQEIDKEVKEA---LKLVKLTGYE---QRHIDEMSGGQKQRVA 144
Cdd:PRK10938  77 KLVSDEWQR-------NNTDMLSpgeddTG----RTTAEIIQDEVKDParcEQLAQQFGITallDRRFKYLSTGETRKTL 145

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488386109 145 IARAIVNKPEILLLDESLSALDLKLRTEMQYELRELQKRlGITFIFVTHDQEEALALSDYIFVMKDGEIQQFGTPTDI 222
Cdd:PRK10938 146 LCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEI 222
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
 5-216 1.15e-05

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: 46.39  E-value: 1.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   5 LSFKKVTKKFDD--TTILNNMNLDIESGYFYTLLGPSGCGKTTI----LKLIAgfeqpNEGQIIYKNQSIEKLPANKRR- 77
Cdd:cd03289    3 MTVKDLTAKYTEggNAVLENISFSISPGQRVGLLGRTGSGKSTLlsafLRLLN-----TEGDIQIDGVSWNSVPLQKWRk 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  78 -VNTVFQDYALFP-----HLNVYEniafglrlkKFSKQEIDKEVKE-ALKLV--KLTGYEQRHIDE----MSGGQKQRVA 144
Cdd:cd03289   78 aFGVIPQKVFIFSgtfrkNLDPYG---------KWSDEEIWKVAEEvGLKSVieQFPGQLDFVLVDggcvLSHGHKQLMC 148

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488386109 145 IARAIVNKPEILLLDESLSALDLKLRTEMQYELRelQKRLGITFIFVTHDQEEALALSDYIfVMKDGEIQQF 216
Cdd:cd03289  149 LARSVLSKAKILLLDEPSAHLDPITYQVIRKTLK--QAFADCTVILSEHRIEAMLECQRFL-VIEENKVRQY 217
PLN03073 PLN03073
ABC transporter F family; Provisional
 19-196 2.23e-05

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 46.39  E-value: 2.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  19 ILNNMNLDIESGYFYTLLGPSGCGKTTILKLIA-----GFeqPNEGQIIYKNQS----------------IEK------- 70
Cdd:PLN03073 192 LIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAmhaidGI--PKNCQILHVEQEvvgddttalqcvlntdIERtqlleee 269

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  71 --LPANKRRVN--TVFQDYALfPHLNVYENIAFGLRLKKFSK--QEIDKEVKEALKLVKLTG------YEQRHIDEMSGG 138
Cdd:PLN03073 270 aqLVAQQRELEfeTETGKGKG-ANKDGVDKDAVSQRLEEIYKrlELIDAYTAEARAASILAGlsftpeMQVKATKTFSGG 348

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 488386109 139 QKQRVAIARAIVNKPEILLLDESLSALDLKLRTEMQYELRELQKrlgiTFIFVTHDQE 196
Cdd:PLN03073 349 WRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPK----TFIVVSHARE 402
PLN03130 PLN03130
ABC transporter C family member; Provisional
 136-219 3.78e-05

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 45.88  E-value: 3.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  136 SGGQKQRVAIARAIVNKPEILLLDESLSALDLKLRTEMQYELRELQKrlGITFIFVTHdQEEALALSDYIFVMKDGEIQQ 215
Cdd:PLN03130 1376 SVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFK--SCTMLIIAH-RLNTIIDCDRILVLDAGRVVE 1452


                  ....
gi 488386109  216 FGTP 219
Cdd:PLN03130 1453 FDTP 1456
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
 75-222 1.04e-04

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


Pssm-ID: 273184 [Multi-domain]  Cd Length: 925  Bit Score: 44.23  E-value: 1.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109   75 KRRVNTVF---QDYALFPHLNVYENIAF--GLRLKKFSKQ---EIDKEVKEALKLVKLTGYE----QRHIDEMSGGQKQR 142
Cdd:TIGR00630 417 KPEALAVTvggKSIADVSELSIREAHEFfnQLTLTPEEKKiaeEVLKEIRERLGFLIDVGLDylslSRAAGTLSGGEAQR 496

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  143 VAIARAI------VnkpeILLLDESLSALDLKLRTEMQYELRELQKrLGITFIFVTHDqEEALALSDYIFVM------KD 210
Cdd:TIGR00630 497 IRLATQIgsgltgV----LYVLDEPSIGLHQRDNRRLINTLKRLRD-LGNTLIVVEHD-EDTIRAADYVIDIgpgageHG 570

                         170
                  ....*....|..
gi 488386109  211 GEIQQFGTPTDI 222
Cdd:TIGR00630 571 GEVVASGTPEEI 582
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 18-138 3.08e-03

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 39.30  E-value: 3.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  18 TILNNMnldIESGYFYTLL--GPSGCGKTTILKLIAG-----FEQ---PNEG-----QIIykNQSIEKLPANKR------ 76
Cdd:PRK13342  25 KPLRRM---IEAGRLSSMIlwGPPGTGKTTLARIIAGatdapFEAlsaVTSGvkdlrEVI--EEARQRRSAGRRtilfid 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  77 ---RVNTVFQDyALFPHLnvyEN---IAFG--------------------LRLKKFSKQEIDKEVKEALK-----LVKLT 125
Cdd:PRK13342 100 eihRFNKAQQD-ALLPHV---EDgtiTLIGattenpsfevnpallsraqvFELKPLSEEDIEQLLKRALEdkergLVELD 175

                        170
                 ....*....|...
gi 488386109 126 GYEQRHIDEMSGG 138
Cdd:PRK13342 176 DEALDALARLANG 188
COG1106 COG1106
ATPase/GTPase, AAA15 family [General function prediction only];
91-210 3.76e-03

ATPase/GTPase, AAA15 family [General function prediction only];


Pssm-ID: 440723 [Multi-domain]  Cd Length: 330  Bit Score: 38.87  E-value: 3.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386109  91 LNVYENIAFGLRLKKFSKQEIDKEVKEALKLVKLTGYEQRHIDEMSGGQKQRVAIARAIVN---KPEILLLDEslsaLDL 167
Cdd:COG1106  159 LELLKIADPGIEDIEVEEEEIEDLVERKLIFKHKGGNVPLPLSEESDGTKRLLALAGALLDalaKGGVLLIDE----IEA 234

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 488386109 168 KLRTEMQYEL----RELQKRLGITFIFVTHDQE------EALALSDYIFVMKD 210
Cdd:COG1106  235 SLHPSLLRKLlklfLDLANKNNAQLIFTTHSTElldaflELLRRDQIWFVEKD 287
 
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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